| ADEH01003694.1_1 |
97.531 |
2.21E-47 |
CD3246 |
VF0599 |
CD3246 |
Adherence |
VFC0001 |
Cell surface protein cleaved and covalently anchored to m-DAP in the peptidoglycan by SrtB |
(CD3246) Cys-Gln thioester bond-forming surface protein [CD3246 (VF0599) - Adherence (VFC0001)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01003689.1_1 |
66.0 |
1.15E-36 |
carB |
VF0558 |
Pyrimidine biosynthesis |
Nutritional/Metabolic factor |
VFC0272 |
CarB, CarA, and PyrB encode the large and small subunits of carbamoylphosphate synthetase and aspartate carbamoyl transferase, respectively. These enzymes catalyze the first two steps in the pyrimidine nucleotide biosynthetic pathway in many bacteria, including Francisella, and are required for the virulence of several pathogens, including Salmonella and E. coli |
(carB) carbamoyl phosphate synthase large subunit [Pyrimidine biosynthesis (VF0558) - Nutritional/Metabolic factor (VFC0272)] [Francisella tularensis subsp. tularensis SCHU S4] |
Francisella tularensis |
| ADEH01003673.1_3 |
62.143 |
2.99E-50 |
carB |
VF0558 |
Pyrimidine biosynthesis |
Nutritional/Metabolic factor |
VFC0272 |
CarB, CarA, and PyrB encode the large and small subunits of carbamoylphosphate synthetase and aspartate carbamoyl transferase, respectively. These enzymes catalyze the first two steps in the pyrimidine nucleotide biosynthetic pathway in many bacteria, including Francisella, and are required for the virulence of several pathogens, including Salmonella and E. coli |
(carB) carbamoyl phosphate synthase large subunit [Pyrimidine biosynthesis (VF0558) - Nutritional/Metabolic factor (VFC0272)] [Francisella tularensis subsp. tularensis SCHU S4] |
Francisella tularensis |
| ADEH01003659.1_1 |
98.413 |
9.23E-37 |
toxA |
VF0376 |
TcdA |
Exotoxin |
VFC0235 |
The toxin genes tcdA and tcdB are situated on the C. difficile chromosome in a 19.6-kilobase (kb) pathogenicity locus (PaLoc), along with the three accessory genes tcdC, tcdR and tcdE.; TcdA and TcdB are homologous to each other, to TcsH and TcsL of C. sordellii and to Tcnalpha of C. novyi. Because of their sequence homology, similar domain structure and glycosyltransferase properties these toxins are designated 'large clostridial cytotoxins'. |
(toxA) toxin A [TcdA (VF0376) - Exotoxin (VFC0235)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01003623.1_1 |
97.059 |
6.69E-18 |
toxA |
VF0376 |
TcdA |
Exotoxin |
VFC0235 |
The toxin genes tcdA and tcdB are situated on the C. difficile chromosome in a 19.6-kilobase (kb) pathogenicity locus (PaLoc), along with the three accessory genes tcdC, tcdR and tcdE.; TcdA and TcdB are homologous to each other, to TcsH and TcsL of C. sordellii and to Tcnalpha of C. novyi. Because of their sequence homology, similar domain structure and glycosyltransferase properties these toxins are designated 'large clostridial cytotoxins'. |
(toxA) toxin A [TcdA (VF0376) - Exotoxin (VFC0235)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01003618.1_1 |
69.091 |
4.19E-22 |
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 |
| ADEH01003562.1_2 |
100.0 |
1.41E-62 |
toxB |
VF0377 |
TcdB |
Exotoxin |
VFC0235 |
Many forms of variant toxin B have been identified, which are functional chimeras of toxin B (reference strain VPI 10463) and C. sordellii lethal toxin, e.g., C. difficile toxin B from strain 1470 and strain 8864. Their substrate specificities resemble that of lethal toxin. C. difficile strain C34 produces a toxin B variant modifying Rho, Rac, and Cdc42 as well as R-Ras, Ral, and Rap. |
(toxB) toxin B [TcdB (VF0377) - Exotoxin (VFC0235)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01003504.1_1 |
75.0 |
1.13E-25 |
ibp |
VF0381 |
