| AEQF01000045.1_27 |
96.584 |
0.0 |
rfaC |
VF0078 |
LOS |
Immune modulation |
VFC0258 |
Biosynthesis pathway of LOS is producing a branched oligosaccharide attached to a lipid A via two 3-deoxy-D-manno-2-octulosonic acid (KDO) molecules. The rfaC gene product adds the first heptose (Hep I) to KDO. The rfaF gene product adds the second Hep onto Hep I and is required for alpha-chain elongation. The lgtF gene product adds the first Glc of the alpha-chain. Genes lgtA, lgtB, lgtE are responsible for the synthesis of different alpha chains. lgtG is required for addition of the fist Glc of the beta chain; lgtA, lgtC, lgtG are subject to phase variation of expression mediated by homopolymeric tracts within their coding regions |
(rfaC) lipopolysaccharide heptosyltransferase I [LOS (VF0078) - Immune modulation (VFC0258)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000045.1_45 |
96.69 |
0.0 |
kdtA/waaA |
VF0078 |
LOS |
Immune modulation |
VFC0258 |
Biosynthesis pathway of LOS is producing a branched oligosaccharide attached to a lipid A via two 3-deoxy-D-manno-2-octulosonic acid (KDO) molecules. The rfaC gene product adds the first heptose (Hep I) to KDO. The rfaF gene product adds the second Hep onto Hep I and is required for alpha-chain elongation. The lgtF gene product adds the first Glc of the alpha-chain. Genes lgtA, lgtB, lgtE are responsible for the synthesis of different alpha chains. lgtG is required for addition of the fist Glc of the beta chain; lgtA, lgtC, lgtG are subject to phase variation of expression mediated by homopolymeric tracts within their coding regions |
(kdtA/waaA) lipid IV(A) 3-deoxy-D-manno-octulosonic acid transferase [LOS (VF0078) - Immune modulation (VFC0258)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000044.1_17 |
67.818 |
0.0 |
lpt6 |
VF0044 |
LOS |
Immune modulation |
VFC0258 |
Lic1A (phosphorylcholine (ChoP) kinase) 5'-CAAT-3' within the 5'-end of its coding sequence; lic2A, also referred to as lexA, variation in the number of 5'-CAAT-3' repeats has been shown to correlate directly with phase variation of the Gal-alpha(1-4)beta-Gal LPS structure; But lgtC (glycosyltransferase), another phase-variable gene, ultimately dictates whether this structure is synthesized. lic3A encode a sialyl transferase which directs the substitution of LPS with sialic acid. |
(lpt6) phosphoethanolamine (Petn) transferase [LOS (VF0044) - Immune modulation (VFC0258)] [Haemophilus influenzae Rd KW20] |
Haemophilus influenzae |
| AEQF01000044.1_24 |
60.556 |
3.79E-139 |
porB |
VF0081 |
Porin |
Invasion |
VFC0083 |
N.meningitidis produces two porins, PorA and PorB, N.gonorrhoeae expresses only one porin, PorB |
(porB) major outer membrane protein PIB [Porin (VF0081) - Invasion (VFC0083)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000042.1_17 |
76.435 |
3.48E-173 |
hpuA |
VF0049 |
HpuAB |
Nutritional/Metabolic factor |
VFC0272 |
Expression of HpuAB undergoes phase variation due to slip-strand mispairing of poly(G) tracts within the hpuA gene |
(hpuA) haemoglobin-haptoglobin-utilization protein [HpuAB (VF0049) - Nutritional/Metabolic factor (VFC0272)] [Neisseria meningitidis Z2491] |
Neisseria meningitidis |
| AEQF01000042.1_18 |
94.321 |
0.0 |
hpuB |
VF0049 |
HpuAB |
Nutritional/Metabolic factor |
VFC0272 |
Expression of HpuAB undergoes phase variation due to slip-strand mispairing of poly(G) tracts within the hpuA gene |
(hpuB) haemoglobin-haptoglobin-utilization protein [HpuAB (VF0049) - Nutritional/Metabolic factor (VFC0272)] [Neisseria meningitidis Z2491] |
Neisseria meningitidis |
| AEQF01000042.1_20 |
72.433 |
0.0 |
htpB |
VF0159 |
Hsp60 |
Adherence |
VFC0001 |
|
(htpB) Hsp60, 60K heat shock protein HtpB [Hsp60 (VF0159) - Adherence (VFC0001)] [Legionella pneumophila subsp. pneumophila str. Philadelphia 1] |
Legionella pneumophila |
| AEQF01000042.1_29 |
76.647 |
6.09E-98 |
luxS |
VF0406 |
AI-2 |
Biofilm |
VFC0271 |
AI-2 is produced and detected by a wide variety of bacteria and is presumed to facilitate interspecies communications. |
(luxS) S-ribosylhomocysteinase [AI-2 (VF0406) - Biofilm (VFC0271)] [Vibrio cholerae O1 biovar El Tor str. N16961] |
Vibrio cholerae |
| AEQF01000040.1_13 |
99.73 |
0.0 |
pilM |
VF0075 |
Type IV pili |
Adherence |
VFC0001 |
One or two different loci are used for the expression of the major pilin encoding gene (pilE), whereas various silent genes (pilS) are spread throughout the chromosome. Recombination between pilS and pilE copies leads to changes in the pilin coding sequence and subsequently to the expression of antigenically different pili. Mutations affecting the length of the homopolymeric G-run located in the region encoding the SP of PilC results in on/off changes in piliation |
(pilM) type IV pilus inner membrane platform protein PilM [Type IV pili (VF0075) - Adherence (VFC0001)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000040.1_14 |
99.497 |
6.12E-147 |
pilN |
VF0075 |
Type IV pili |
Adherence |
VFC0001 |
One or two different loci are used for the expression of the major pilin encoding gene (pilE), whereas various silent genes (pilS) are spread throughout the chromosome. Recombination between pilS and pilE copies leads to changes in the pilin coding sequence and subsequently to the expression of antigenically different pili. Mutations affecting the length of the homopolymeric G-run located in the region encoding the SP of PilC results in on/off changes in piliation |
(pilN) type IV pilus inner membrane platform protein PilN [Type IV pili (VF0075) - Adherence (VFC0001)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000040.1_15 |
100.0 |
3.63E-157 |
pilO |
VF0075 |
Type IV pili |
Adherence |
VFC0001 |
One or two different loci are used for the expression of the major pilin encoding gene (pilE), whereas various silent genes (pilS) are spread throughout the chromosome. Recombination between pilS and pilE copies leads to changes in the pilin coding sequence and subsequently to the expression of antigenically different pili. Mutations affecting the length of the homopolymeric G-run located in the region encoding the SP of PilC results in on/off changes in piliation |
(pilO) type IV pilus inner membrane platform protein PilO [Type IV pili (VF0075) - Adherence (VFC0001)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000040.1_16 |
100.0 |
1.68E-136 |
pilP |
VF0075 |
Type IV pili |
Adherence |
VFC0001 |
One or two different loci are used for the expression of the major pilin encoding gene (pilE), whereas various silent genes (pilS) are spread throughout the chromosome. Recombination between pilS and pilE copies leads to changes in the pilin coding sequence and subsequently to the expression of antigenically different pili. Mutations affecting the length of the homopolymeric G-run located in the region encoding the SP of PilC results in on/off changes in piliation |