Iota-toxin |
Exotoxin |
VFC0235 |
ADP-ribosylating toxin (ADPRT) family can be classified into four groups, at least with respect to their protein acceptors, as follows:; (I) heterotrimeric GTP-binding protein ADPRT (e.g. cholera toxin, B. pertussis pertussis toxin, E. coli heat-labile enterotoxin); (II) elongation factor 2 ADPRT (e.g. diphtheria toxin, P. aeruginosa exotoxin A); (III) small GTP-binding protein ADPRT (e.g. C. botulinum C3 exoenzyme, P. aeruginosa exoenzyme S); (IV) actin ADPRT. (e.g. B. cereus VIP, C. perfringens iota-toxin, C. botulinum C2 toxin, C. spiroforme toxin, and C. difficile toxin.); The binary iota toxin is produced exclusively by C. perfringens type E strains; The two proteins that comprise iota toxin were designated iota a or Ia (slower moving) and iota b or Ib (faster moving), based on electrophoretic mobility in crossed immunoelectrophoresis; Iota toxin requires proteolytic activation. The proteolytic activation of Ib precursor into Ib occurs at A211, which then facilitates Ia docking, formation of voltage-dependent ion-permeable channels in membranes, and formation of heptamers on cell membrane. Ia is also proteolytically activated by proteases, with a resultant loss of 9 to 13 amino acids from the N terminus. Proteolytic activation of Ia is unique among the 'A' components from binary toxins |
(ibp) iota toxin component Ib [Iota-toxin (VF0381) - Exotoxin (VFC0235)] [Clostridium perfringens E str. NCIB 10748] |
Clostridium perfringens |
| ADEH01003499.1_1 |
62.295 |
8.07E-48 |
carB |
VF0558 |
Pyrimidine biosynthesis |
Nutritional/Metabolic factor |
VFC0272 |
CarB, CarA, and PyrB encode the large and small subunits of carbamoylphosphate synthetase and aspartate carbamoyl transferase, respectively. These enzymes catalyze the first two steps in the pyrimidine nucleotide biosynthetic pathway in many bacteria, including Francisella, and are required for the virulence of several pathogens, including Salmonella and E. coli |
(carB) carbamoyl phosphate synthase large subunit [Pyrimidine biosynthesis (VF0558) - Nutritional/Metabolic factor (VFC0272)] [Francisella tularensis subsp. tularensis SCHU S4] |
Francisella tularensis |
| ADEH01003492.1_1 |
100.0 |
6.73E-36 |
toxA |
VF0376 |
TcdA |
Exotoxin |
VFC0235 |
The toxin genes tcdA and tcdB are situated on the C. difficile chromosome in a 19.6-kilobase (kb) pathogenicity locus (PaLoc), along with the three accessory genes tcdC, tcdR and tcdE.; TcdA and TcdB are homologous to each other, to TcsH and TcsL of C. sordellii and to Tcnalpha of C. novyi. Because of their sequence homology, similar domain structure and glycosyltransferase properties these toxins are designated 'large clostridial cytotoxins'. |
(toxA) toxin A [TcdA (VF0376) - Exotoxin (VFC0235)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01003459.1_1 |
61.983 |
4.14E-50 |
fleQ |
VF0157 |
Flagella |
Motility |
VFC0204 |
Flagella expression is associated with the cellular cycle in L. pneumophila, the bacteria are not motile while multiplying in host cells, but become motile in the later stages of the infection process |
(fleQ) transcriptional regulator FleQ [Flagella (VF0157) - Motility (VFC0204)] [Legionella pneumophila subsp. pneumophila str. Philadelphia 1] |
Legionella pneumophila |
| ADEH01003449.1_1 |
98.485 |
2.29E-78 |
CD2831 |
VF0598 |
CD2831 |
Adherence |
VFC0001 |
Cell surface protein cleaved and covalently anchored to m-DAP in the peptidoglycan by SrtB |
(CD2831) SrtB-anchored collagen-binding adhesin [CD2831 (VF0598) - Adherence (VFC0001)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01003340.1_1 |
61.224 |
8.27E-131 |
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 |
| ADEH01003131.1_1 |
100.0 |
1.73E-57 |
zmp1 |
VF0600 |
Zmp1 |
Exoenzyme |
VFC0251 |
|
(zmp1) zinc metalloprotease Zmp1 [Zmp1 (VF0600) - Exoenzyme (VFC0251)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01003129.1_2 |
61.538 |
5.88E-39 |
fleQ |
VF0157 |
Flagella |
Motility |
VFC0204 |
Flagella expression is associated with the cellular cycle in L. pneumophila, the bacteria are not motile while multiplying in host cells, but become motile in the later stages of the infection process |
(fleQ) transcriptional regulator FleQ [Flagella (VF0157) - Motility (VFC0204)] [Legionella pneumophila subsp. pneumophila str. Philadelphia 1] |
Legionella pneumophila |
| ADEH01003064.1_8 |
60.19 |
9.8E-96 |
cps4I |
VF0144 |
Capsule |
Immune modulation |
VFC0258 |
Ninety different capsule types have been identified. Each has a structurally distinct capsule, composed of repeating oligosaccharide units joined by glycosidic linkages |
(cps4I) capsular polysaccharide biosynthesis protein Cps4I [Capsule (VF0144) - Immune modulation (VFC0258)] [Streptococcus pneumoniae TIGR4] |
Streptococcus pneumoniae |
| ADEH01003035.1_1 |
65.455 |
3.3E-20 |
kpsF |
VF0323 |
Capsule |
Immune modulation |
VFC0258 |
Major antigenic component of the classic Penner serotyping system; Variation in the capsule structure may cause by multiple mechanisms, such as exchange of capsular genes and entire clusters by horizontal transfer, gene duplication, deletion, fusion and the presence of homopolymeric G tracts in several cps genes |
(kpsF) D-arabinose 5-phosphate isomerase [Capsule (VF0323) - Immune modulation (VFC0258)] [Campylobacter jejuni subsp. jejuni NCTC 11168] |
Campylobacter jejuni |
| ADEH01002983.1_1 |
62.044 |
4.86E-56 |
fleQ |
VF0157 |
Flagella |
Motility |
VFC0204 |
Flagella expression is associated with the cellular cycle in L. pneumophila, the bacteria are not motile while multiplying in host cells, but become motile in the later stages of the infection process |
(fleQ) transcriptional regulator FleQ [Flagella (VF0157) - Motility (VFC0204)] [Legionella pneumophila subsp. pneumophila str. Philadelphia 1] |
Legionella pneumophila |
| ADEH01002804.1_1 |
100.0 |
8.48E-40 |
CD2831 |
VF0598 |
CD2831 |
Adherence |
VFC0001 |
Cell surface protein cleaved and covalently anchored to m-DAP in the peptidoglycan by SrtB |
(CD2831) SrtB-anchored collagen-binding adhesin [CD2831 (VF0598) - Adherence (VFC0001)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01002783.1_1 |
65.625 |
9.73E-12 |
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 |
| ADEH01002729.1_2 |
100.0 |
1.74E-43 |
fbpA/fbp68 |
VF0595 |
FbpA/Fbp68 |
Adherence |
VFC0001 |
Fibronectin is a dimeric glycoprotein (~440 kDa) which is present in a soluble form in plasma and in an immobilized form on cell surfaces and in extracellular matrix. It is an important target for bacterial attachment in many pathogens, such as S. pyogenes, S. pneumoniae and L. monocytogenes, where fibronectin-binding proteins are important virulence factors. |
(fbpA/fbp68) fibronectin-binding protein FbpA [FbpA/Fbp68 (VF0595) - Adherence (VFC0001)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01002676.1_1 |
65.625 |
1.29E-34 |
slpA |
VF0589 |
SlpA |
Adherence |
VFC0001 |
S-layers have been observed in hundreds of prokaryotic species, including a diverse range of bacteria and virtually all archaea. A typical S-layer consists of a single protein arranged in a two dimensional paracrystalline array, forming the outermost surface of the cell;The majority of the C. difficile S-layer is formed by the low and high molecular weight S-layer proteins (LMW SLP and HMW SLP) which are coded by a single gene slpA;HMW SLP binds to the cell wall through a non-covalent interaction, while LMW SLP is presented as the outermost surface of the cell |