(pilP) type IV pilus biogenesis protein PilP [Type IV pili (VF0075) - Adherence (VFC0001)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000040.1_17 |
99.48 |
0.0 |
pilQ |
VF0075 |
Type IV pili |
Adherence |
VFC0001 |
One or two different loci are used for the expression of the major pilin encoding gene (pilE), whereas various silent genes (pilS) are spread throughout the chromosome. Recombination between pilS and pilE copies leads to changes in the pilin coding sequence and subsequently to the expression of antigenically different pili. Mutations affecting the length of the homopolymeric G-run located in the region encoding the SP of PilC results in on/off changes in piliation |
(pilQ) type IV pilus secretin protein PilQ [Type IV pili (VF0075) - Adherence (VFC0001)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000040.1_58 |
68.447 |
0.0 |
pilC |
VF0075 |
Type IV pili |
Adherence |
VFC0001 |
One or two different loci are used for the expression of the major pilin encoding gene (pilE), whereas various silent genes (pilS) are spread throughout the chromosome. Recombination between pilS and pilE copies leads to changes in the pilin coding sequence and subsequently to the expression of antigenically different pili. Mutations affecting the length of the homopolymeric G-run located in the region encoding the SP of PilC results in on/off changes in piliation |
(pilC) pilus assembly protein [Type IV pili (VF0075) - Adherence (VFC0001)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000040.1_78 |
93.796 |
0.0 |
fHbp |
VF0452 |
FHbp |
Immune modulation |
VFC0258 |
|
(fHbp) factor H binding protein [FHbp (VF0452) - Immune modulation (VFC0258)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000040.1_124 |
65.702 |
9.13E-110 |
flmH |
VF0473 |
Polar flagella |
Motility |
VFC0204 |
Types of bacterial movement: swimming, swarming, gliding, twitching and sliding. Only swimming and swarming are correlated with the presence of flagella. Swimming is an individual endeavour, while swarming is the movement of a group of bacteria; constitutively expressed for motility in liquid environments |
(flmH) short chain dehydrogenase/reductase family oxidoreductase [Polar flagella (VF0473) - Motility (VFC0204)] [Aeromonas hydrophila ML09-119] |
Aeromonas hydrophila |
| AEQF01000040.1_197 |
60.811 |
1.09E-24 |
acpXL |
VF0367 |
LPS |
Immune modulation |
VFC0258 |
Brucella possesses a non-classical LPS as compared with the so-called classical LPS from enterobacteria such as Escherichia coli. B. abortus lipid A possesses a diaminoglucose backbone (rather than glucosamine), and acyl groups are longer (C28 rather than C12 and C16) and are only linked to the core by amide bounds (rather than ester and amide bonds).; In contrast to enterobacterial LPSs, Brucella LPS is several-hundred-times less active and toxic than E. coli LPS.; this is an evolutionary adaptation to an intracellular lifestyle, low endotoxic activity is shared by other intracellular pathogens such as Bartonella and Legionella. |
(acpXL) acyl carrier protein [LPS (VF0367) - Immune modulation (VFC0258)] [Brucella melitensis bv. 1 str. 16M] |
Brucella melitensis |
| AEQF01000040.1_201 |
99.603 |
0.0 |
katA |
VF0454 |
KatA |
Stress survival |
VFC0282 |
|
(katA) catalase [KatA (VF0454) - Stress survival (VFC0282)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000039.1_14 |
76.953 |
1.4E-138 |
lgtB |
VF0078 |
LOS |
Immune modulation |
VFC0258 |
Biosynthesis pathway of LOS is producing a branched oligosaccharide attached to a lipid A via two 3-deoxy-D-manno-2-octulosonic acid (KDO) molecules. The rfaC gene product adds the first heptose (Hep I) to KDO. The rfaF gene product adds the second Hep onto Hep I and is required for alpha-chain elongation. The lgtF gene product adds the first Glc of the alpha-chain. Genes lgtA, lgtB, lgtE are responsible for the synthesis of different alpha chains. lgtG is required for addition of the fist Glc of the beta chain; lgtA, lgtC, lgtG are subject to phase variation of expression mediated by homopolymeric tracts within their coding regions |
(lgtB) glycosyltransferase family 25 protein [LOS (VF0078) - Immune modulation (VFC0258)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000039.1_15 |
100.0 |
2.94E-13 |
lgtA |
VF0078 |
LOS |
Immune modulation |
VFC0258 |
Biosynthesis pathway of LOS is producing a branched oligosaccharide attached to a lipid A via two 3-deoxy-D-manno-2-octulosonic acid (KDO) molecules. The rfaC gene product adds the first heptose (Hep I) to KDO. The rfaF gene product adds the second Hep onto Hep I and is required for alpha-chain elongation. The lgtF gene product adds the first Glc of the alpha-chain. Genes lgtA, lgtB, lgtE are responsible for the synthesis of different alpha chains. lgtG is required for addition of the fist Glc of the beta chain; lgtA, lgtC, lgtG are subject to phase variation of expression mediated by homopolymeric tracts within their coding regions |
(lgtA) glycosyltransferase [LOS (VF0078) - Immune modulation (VFC0258)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000039.1_16 |
95.341 |
0.0 |
lgtB |
VF0078 |
LOS |
Immune modulation |
VFC0258 |
Biosynthesis pathway of LOS is producing a branched oligosaccharide attached to a lipid A via two 3-deoxy-D-manno-2-octulosonic acid (KDO) molecules. The rfaC gene product adds the first heptose (Hep I) to KDO. The rfaF gene product adds the second Hep onto Hep I and is required for alpha-chain elongation. The lgtF gene product adds the first Glc of the alpha-chain. Genes lgtA, lgtB, lgtE are responsible for the synthesis of different alpha chains. lgtG is required for addition of the fist Glc of the beta chain; lgtA, lgtC, lgtG are subject to phase variation of expression mediated by homopolymeric tracts within their coding regions |
(lgtB) glycosyltransferase family 25 protein [LOS (VF0078) - Immune modulation (VFC0258)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000039.1_17 |
97.994 |
0.0 |
lgtA |
VF0078 |
LOS |
Immune modulation |
VFC0258 |
Biosynthesis pathway of LOS is producing a branched oligosaccharide attached to a lipid A via two 3-deoxy-D-manno-2-octulosonic acid (KDO) molecules. The rfaC gene product adds the first heptose (Hep I) to KDO. The rfaF gene product adds the second Hep onto Hep I and is required for alpha-chain elongation. The lgtF gene product adds the first Glc of the alpha-chain. Genes lgtA, lgtB, lgtE are responsible for the synthesis of different alpha chains. lgtG is required for addition of the fist Glc of the beta chain; lgtA, lgtC, lgtG are subject to phase variation of expression mediated by homopolymeric tracts within their coding regions |
(lgtA) glycosyltransferase [LOS (VF0078) - Immune modulation (VFC0258)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000034.1_1 |
97.091 |
0.0 |
frpC |
VF0897 |
RTX protein |
Adherence |
VFC0001 |
|
(frpC) iron-regulated protein FrpC [RTX protein (VF0897) - Adherence (VFC0001)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000034.1_39 |
91.473 |
1.06E-88 |
pilV |
VF0075 |
Type IV pili |
Adherence |
VFC0001 |
One or two different loci are used for the expression of the major pilin encoding gene (pilE), whereas various silent genes (pilS) are spread throughout the chromosome. Recombination between pilS and pilE copies leads to changes in the pilin coding sequence and subsequently to the expression of antigenically different pili. Mutations affecting the length of the homopolymeric G-run located in the region encoding the SP of PilC results in on/off changes in piliation |
(pilV) type IV pilus minor pilin PilV [Type IV pili (VF0075) - Adherence (VFC0001)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000033.1_14 |
99.102 |
0.0 |
recN |
VF0457 |
RecN |
Stress survival |
VFC0282 |
|
(recN) DNA repair protein RecN [RecN (VF0457) - Stress survival (VFC0282)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000033.1_56 |
79.846 |
0.0 |
iga |
VF0080 |
IgA1 protease |
Effector delivery system |
VFC0086 |
|
(iga) IgA-specific serine endopeptidase [IgA1 protease (VF0080) - Effector delivery system (VFC0086)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000033.1_95 |
99.425 |
2.9E-123 |
nspA |
VF0453 |
NspA |
Immune modulation |
VFC0258 |
|
(nspA) neisserial surface protein A [NspA (VF0453) - Immune modulation (VFC0258)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000033.1_127 |
100.0 |
0.0 |
fbpA |
VF0272 |
FbpABC |
Nutritional/Metabolic factor |
VFC0272 |
|
(fbpA) iron(III) ABC transporter, periplasmic binding protein [FbpABC (VF0272) - Nutritional/Metabolic factor (VFC0272)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000033.1_128 |
99.802 |
0.0 |
fbpB |
VF0272 |
FbpABC |
Nutritional/Metabolic factor |
VFC0272 |
|
(fbpB) iron(III) ABC transporter, permease protein [FbpABC (VF0272) - Nutritional/Metabolic factor (VFC0272)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000033.1_129 |
100.0 |
0.0 |
fbpC |
VF0272 |
FbpABC |
Nutritional/Metabolic factor |
VFC0272 |
|
(fbpC) iron(III) ABC transporter, ATP-binding protein [FbpABC (VF0272) - Nutritional/Metabolic factor (VFC0272)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000033.1_174 |
96.266 |
1.13E-179 |
mntA |
VF0455 |
MntABC |
Stress survival |
VFC0282 |
An ATP binding cassette (ABC) permease containing a periplasmic metal binding receptor protein (MBR), MntC |
(mntA) ABC transporter ATP-binding protein MntA [MntABC (VF0455) - Stress survival (VFC0282)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000033.1_175 |
99.656 |
0.0 |
mntB |
VF0455 |
MntABC |
Stress survival |
VFC0282 |
An ATP binding cassette (ABC) permease containing a periplasmic metal binding receptor protein (MBR), MntC |
(mntB) Manganese transport system membrane protein MntB [MntABC (VF0455) - Stress survival (VFC0282)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000033.1_176 |
97.697 |
0.0 |
mntC |
VF0455 |
MntABC |
Stress survival |
VFC0282 |
An ATP binding cassette (ABC) permease containing a periplasmic metal binding receptor protein (MBR), MntC |
(mntC) periplasmic binding protein MntC [MntABC (VF0455) - Stress survival (VFC0282)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000033.1_177 |
98.02 |
0.0 |
frpA |
VF0897 |
RTX protein |
Adherence |
VFC0001 |
|
(frpA) iron-regulated protein FrpA [RTX protein (VF0897) - Adherence (VFC0001)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000032.1_35 |
98.276 |
9.96E-84 |
pilZ |
VF0075 |
Type IV pili |
Adherence |
VFC0001 |
One or two different loci are used for the expression of the major pilin encoding gene (pilE), whereas various silent genes (pilS) are spread throughout the chromosome. Recombination between pilS and pilE copies leads to changes in the pilin coding sequence and subsequently to the expression of antigenically different pili. Mutations affecting the length of the homopolymeric G-run located in the region encoding the SP of PilC results in on/off changes in piliation |
(pilZ) type IV pilus assembly protein PilZ [Type IV pili (VF0075) - Adherence (VFC0001)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000032.1_37 |
99.189 |
0.0 |
pilT2 |
VF0075 |
Type IV pili |
Adherence |
VFC0001 |
One or two different loci are used for the expression of the major pilin encoding gene (pilE), whereas various silent genes (pilS) are spread throughout the chromosome. Recombination between pilS and pilE copies leads to changes in the pilin coding sequence and subsequently to the expression of antigenically different pili. Mutations affecting the length of the homopolymeric G-run located in the region encoding the SP of PilC results in on/off changes in piliation |
(pilT2) twitching motility protein PilT [Type IV pili (VF0075) - Adherence (VFC0001)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000026.1_33 |
63.784 |
6.0E-91 |
sodB |
VF0169 |
SodB |
Stress survival |
VFC0282 |
|
(sodB) superoxide dismutase [SodB (VF0169) - Stress survival (VFC0282)] [Legionella pneumophila subsp. pneumophila str. Philadelphia 1] |
Legionella pneumophila |
| AEQF01000026.1_35 |
87.556 |
8.28E-148 |
pilH |
VF0075 |
Type IV pili |
Adherence |
VFC0001 |
One or two different loci are used for the expression of the major pilin encoding gene (pilE), whereas various silent genes (pilS) are spread throughout the chromosome. Recombination between pilS and pilE copies leads to changes in the pilin coding sequence and subsequently to the expression of antigenically different pili. Mutations affecting the length of the homopolymeric G-run located in the region encoding the SP of PilC results in on/off changes in piliation |
(pilH) pilin-like protein may involving in pseudopilus formation [Type IV pili (VF0075) - Adherence (VFC0001)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000026.1_36 |
93.103 |
1.39E-139 |
pilI |
VF0075 |
Type IV pili |
Adherence |
VFC0001 |
One or two different loci are used for the expression of the major pilin encoding gene (pilE), whereas various silent genes (pilS) are spread throughout the chromosome. Recombination between pilS and pilE copies leads to changes in the pilin coding sequence and subsequently to the expression of antigenically different pili. Mutations affecting the length of the homopolymeric G-run located in the region encoding the SP of PilC results in on/off changes in piliation |
(pilI) pilin-like protein may involving in pseudopilus formation [Type IV pili (VF0075) - Adherence (VFC0001)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000026.1_37 |
94.888 |
0.0 |
pilJ |
VF0075 |
Type IV pili |
Adherence |
VFC0001 |
One or two different loci are used for the expression of the major pilin encoding gene (pilE), whereas various silent genes (pilS) are spread throughout the chromosome. Recombination between pilS and pilE copies leads to changes in the pilin coding sequence and subsequently to the expression of antigenically different pili. Mutations affecting the length of the homopolymeric G-run located in the region encoding the SP of PilC results in on/off changes in piliation |