(slpA) cell surface protein (S-layer precursor protein) [SlpA (VF0589) - Adherence (VFC0001)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01002662.1_1 |
60.0 |
2.87E-6 |
CT_061 |
VF0711 |
TTSS secreted effectors |
Effector delivery system |
VFC0086 |
|
(CT_061) RNA polymerase sigma factor sigma-28 [TTSS secreted effectors (VF0711) - Effector delivery system (VFC0086)] [Chlamydia trachomatis D/UW-3/CX] |
Chlamydia trachomatis |
| ADEH01002607.1_2 |
90.909 |
1.19E-8 |
hasC |
VF0244 |
Hyaluronic acid capsule |
Immune modulation |
VFC0258 |
|
(hasC) UTP--glucose-1-phosphate uridylyltransferase HasC [Hyaluronic acid capsule (VF0244) - Immune modulation (VFC0258)] [Streptococcus pyogenes M1 GAS] |
Streptococcus pyogenes |
| ADEH01002582.1_1 |
100.0 |
9.55E-20 |
toxB |
VF0377 |
TcdB |
Exotoxin |
VFC0235 |
Many forms of variant toxin B have been identified, which are functional chimeras of toxin B (reference strain VPI 10463) and C. sordellii lethal toxin, e.g., C. difficile toxin B from strain 1470 and strain 8864. Their substrate specificities resemble that of lethal toxin. C. difficile strain C34 produces a toxin B variant modifying Rho, Rac, and Cdc42 as well as R-Ras, Ral, and Rap. |
(toxB) toxin B [TcdB (VF0377) - Exotoxin (VFC0235)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01002462.1_1 |
100.0 |
7.3E-51 |
toxA |
VF0376 |
TcdA |
Exotoxin |
VFC0235 |
The toxin genes tcdA and tcdB are situated on the C. difficile chromosome in a 19.6-kilobase (kb) pathogenicity locus (PaLoc), along with the three accessory genes tcdC, tcdR and tcdE.; TcdA and TcdB are homologous to each other, to TcsH and TcsL of C. sordellii and to Tcnalpha of C. novyi. Because of their sequence homology, similar domain structure and glycosyltransferase properties these toxins are designated 'large clostridial cytotoxins'. |
(toxA) toxin A [TcdA (VF0376) - Exotoxin (VFC0235)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01002462.1_2 |
97.814 |
2.74E-116 |
toxA |
VF0376 |
TcdA |
Exotoxin |
VFC0235 |
The toxin genes tcdA and tcdB are situated on the C. difficile chromosome in a 19.6-kilobase (kb) pathogenicity locus (PaLoc), along with the three accessory genes tcdC, tcdR and tcdE.; TcdA and TcdB are homologous to each other, to TcsH and TcsL of C. sordellii and to Tcnalpha of C. novyi. Because of their sequence homology, similar domain structure and glycosyltransferase properties these toxins are designated 'large clostridial cytotoxins'. |
(toxA) toxin A [TcdA (VF0376) - Exotoxin (VFC0235)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01002462.1_3 |
98.958 |
6.88E-57 |
toxA |
VF0376 |
TcdA |
Exotoxin |
VFC0235 |
The toxin genes tcdA and tcdB are situated on the C. difficile chromosome in a 19.6-kilobase (kb) pathogenicity locus (PaLoc), along with the three accessory genes tcdC, tcdR and tcdE.; TcdA and TcdB are homologous to each other, to TcsH and TcsL of C. sordellii and to Tcnalpha of C. novyi. Because of their sequence homology, similar domain structure and glycosyltransferase properties these toxins are designated 'large clostridial cytotoxins'. |
(toxA) toxin A [TcdA (VF0376) - Exotoxin (VFC0235)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01002437.1_1 |
66.667 |
5.9E-6 |
cwpV |
VF0596 |
CwpV |
Adherence |
VFC0001 |
CwpV is the largest member of the CWP family and consists of three distinct domains: (1) an N-terminal region with putative cell wall binding activity, (2) a region of unknown function terminating in a serine-glycine-rich flexible linker, (3) C-terminal domain; Five different types of CwpV have been described to date, each differing in its C-terminal domain. The characteristic feature of this domain is the presence of 4~9 tandem repeats of amino acids, each repeat comprising between 79 and 120 amino acids |
(cwpV) hemagglutinin/adhesin [CwpV (VF0596) - Adherence (VFC0001)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01002321.1_1 |
96.104 |
4.98E-43 |
toxA |
VF0376 |
TcdA |
Exotoxin |
VFC0235 |
The toxin genes tcdA and tcdB are situated on the C. difficile chromosome in a 19.6-kilobase (kb) pathogenicity locus (PaLoc), along with the three accessory genes tcdC, tcdR and tcdE.; TcdA and TcdB are homologous to each other, to TcsH and TcsL of C. sordellii and to Tcnalpha of C. novyi. Because of their sequence homology, similar domain structure and glycosyltransferase properties these toxins are designated 'large clostridial cytotoxins'. |
(toxA) toxin A [TcdA (VF0376) - Exotoxin (VFC0235)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01002321.1_2 |
91.429 |
6.67E-15 |
toxA |
VF0376 |
TcdA |
Exotoxin |
VFC0235 |
The toxin genes tcdA and tcdB are situated on the C. difficile chromosome in a 19.6-kilobase (kb) pathogenicity locus (PaLoc), along with the three accessory genes tcdC, tcdR and tcdE.; TcdA and TcdB are homologous to each other, to TcsH and TcsL of C. sordellii and to Tcnalpha of C. novyi. Because of their sequence homology, similar domain structure and glycosyltransferase properties these toxins are designated 'large clostridial cytotoxins'. |
(toxA) toxin A [TcdA (VF0376) - Exotoxin (VFC0235)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01002316.1_1 |
76.712 |
6.08E-29 |
ibp |
VF0381 |
Iota-toxin |
Exotoxin |
VFC0235 |
ADP-ribosylating toxin (ADPRT) family can be classified into four groups, at least with respect to their protein acceptors, as follows:; (I) heterotrimeric GTP-binding protein ADPRT (e.g. cholera toxin, B. pertussis pertussis toxin, E. coli heat-labile enterotoxin); (II) elongation factor 2 ADPRT (e.g. diphtheria toxin, P. aeruginosa exotoxin A); (III) small GTP-binding protein ADPRT (e.g. C. botulinum C3 exoenzyme, P. aeruginosa exoenzyme S); (IV) actin ADPRT. (e.g. B. cereus VIP, C. perfringens iota-toxin, C. botulinum C2 toxin, C. spiroforme toxin, and C. difficile toxin.); The binary iota toxin is produced exclusively by C. perfringens type E strains; The two proteins that comprise iota toxin were designated iota a or Ia (slower moving) and iota b or Ib (faster moving), based on electrophoretic mobility in crossed immunoelectrophoresis; Iota toxin requires proteolytic activation. The proteolytic activation of Ib precursor into Ib occurs at A211, which then facilitates Ia docking, formation of voltage-dependent ion-permeable channels in membranes, and formation of heptamers on cell membrane. Ia is also proteolytically activated by proteases, with a resultant loss of 9 to 13 amino acids from the N terminus. Proteolytic activation of Ia is unique among the 'A' components from binary toxins |
(ibp) iota toxin component Ib [Iota-toxin (VF0381) - Exotoxin (VFC0235)] [Clostridium perfringens E str. NCIB 10748] |
Clostridium perfringens |
| ADEH01002308.1_1 |
100.0 |
2.11E-15 |
toxA |
VF0376 |
TcdA |
Exotoxin |
VFC0235 |
The toxin genes tcdA and tcdB are situated on the C. difficile chromosome in a 19.6-kilobase (kb) pathogenicity locus (PaLoc), along with the three accessory genes tcdC, tcdR and tcdE.; TcdA and TcdB are homologous to each other, to TcsH and TcsL of C. sordellii and to Tcnalpha of C. novyi. Because of their sequence homology, similar domain structure and glycosyltransferase properties these toxins are designated 'large clostridial cytotoxins'. |