(pilJ) pilin-like protein may involving in pseudopilus formation [Type IV pili (VF0075) - Adherence (VFC0001)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000026.1_38 |
95.477 |
4.43E-139 |
pilK |
VF0075 |
Type IV pili |
Adherence |
VFC0001 |
One or two different loci are used for the expression of the major pilin encoding gene (pilE), whereas various silent genes (pilS) are spread throughout the chromosome. Recombination between pilS and pilE copies leads to changes in the pilin coding sequence and subsequently to the expression of antigenically different pili. Mutations affecting the length of the homopolymeric G-run located in the region encoding the SP of PilC results in on/off changes in piliation |
(pilK) pilin-like protein may involving in pseudopilus formation [Type IV pili (VF0075) - Adherence (VFC0001)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000026.1_39 |
92.357 |
3.01E-107 |
pilX |
VF0075 |
Type IV pili |
Adherence |
VFC0001 |
One or two different loci are used for the expression of the major pilin encoding gene (pilE), whereas various silent genes (pilS) are spread throughout the chromosome. Recombination between pilS and pilE copies leads to changes in the pilin coding sequence and subsequently to the expression of antigenically different pili. Mutations affecting the length of the homopolymeric G-run located in the region encoding the SP of PilC results in on/off changes in piliation |
(pilX) type IV pilus minor pilin PilX [Type IV pili (VF0075) - Adherence (VFC0001)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000026.1_105 |
93.007 |
1.61E-98 |
opa |
VF0076 |
Opa |
Invasion |
VFC0083 |
Opa proteins were originally identified because their expression changes the color and opacity of colonies. The effect may be due to an increased interbacterial aggregation that results from the lectin-like ability of Opa proteins to bind to LOS on adjacent bacteria; A single gonococcal strain can harbor up to 12 opa genes, meningococci usually encode 3 to 4 Opa proteins; all opa genes sequenced to date contain 5' tandem repeats [CTCTT]n that cause high-frequency phase variable expression; grouped into two major classes according to the binding specificity for human surface receptors: the OpaHS-type (heparansulphate proteoglycan (HSPG) and OpaCEA-type (carcinoembryonic antigen (CEA) or related molecules) |
(opa) outer membrane beta-barrel protein [Opa (VF0076) - Invasion (VFC0083)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000026.1_107 |
83.146 |
7.6E-49 |
opa |
VF0076 |
Opa |
Invasion |
VFC0083 |
Opa proteins were originally identified because their expression changes the color and opacity of colonies. The effect may be due to an increased interbacterial aggregation that results from the lectin-like ability of Opa proteins to bind to LOS on adjacent bacteria; A single gonococcal strain can harbor up to 12 opa genes, meningococci usually encode 3 to 4 Opa proteins; all opa genes sequenced to date contain 5' tandem repeats [CTCTT]n that cause high-frequency phase variable expression; grouped into two major classes according to the binding specificity for human surface receptors: the OpaHS-type (heparansulphate proteoglycan (HSPG) and OpaCEA-type (carcinoembryonic antigen (CEA) or related molecules) |
(opa) outer membrane beta-barrel protein [Opa (VF0076) - Invasion (VFC0083)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000026.1_125 |
91.349 |
0.0 |
porA |
VF0081 |
Porin |
Invasion |
VFC0083 |
N.meningitidis produces two porins, PorA and PorB, N.gonorrhoeae expresses only one porin, PorB |
(porA) porin PorA [Porin (VF0081) - Invasion (VFC0083)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000026.1_140 |
89.022 |
0.0 |
frpC |
VF0897 |
RTX protein |
Adherence |
VFC0001 |
|
(frpC) iron-regulated protein FrpC [RTX protein (VF0897) - Adherence (VFC0001)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000026.1_145 |
70.286 |
0.0 |
hlyB |
VF0225 |
Alpha-Hemolysin |
Exotoxin |
VFC0235 |
Best-characterized RTX protein secreted by a type I secretion system: the structural gene encoding the hemolysin (hlyA) is part of an operon that also encodes a dedicated export system (HlyB and HlyD comprising a type I secretion system) and a toxin modifying enzyme (HlyC). The HlyC protein is responsible for acylation of HlyA, resulting in toxin activation; The hly operon is found on a plasmid of EHEC O157:H7, while the hly operon is often located adjacent to the P fimbrial genes on the same pathogenicity island on the chromosome of UPEC strains |
(hlyB) Hemolysin B [Alpha-Hemolysin (VF0225) - Exotoxin (VFC0235)] [Escherichia coli CFT073] |
Escherichia coli (UPEC) |
| AEQF01000026.1_227 |
63.452 |
7.19E-94 |
clpP |
VF0074 |
ClpP |
Stress survival |
VFC0282 |
21.6 kDa protein belongs to a family of proteases highly conserved in prokaryotes and eukaryotes |
(clpP) ATP-dependent Clp protease proteolytic subunit [ClpP (VF0074) - Stress survival (VFC0282)] [Listeria monocytogenes EGD-e] |
Listeria monocytogenes |
| AEQF01000026.1_229 |
99.605 |
0.0 |
pilW |
VF0075 |
Type IV pili |
Adherence |
VFC0001 |
One or two different loci are used for the expression of the major pilin encoding gene (pilE), whereas various silent genes (pilS) are spread throughout the chromosome. Recombination between pilS and pilE copies leads to changes in the pilin coding sequence and subsequently to the expression of antigenically different pili. Mutations affecting the length of the homopolymeric G-run located in the region encoding the SP of PilC results in on/off changes in piliation |
(pilW) type IV fimbrial biogenesis and twitching motility protein PilW [Type IV pili (VF0075) - Adherence (VFC0001)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000026.1_255 |
69.455 |
2.65E-143 |
kdsA |
VF0044 |
LOS |
Immune modulation |
VFC0258 |
Lic1A (phosphorylcholine (ChoP) kinase) 5'-CAAT-3' within the 5'-end of its coding sequence; lic2A, also referred to as lexA, variation in the number of 5'-CAAT-3' repeats has been shown to correlate directly with phase variation of the Gal-alpha(1-4)beta-Gal LPS structure; But lgtC (glycosyltransferase), another phase-variable gene, ultimately dictates whether this structure is synthesized. lic3A encode a sialyl transferase which directs the substitution of LPS with sialic acid. |
(kdsA) 2-dehydro-3-deoxyphosphooctonate aldolase [LOS (VF0044) - Immune modulation (VFC0258)] [Haemophilus influenzae Rd KW20] |
Haemophilus influenzae |
| AEQF01000024.1_1 |
77.551 |
2.45E-132 |
opa |
VF0076 |
Opa |
Invasion |
VFC0083 |