(toxA) toxin A [TcdA (VF0376) - Exotoxin (VFC0235)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01002216.1_1 |
98.039 |
1.57E-162 |
toxA |
VF0376 |
TcdA |
Exotoxin |
VFC0235 |
The toxin genes tcdA and tcdB are situated on the C. difficile chromosome in a 19.6-kilobase (kb) pathogenicity locus (PaLoc), along with the three accessory genes tcdC, tcdR and tcdE.; TcdA and TcdB are homologous to each other, to TcsH and TcsL of C. sordellii and to Tcnalpha of C. novyi. Because of their sequence homology, similar domain structure and glycosyltransferase properties these toxins are designated 'large clostridial cytotoxins'. |
(toxA) toxin A [TcdA (VF0376) - Exotoxin (VFC0235)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01002179.1_1 |
68.224 |
4.2E-47 |
cps4I |
VF0144 |
Capsule |
Immune modulation |
VFC0258 |
Ninety different capsule types have been identified. Each has a structurally distinct capsule, composed of repeating oligosaccharide units joined by glycosidic linkages |
(cps4I) capsular polysaccharide biosynthesis protein Cps4I [Capsule (VF0144) - Immune modulation (VFC0258)] [Streptococcus pneumoniae TIGR4] |
Streptococcus pneumoniae |
| ADEH01002014.1_1 |
100.0 |
1.72E-28 |
cbpA |
VF0592 |
CbpA |
Adherence |
VFC0001 |
MSCRAMMs have a common surface localization that in Gram-positive bacteria is usually mediated by a cell wall sorting signal through which they are covalently anchored to the cell wall peptidoglycan by sortase. |
(cbpA) collagen-binding adhesin CbpA [CbpA (VF0592) - Adherence (VFC0001)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01002008.1_3 |
64.706 |
1.66E-9 |
lap |
VF0444 |
Lap |
Adherence |
VFC0001 |
Originally named surface protein p104, is a 104 kDa adhesion protein, present in every Listeria spp. except L. grayi |
(lap) Listeria adhesion protein Lap [Lap (VF0444) - Adherence (VFC0001)] [Listeria monocytogenes EGD-e] |
Listeria monocytogenes |
| ADEH01001854.1_1 |
100.0 |
1.14E-82 |
CD0873 |
VF0593 |
CD0873 |
Adherence |
VFC0001 |
Numerous bacterial adhesins also characterized as lipoproteins, similar to CD0873, including the adhesin PsaA, a solute-binding lipoprotein of the Mn2+ ABC transporter of S. pneumoniae; CD0873 is annotated as a substrate-binding protein component SBP of an ABC transporter and is an immunoreactive protein in human infection |
(CD0873) ABC transporter substrate-binding protein [CD0873 (VF0593) - Adherence (VFC0001)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01001836.1_1 |
100.0 |
2.81E-12 |
zmp1 |
VF0600 |
Zmp1 |
Exoenzyme |
VFC0251 |
|
(zmp1) zinc metalloprotease Zmp1 [Zmp1 (VF0600) - Exoenzyme (VFC0251)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01001836.1_2 |
97.727 |
3.46E-23 |
zmp1 |
VF0600 |
Zmp1 |
Exoenzyme |
VFC0251 |
|
(zmp1) zinc metalloprotease Zmp1 [Zmp1 (VF0600) - Exoenzyme (VFC0251)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01001814.1_1 |
77.622 |
2.95E-69 |
slpA |
VF0589 |
SlpA |
Adherence |
VFC0001 |
S-layers have been observed in hundreds of prokaryotic species, including a diverse range of bacteria and virtually all archaea. A typical S-layer consists of a single protein arranged in a two dimensional paracrystalline array, forming the outermost surface of the cell;The majority of the C. difficile S-layer is formed by the low and high molecular weight S-layer proteins (LMW SLP and HMW SLP) which are coded by a single gene slpA;HMW SLP binds to the cell wall through a non-covalent interaction, while LMW SLP is presented as the outermost surface of the cell |
(slpA) cell surface protein (S-layer precursor protein) [SlpA (VF0589) - Adherence (VFC0001)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01001773.1_1 |
70.769 |
4.19E-28 |
hasC |
VF0244 |
Hyaluronic acid capsule |
Immune modulation |
VFC0258 |
|
(hasC) UTP--glucose-1-phosphate uridylyltransferase HasC [Hyaluronic acid capsule (VF0244) - Immune modulation (VFC0258)] [Streptococcus pyogenes M1 GAS] |
Streptococcus pyogenes |
| ADEH01001682.1_1 |
100.0 |
1.08E-18 |
cbpA |
VF0592 |
CbpA |
Adherence |
VFC0001 |
MSCRAMMs have a common surface localization that in Gram-positive bacteria is usually mediated by a cell wall sorting signal through which they are covalently anchored to the cell wall peptidoglycan by sortase. |
(cbpA) collagen-binding adhesin CbpA [CbpA (VF0592) - Adherence (VFC0001)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01001681.1_1 |
95.789 |
2.44E-55 |
cbpA |
VF0592 |
CbpA |
Adherence |
VFC0001 |
MSCRAMMs have a common surface localization that in Gram-positive bacteria is usually mediated by a cell wall sorting signal through which they are covalently anchored to the cell wall peptidoglycan by sortase. |
(cbpA) collagen-binding adhesin CbpA [CbpA (VF0592) - Adherence (VFC0001)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01001664.1_1 |
100.0 |
1.03E-145 |
CD3246 |
VF0599 |
CD3246 |
Adherence |
VFC0001 |
Cell surface protein cleaved and covalently anchored to m-DAP in the peptidoglycan by SrtB |
(CD3246) Cys-Gln thioester bond-forming surface protein [CD3246 (VF0599) - Adherence (VFC0001)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01001652.1_1 |
82.222 |
5.67E-18 |
cwpV |
VF0596 |
CwpV |
Adherence |
VFC0001 |
CwpV is the largest member of the CWP family and consists of three distinct domains: (1) an N-terminal region with putative cell wall binding activity, (2) a region of unknown function terminating in a serine-glycine-rich flexible linker, (3) C-terminal domain; Five different types of CwpV have been described to date, each differing in its C-terminal domain. The characteristic feature of this domain is the presence of 4~9 tandem repeats of amino acids, each repeat comprising between 79 and 120 amino acids |
(cwpV) hemagglutinin/adhesin [CwpV (VF0596) - Adherence (VFC0001)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01001652.1_2 |
95.939 |
1.17E-121 |
cwpV |
VF0596 |
CwpV |
Adherence |
VFC0001 |
CwpV is the largest member of the CWP family and consists of three distinct domains: (1) an N-terminal region with putative cell wall binding activity, (2) a region of unknown function terminating in a serine-glycine-rich flexible linker, (3) C-terminal domain; Five different types of CwpV have been described to date, each differing in its C-terminal domain. The characteristic feature of this domain is the presence of 4~9 tandem repeats of amino acids, each repeat comprising between 79 and 120 amino acids |
(cwpV) hemagglutinin/adhesin [CwpV (VF0596) - Adherence (VFC0001)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01001652.1_3 |
100.0 |
4.56E-40 |
cwpV |
VF0596 |
CwpV |
Adherence |
VFC0001 |
CwpV is the largest member of the CWP family and consists of three distinct domains: (1) an N-terminal region with putative cell wall binding activity, (2) a region of unknown function terminating in a serine-glycine-rich flexible linker, (3) C-terminal domain; Five different types of CwpV have been described to date, each differing in its C-terminal domain. The characteristic feature of this domain is the presence of 4~9 tandem repeats of amino acids, each repeat comprising between 79 and 120 amino acids |
(cwpV) hemagglutinin/adhesin [CwpV (VF0596) - Adherence (VFC0001)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01001594.1_1 |
92.593 |
1.81E-27 |
toxB |
VF0377 |
TcdB |
Exotoxin |
VFC0235 |