Opa proteins were originally identified because their expression changes the color and opacity of colonies. The effect may be due to an increased interbacterial aggregation that results from the lectin-like ability of Opa proteins to bind to LOS on adjacent bacteria; A single gonococcal strain can harbor up to 12 opa genes, meningococci usually encode 3 to 4 Opa proteins; all opa genes sequenced to date contain 5' tandem repeats [CTCTT]n that cause high-frequency phase variable expression; grouped into two major classes according to the binding specificity for human surface receptors: the OpaHS-type (heparansulphate proteoglycan (HSPG) and OpaCEA-type (carcinoembryonic antigen (CEA) or related molecules) |
(opa) outer membrane beta-barrel protein [Opa (VF0076) - Invasion (VFC0083)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000018.1_1 |
98.81 |
0.0 |
rfaF |
VF0078 |
LOS |
Immune modulation |
VFC0258 |
Biosynthesis pathway of LOS is producing a branched oligosaccharide attached to a lipid A via two 3-deoxy-D-manno-2-octulosonic acid (KDO) molecules. The rfaC gene product adds the first heptose (Hep I) to KDO. The rfaF gene product adds the second Hep onto Hep I and is required for alpha-chain elongation. The lgtF gene product adds the first Glc of the alpha-chain. Genes lgtA, lgtB, lgtE are responsible for the synthesis of different alpha chains. lgtG is required for addition of the fist Glc of the beta chain; lgtA, lgtC, lgtG are subject to phase variation of expression mediated by homopolymeric tracts within their coding regions |
(rfaF) lipopolysaccharide heptosyltransferase II [LOS (VF0078) - Immune modulation (VFC0258)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000017.1_1 |
68.021 |
0.0 |
lbpB |
VF0047 |
Lbp |
Nutritional/Metabolic factor |
VFC0272 |
The entry site of N. meningitidis into the body is the nasopharynx, where lactoferrin predominates as the main source of iron |
(lbpB) lactoferrin-binding protein B [Lbp (VF0047) - Nutritional/Metabolic factor (VFC0272)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000017.1_2 |
96.504 |
0.0 |
lbpA |
VF0047 |
Lbp |
Nutritional/Metabolic factor |
VFC0272 |
The entry site of N. meningitidis into the body is the nasopharynx, where lactoferrin predominates as the main source of iron |
(lbpA) lactoferrin-binding protein A [Lbp (VF0047) - Nutritional/Metabolic factor (VFC0272)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000016.1_1 |
89.552 |
8.89E-20 |
opa |
VF0076 |
Opa |
Invasion |
VFC0083 |
Opa proteins were originally identified because their expression changes the color and opacity of colonies. The effect may be due to an increased interbacterial aggregation that results from the lectin-like ability of Opa proteins to bind to LOS on adjacent bacteria; A single gonococcal strain can harbor up to 12 opa genes, meningococci usually encode 3 to 4 Opa proteins; all opa genes sequenced to date contain 5' tandem repeats [CTCTT]n that cause high-frequency phase variable expression; grouped into two major classes according to the binding specificity for human surface receptors: the OpaHS-type (heparansulphate proteoglycan (HSPG) and OpaCEA-type (carcinoembryonic antigen (CEA) or related molecules) |
(opa) outer membrane beta-barrel protein [Opa (VF0076) - Invasion (VFC0083)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000016.1_81 |
82.993 |
4.01E-84 |
lbpB |
VF0047 |
Lbp |
Nutritional/Metabolic factor |
VFC0272 |
The entry site of N. meningitidis into the body is the nasopharynx, where lactoferrin predominates as the main source of iron |
(lbpB) lactoferrin-binding protein B [Lbp (VF0047) - Nutritional/Metabolic factor (VFC0272)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000015.1_16 |
92.308 |
2.05E-97 |
opa |
VF0076 |
Opa |
Invasion |
VFC0083 |
Opa proteins were originally identified because their expression changes the color and opacity of colonies. The effect may be due to an increased interbacterial aggregation that results from the lectin-like ability of Opa proteins to bind to LOS on adjacent bacteria; A single gonococcal strain can harbor up to 12 opa genes, meningococci usually encode 3 to 4 Opa proteins; all opa genes sequenced to date contain 5' tandem repeats [CTCTT]n that cause high-frequency phase variable expression; grouped into two major classes according to the binding specificity for human surface receptors: the OpaHS-type (heparansulphate proteoglycan (HSPG) and OpaCEA-type (carcinoembryonic antigen (CEA) or related molecules) |
(opa) outer membrane beta-barrel protein [Opa (VF0076) - Invasion (VFC0083)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000013.1_15 |
98.301 |
0.0 |
mtrC |
VF0451 |
MtrCDE |
Antimicrobial activity/Competitive advantage |
VFC0325 |
Resistance/nodulation/division (RND)-type efflux pump; regulated by two transcriptional regulators: a repressor MtrR and an activator MtrA |
(mtrC) membrane fusion protein MtrC [MtrCDE (VF0451) - Antimicrobial activity/Competitive advantage (VFC0325)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000013.1_16 |
99.719 |
0.0 |
mtrD |
VF0451 |
MtrCDE |
Antimicrobial activity/Competitive advantage |
VFC0325 |
Resistance/nodulation/division (RND)-type efflux pump; regulated by two transcriptional regulators: a repressor MtrR and an activator MtrA |
(mtrD) multiple transferable resistance system protein MtrD [MtrCDE (VF0451) - Antimicrobial activity/Competitive advantage (VFC0325)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000013.1_17 |
99.572 |
0.0 |
mtrE |
VF0451 |
MtrCDE |
Antimicrobial activity/Competitive advantage |
VFC0325 |
Resistance/nodulation/division (RND)-type efflux pump; regulated by two transcriptional regulators: a repressor MtrR and an activator MtrA |
(mtrE) multidrug efflux pump channel protein MtrE [MtrCDE (VF0451) - Antimicrobial activity/Competitive advantage (VFC0325)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000013.1_28 |
97.74 |
0.0 |
rfaK |
VF0078 |
LOS |
Immune modulation |
VFC0258 |
Biosynthesis pathway of LOS is producing a branched oligosaccharide attached to a lipid A via two 3-deoxy-D-manno-2-octulosonic acid (KDO) molecules. The rfaC gene product adds the first heptose (Hep I) to KDO. The rfaF gene product adds the second Hep onto Hep I and is required for alpha-chain elongation. The lgtF gene product adds the first Glc of the alpha-chain. Genes lgtA, lgtB, lgtE are responsible for the synthesis of different alpha chains. lgtG is required for addition of the fist Glc of the beta chain; lgtA, lgtC, lgtG are subject to phase variation of expression mediated by homopolymeric tracts within their coding regions |
(rfaK) glycosyltransferase family 4 protein [LOS (VF0078) - Immune modulation (VFC0258)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000013.1_29 |
98.81 |
0.0 |
lgtF |
VF0078 |
LOS |
Immune modulation |
VFC0258 |
Biosynthesis pathway of LOS is producing a branched oligosaccharide attached to a lipid A via two 3-deoxy-D-manno-2-octulosonic acid (KDO) molecules. The rfaC gene product adds the first heptose (Hep I) to KDO. The rfaF gene product adds the second Hep onto Hep I and is required for alpha-chain elongation. The lgtF gene product adds the first Glc of the alpha-chain. Genes lgtA, lgtB, lgtE are responsible for the synthesis of different alpha chains. lgtG is required for addition of the fist Glc of the beta chain; lgtA, lgtC, lgtG are subject to phase variation of expression mediated by homopolymeric tracts within their coding regions |
(lgtF) glycosyltransferase family 2 protein [LOS (VF0078) - Immune modulation (VFC0258)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000013.1_62 |
94.325 |
0.0 |
hmbR |
VF0048 |
HmbR |
Nutritional/Metabolic factor |
VFC0272 |
The gene encoding the hemoglobin receptor, hmbR, is located downstream of a gene involved in the catabolism of heme, hemO; expression of HmbR undergoes phase variation due to slip-strand mispairing of poly(G) tracts within the hmbR gene. The advantage associated with phase-varying surface proteins is evasion of the host immune response |
(hmbR) hemoglobin receptor [HmbR (VF0048) - Nutritional/Metabolic factor (VFC0272)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000012.1_1 |
87.291 |
0.0 |
tbpB |
VF0046 |
Tbp |
Nutritional/Metabolic factor |
VFC0272 |
The tbp locus is a bicistronic operon consisting of tbpA and tbpB. Unlike the case for many other genes of Neisseria, there is no phase variation of the transferrin receptor |
(tbpB) transferrin-binding protein B [Tbp (VF0046) - Nutritional/Metabolic factor (VFC0272)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000012.1_2 |
96.503 |
0.0 |
tbpA |
VF0046 |
Tbp |
Nutritional/Metabolic factor |
VFC0272 |
The tbp locus is a bicistronic operon consisting of tbpA and tbpB. Unlike the case for many other genes of Neisseria, there is no phase variation of the transferrin receptor |
(tbpA) transferrin-binding protein A [Tbp (VF0046) - Nutritional/Metabolic factor (VFC0272)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000010.1_1 |
99.821 |
0.0 |
pilF |
VF0075 |
Type IV pili |
Adherence |
VFC0001 |
One or two different loci are used for the expression of the major pilin encoding gene (pilE), whereas various silent genes (pilS) are spread throughout the chromosome. Recombination between pilS and pilE copies leads to changes in the pilin coding sequence and subsequently to the expression of antigenically different pili. Mutations affecting the length of the homopolymeric G-run located in the region encoding the SP of PilC results in on/off changes in piliation |
(pilF) type IV pilus assembly ATPase protein [Type IV pili (VF0075) - Adherence (VFC0001)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000010.1_4 |
97.902 |
0.0 |
pilD |
VF0075 |
Type IV pili |
Adherence |
VFC0001 |
One or two different loci are used for the expression of the major pilin encoding gene (pilE), whereas various silent genes (pilS) are spread throughout the chromosome. Recombination between pilS and pilE copies leads to changes in the pilin coding sequence and subsequently to the expression of antigenically different pili. Mutations affecting the length of the homopolymeric G-run located in the region encoding the SP of PilC results in on/off changes in piliation |
(pilD) type IV pilus prepilin peptidase [Type IV pili (VF0075) - Adherence (VFC0001)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000010.1_5 |
99.512 |
0.0 |
pilG |
VF0075 |
Type IV pili |
Adherence |
VFC0001 |
One or two different loci are used for the expression of the major pilin encoding gene (pilE), whereas various silent genes (pilS) are spread throughout the chromosome. Recombination between pilS and pilE copies leads to changes in the pilin coding sequence and subsequently to the expression of antigenically different pili. Mutations affecting the length of the homopolymeric G-run located in the region encoding the SP of PilC results in on/off changes in piliation |
(pilG) pilus assembly protein PilG [Type IV pili (VF0075) - Adherence (VFC0001)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000010.1_37 |
98.718 |
2.02E-48 |
frpC |
VF0897 |
RTX protein |
Adherence |
VFC0001 |
|
(frpC) iron-regulated protein FrpC [RTX protein (VF0897) - Adherence (VFC0001)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000010.1_111 |
82.902 |
1.09E-111 |
opa |
VF0076 |
Opa |
Invasion |
VFC0083 |
Opa proteins were originally identified because their expression changes the color and opacity of colonies. The effect may be due to an increased interbacterial aggregation that results from the lectin-like ability of Opa proteins to bind to LOS on adjacent bacteria; A single gonococcal strain can harbor up to 12 opa genes, meningococci usually encode 3 to 4 Opa proteins; all opa genes sequenced to date contain 5' tandem repeats [CTCTT]n that cause high-frequency phase variable expression; grouped into two major classes according to the binding specificity for human surface receptors: the OpaHS-type (heparansulphate proteoglycan (HSPG) and OpaCEA-type (carcinoembryonic antigen (CEA) or related molecules) |
(opa) outer membrane beta-barrel protein [Opa (VF0076) - Invasion (VFC0083)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000008.1_18 |
96.923 |
0.0 |
farA |
VF0450 |
FarAB |
Antimicrobial activity/Competitive advantage |
VFC0325 |
The far efflux system is composed of the FarA membrane fusion protein, the FarB cytoplasmic membrane transporter protein, and the MtrE protein as the outer membrane channel to export antibacterial fatty acids from inside the cell; belongs to Major Facilitator Superfamily (MFS) of efflux pumps and uses the proton motive force as an energy source for export of toxic agents |
(farA) fatty acid efflux system protein FarA [FarAB (VF0450) - Antimicrobial activity/Competitive advantage (VFC0325)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000008.1_19 |
97.826 |
0.0 |
farB |
VF0450 |
FarAB |
Antimicrobial activity/Competitive advantage |
VFC0325 |
The far efflux system is composed of the FarA membrane fusion protein, the FarB cytoplasmic membrane transporter protein, and the MtrE protein as the outer membrane channel to export antibacterial fatty acids from inside the cell; belongs to Major Facilitator Superfamily (MFS) of efflux pumps and uses the proton motive force as an energy source for export of toxic agents |
(farB) fatty acid efflux system protein FarB [FarAB (VF0450) - Antimicrobial activity/Competitive advantage (VFC0325)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000005.1_12 |
79.898 |
0.0 |
tufA |
VF0460 |
EF-Tu |
Adherence |
VFC0001 |
|
(tufA) elongation factor Tu [EF-Tu (VF0460) - Adherence (VFC0001)] [Francisella tularensis subsp. tularensis SCHU S4] |
Francisella tularensis |
| AEQF01000004.1_8 |
62.887 |
1.28E-139 |
wbtL |
VF0542 |
LPS |
Immune modulation |
VFC0258 |
The structure of Francisella spp. lipid A is unique in that it is modified by various carbohydrates that greatly reduce TLR4 activation and allow for immune evasion |
(wbtL) glucose-1-phosphate thymidylyltransferase [LPS (VF0542) - Immune modulation (VFC0258)] [Francisella tularensis subsp. tularensis SCHU S4] |
Francisella tularensis |
| AEQF01000004.1_9 |
65.179 |
5.74E-171 |
rffG |
VF0044 |
LOS |
Immune modulation |
VFC0258 |
Lic1A (phosphorylcholine (ChoP) kinase) 5'-CAAT-3' within the 5'-end of its coding sequence; lic2A, also referred to as lexA, variation in the number of 5'-CAAT-3' repeats has been shown to correlate directly with phase variation of the Gal-alpha(1-4)beta-Gal LPS structure; But lgtC (glycosyltransferase), another phase-variable gene, ultimately dictates whether this structure is synthesized. lic3A encode a sialyl transferase which directs the substitution of LPS with sialic acid. |
(rffG) dTDP-glucose 46-dehydratase [LOS (VF0044) - Immune modulation (VFC0258)] [Haemophilus influenzae Rd KW20] |
Haemophilus influenzae |
| AEQF01000004.1_10 |
63.988 |
2.39E-164 |
galE |
VF0044 |
LOS |
Immune modulation |
VFC0258 |
Lic1A (phosphorylcholine (ChoP) kinase) 5'-CAAT-3' within the 5'-end of its coding sequence; lic2A, also referred to as lexA, variation in the number of 5'-CAAT-3' repeats has been shown to correlate directly with phase variation of the Gal-alpha(1-4)beta-Gal LPS structure; But lgtC (glycosyltransferase), another phase-variable gene, ultimately dictates whether this structure is synthesized. lic3A encode a sialyl transferase which directs the substitution of LPS with sialic acid. |
(galE) UDP-glucose 4-epimerase [LOS (VF0044) - Immune modulation (VFC0258)] [Haemophilus influenzae Rd KW20] |
Haemophilus influenzae |
| AEQF01000004.1_15 |
100.0 |
0.0 |
siaC/synC |
VF0079 |
Capsule |
Immune modulation |
VFC0258 |
The meningococcal capsule-synthesis (cps) gene cluster consists of five regions:; region A harbors the polysaccharide synthesis operon (sia, syn genes); region B contains lip genes responsible for lipid modification; region C harbors ctr genes necessary for polysaccharide transport; region D is involved in lipopolysaccharide synthesis; region D' is a truncated duplication of the region D; region E contains the tex gene homologue; on-off switching of expression via a poly-cytidine tract within siaD |
(siaC/synC) polysialic acid capsule biosynthesis protein SiaC [Capsule (VF0079) - Immune modulation (VFC0258)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000004.1_16 |
99.561 |
1.47E-170 |
siaB/synB |
VF0079 |
Capsule |
Immune modulation |
VFC0258 |
The meningococcal capsule-synthesis (cps) gene cluster consists of five regions:; region A harbors the polysaccharide synthesis operon (sia, syn genes); region B contains lip genes responsible for lipid modification; region C harbors ctr genes necessary for polysaccharide transport; region D is involved in lipopolysaccharide synthesis; region D' is a truncated duplication of the region D; region E contains the tex gene homologue; on-off switching of expression via a poly-cytidine tract within siaD |
(siaB/synB) polysialic acid capsule biosynthesis protein SiaB [Capsule (VF0079) - Immune modulation (VFC0258)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000004.1_17 |
99.469 |
0.0 |
siaA/synA |
VF0079 |
Capsule |
Immune modulation |
VFC0258 |
The meningococcal capsule-synthesis (cps) gene cluster consists of five regions:; region A harbors the polysaccharide synthesis operon (sia, syn genes); region B contains lip genes responsible for lipid modification; region C harbors ctr genes necessary for polysaccharide transport; region D is involved in lipopolysaccharide synthesis; region D' is a truncated duplication of the region D; region E contains the tex gene homologue; on-off switching of expression via a poly-cytidine tract within siaD |
(siaA/synA) polysialic acid capsule biosynthesis protein SynX [Capsule (VF0079) - Immune modulation (VFC0258)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000004.1_18 |
100.0 |
0.0 |
ctrA |
VF0079 |
Capsule |
Immune modulation |
VFC0258 |
The meningococcal capsule-synthesis (cps) gene cluster consists of five regions:; region A harbors the polysaccharide synthesis operon (sia, syn genes); region B contains lip genes responsible for lipid modification; region C harbors ctr genes necessary for polysaccharide transport; region D is involved in lipopolysaccharide synthesis; region D' is a truncated duplication of the region D; region E contains the tex gene homologue; on-off switching of expression via a poly-cytidine tract within siaD |
(ctrA) capsule polysaccharide export outer membrane protein CtrA [Capsule (VF0079) - Immune modulation (VFC0258)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000004.1_19 |
100.0 |
0.0 |
ctrB |
VF0079 |
Capsule |
Immune modulation |
VFC0258 |
The meningococcal capsule-synthesis (cps) gene cluster consists of five regions:; region A harbors the polysaccharide synthesis operon (sia, syn genes); region B contains lip genes responsible for lipid modification; region C harbors ctr genes necessary for polysaccharide transport; region D is involved in lipopolysaccharide synthesis; region D' is a truncated duplication of the region D; region E contains the tex gene homologue; on-off switching of expression via a poly-cytidine tract within siaD |
(ctrB) capsule polysaccharide export inner-membrane protein CtrB [Capsule (VF0079) - Immune modulation (VFC0258)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000004.1_20 |
100.0 |
0.0 |
ctrC |
VF0079 |
Capsule |
Immune modulation |
VFC0258 |
The meningococcal capsule-synthesis (cps) gene cluster consists of five regions:; region A harbors the polysaccharide synthesis operon (sia, syn genes); region B contains lip genes responsible for lipid modification; region C harbors ctr genes necessary for polysaccharide transport; region D is involved in lipopolysaccharide synthesis; region D' is a truncated duplication of the region D; region E contains the tex gene homologue; on-off switching of expression via a poly-cytidine tract within siaD |
(ctrC) capsule polysaccharide export inner-membrane protein CtrC [Capsule (VF0079) - Immune modulation (VFC0258)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000004.1_21 |
93.981 |
2.18E-154 |
ctrD |
VF0079 |
Capsule |
Immune modulation |
VFC0258 |
The meningococcal capsule-synthesis (cps) gene cluster consists of five regions:; region A harbors the polysaccharide synthesis operon (sia, syn genes); region B contains lip genes responsible for lipid modification; region C harbors ctr genes necessary for polysaccharide transport; region D is involved in lipopolysaccharide synthesis; region D' is a truncated duplication of the region D; region E contains the tex gene homologue; on-off switching of expression via a poly-cytidine tract within siaD |
(ctrD) capsule polysaccharide export ATP-binding protein CtrD [Capsule (VF0079) - Immune modulation (VFC0258)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000004.1_26 |
65.465 |
2.47E-170 |
rffG |
VF0044 |
LOS |
Immune modulation |
VFC0258 |
Lic1A (phosphorylcholine (ChoP) kinase) 5'-CAAT-3' within the 5'-end of its coding sequence; lic2A, also referred to as lexA, variation in the number of 5'-CAAT-3' repeats has been shown to correlate directly with phase variation of the Gal-alpha(1-4)beta-Gal LPS structure; But lgtC (glycosyltransferase), another phase-variable gene, ultimately dictates whether this structure is synthesized. lic3A encode a sialyl transferase which directs the substitution of LPS with sialic acid. |
(rffG) dTDP-glucose 46-dehydratase [LOS (VF0044) - Immune modulation (VFC0258)] [Haemophilus influenzae Rd KW20] |
Haemophilus influenzae |
| AEQF01000004.1_27 |
62.887 |
1.28E-139 |
wbtL |
VF0542 |
LPS |
Immune modulation |
VFC0258 |
The structure of Francisella spp. lipid A is unique in that it is modified by various carbohydrates that greatly reduce TLR4 activation and allow for immune evasion |
(wbtL) glucose-1-phosphate thymidylyltransferase [LPS (VF0542) - Immune modulation (VFC0258)] [Francisella tularensis subsp. tularensis SCHU S4] |
Francisella tularensis |
| AEQF01000004.1_28 |
60.92 |
9.52E-78 |
rfbC |
VF0171 |
LPS |
Immune modulation |
VFC0258 |
|
(rfbC) dTDP-4-dehydrorhamnose 3,5-epimerase [LPS (VF0171) - Immune modulation (VFC0258)] [Legionella pneumophila subsp. pneumophila str. Philadelphia 1] |
Legionella pneumophila |
| AEQF01000004.1_29 |
97.727 |
0.0 |
lipA |
VF0079 |
Capsule |
Immune modulation |
VFC0258 |
The meningococcal capsule-synthesis (cps) gene cluster consists of five regions:; region A harbors the polysaccharide synthesis operon (sia, syn genes); region B contains lip genes responsible for lipid modification; region C harbors ctr genes necessary for polysaccharide transport; region D is involved in lipopolysaccharide synthesis; region D' is a truncated duplication of the region D; region E contains the tex gene homologue; on-off switching of expression via a poly-cytidine tract within siaD |
(lipA) capsule polysaccharide modification protein LipA [Capsule (VF0079) - Immune modulation (VFC0258)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000004.1_30 |
99.043 |
0.0 |
lipB |
VF0079 |
Capsule |
Immune modulation |
VFC0258 |
The meningococcal capsule-synthesis (cps) gene cluster consists of five regions:; region A harbors the polysaccharide synthesis operon (sia, syn genes); region B contains lip genes responsible for lipid modification; region C harbors ctr genes necessary for polysaccharide transport; region D is involved in lipopolysaccharide synthesis; region D' is a truncated duplication of the region D; region E contains the tex gene homologue; on-off switching of expression via a poly-cytidine tract within siaD |
(lipB) capsule polysaccharide modification protein LipB [Capsule (VF0079) - Immune modulation (VFC0258)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000003.1_12 |
99.617 |
0.0 |
msrA/B(pilB |
VF0456 |
MsrAB |
Stress survival |
VFC0282 |
Methionine sulfoxide reductases (Msr) are enzymes that catalyze the reduction of free and protein-bound methionine sulfoxide (MetSO) back to Met. Two structurally unrelated classes of Msrs have been described so far. MsrAs are stereo specific toward the S isomer on the sulfur of the sulfoxide function, whereas MsrBs are specific toward the R isomer |
(msrA/B(pilB)) trifunctional thioredoxin/methionine sulfoxide reductase A/B protein [MsrAB (VF0456) - Stress survival (VFC0282)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000003.1_16 |
81.8 |
0.0 |
pilC |
VF0075 |
Type IV pili |
Adherence |
VFC0001 |
One or two different loci are used for the expression of the major pilin encoding gene (pilE), whereas various silent genes (pilS) are spread throughout the chromosome. Recombination between pilS and pilE copies leads to changes in the pilin coding sequence and subsequently to the expression of antigenically different pili. Mutations affecting the length of the homopolymeric G-run located in the region encoding the SP of PilC results in on/off changes in piliation |
(pilC) pilus assembly protein [Type IV pili (VF0075) - Adherence (VFC0001)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000003.1_27 |
100.0 |
0.0 |
pilU |
VF0075 |
Type IV pili |
Adherence |
VFC0001 |
One or two different loci are used for the expression of the major pilin encoding gene (pilE), whereas various silent genes (pilS) are spread throughout the chromosome. Recombination between pilS and pilE copies leads to changes in the pilin coding sequence and subsequently to the expression of antigenically different pili. Mutations affecting the length of the homopolymeric G-run located in the region encoding the SP of PilC results in on/off changes in piliation |
(pilU) twitching motility protein PilU [Type IV pili (VF0075) - Adherence (VFC0001)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000003.1_28 |
100.0 |
0.0 |
pilT |
VF0075 |
Type IV pili |
Adherence |
VFC0001 |
One or two different loci are used for the expression of the major pilin encoding gene (pilE), whereas various silent genes (pilS) are spread throughout the chromosome. Recombination between pilS and pilE copies leads to changes in the pilin coding sequence and subsequently to the expression of antigenically different pili. Mutations affecting the length of the homopolymeric G-run located in the region encoding the SP of PilC results in on/off changes in piliation |
(pilT) twitching motility protein PilT [Type IV pili (VF0075) - Adherence (VFC0001)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000002.1_1 |
75.701 |
8.4E-51 |
pilS |
VF0075 |
Type IV pili |
Adherence |
VFC0001 |
One or two different loci are used for the expression of the major pilin encoding gene (pilE), whereas various silent genes (pilS) are spread throughout the chromosome. Recombination between pilS and pilE copies leads to changes in the pilin coding sequence and subsequently to the expression of antigenically different pili. Mutations affecting the length of the homopolymeric G-run located in the region encoding the SP of PilC results in on/off changes in piliation |
(pilS) pilin [Type IV pili (VF0075) - Adherence (VFC0001)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |
| AEQF01000002.1_2 |
79.825 |
1.4E-59 |
pilS |
VF0075 |
Type IV pili |
Adherence |
VFC0001 |
One or two different loci are used for the expression of the major pilin encoding gene (pilE), whereas various silent genes (pilS) are spread throughout the chromosome. Recombination between pilS and pilE copies leads to changes in the pilin coding sequence and subsequently to the expression of antigenically different pili. Mutations affecting the length of the homopolymeric G-run located in the region encoding the SP of PilC results in on/off changes in piliation |
(pilS) pilin [Type IV pili (VF0075) - Adherence (VFC0001)] [Neisseria meningitidis MC58] |
Neisseria meningitidis |