Many forms of variant toxin B have been identified, which are functional chimeras of toxin B (reference strain VPI 10463) and C. sordellii lethal toxin, e.g., C. difficile toxin B from strain 1470 and strain 8864. Their substrate specificities resemble that of lethal toxin. C. difficile strain C34 produces a toxin B variant modifying Rho, Rac, and Cdc42 as well as R-Ras, Ral, and Rap. |
(toxB) toxin B [TcdB (VF0377) - Exotoxin (VFC0235)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01001594.1_2 |
100.0 |
6.74E-34 |
toxB |
VF0377 |
TcdB |
Exotoxin |
VFC0235 |
Many forms of variant toxin B have been identified, which are functional chimeras of toxin B (reference strain VPI 10463) and C. sordellii lethal toxin, e.g., C. difficile toxin B from strain 1470 and strain 8864. Their substrate specificities resemble that of lethal toxin. C. difficile strain C34 produces a toxin B variant modifying Rho, Rac, and Cdc42 as well as R-Ras, Ral, and Rap. |
(toxB) toxin B [TcdB (VF0377) - Exotoxin (VFC0235)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01001594.1_3 |
99.315 |
5.83E-89 |
toxB |
VF0377 |
TcdB |
Exotoxin |
VFC0235 |
Many forms of variant toxin B have been identified, which are functional chimeras of toxin B (reference strain VPI 10463) and C. sordellii lethal toxin, e.g., C. difficile toxin B from strain 1470 and strain 8864. Their substrate specificities resemble that of lethal toxin. C. difficile strain C34 produces a toxin B variant modifying Rho, Rac, and Cdc42 as well as R-Ras, Ral, and Rap. |
(toxB) toxin B [TcdB (VF0377) - Exotoxin (VFC0235)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01001521.1_1 |
84.0 |
2.97E-9 |
flhB |
VF0051 |
Flagella |
Motility |
VFC0204 |
H. pylori typically produce 4-6 unipolar flagella, which are encased in a membranous sheath and capped by terminal bulbs |
(flhB) flagellar biosynthesis protein [Flagella (VF0051) - Motility (VFC0204)] [Helicobacter pylori 26695] |
Helicobacter pylori |
| ADEH01001426.1_1 |
63.333 |
1.38E-37 |
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 |
| ADEH01001419.1_1 |
98.427 |
0.0 |
toxB |
VF0377 |
TcdB |
Exotoxin |
VFC0235 |
Many forms of variant toxin B have been identified, which are functional chimeras of toxin B (reference strain VPI 10463) and C. sordellii lethal toxin, e.g., C. difficile toxin B from strain 1470 and strain 8864. Their substrate specificities resemble that of lethal toxin. C. difficile strain C34 produces a toxin B variant modifying Rho, Rac, and Cdc42 as well as R-Ras, Ral, and Rap. |
(toxB) toxin B [TcdB (VF0377) - Exotoxin (VFC0235)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01001405.1_1 |
72.368 |
1.36E-30 |
cwp84 |
VF0590 |
Cwp84 |
Exoenzyme |
VFC0251 |
|
(cwp84) cell wall-binding cysteine protease Cwp84 [Cwp84 (VF0590) - Exoenzyme (VFC0251)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01001319.1_2 |
63.636 |
1.58E-10 |
lap |
VF0444 |
Lap |
Adherence |
VFC0001 |
Originally named surface protein p104, is a 104 kDa adhesion protein, present in every Listeria spp. except L. grayi |
(lap) Listeria adhesion protein Lap [Lap (VF0444) - Adherence (VFC0001)] [Listeria monocytogenes EGD-e] |
Listeria monocytogenes |
| ADEH01001264.1_1 |
100.0 |
1.48E-47 |
toxB |
VF0377 |
TcdB |
Exotoxin |
VFC0235 |
Many forms of variant toxin B have been identified, which are functional chimeras of toxin B (reference strain VPI 10463) and C. sordellii lethal toxin, e.g., C. difficile toxin B from strain 1470 and strain 8864. Their substrate specificities resemble that of lethal toxin. C. difficile strain C34 produces a toxin B variant modifying Rho, Rac, and Cdc42 as well as R-Ras, Ral, and Rap. |
(toxB) toxin B [TcdB (VF0377) - Exotoxin (VFC0235)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01001231.1_2 |
64.789 |
2.14E-26 |
cwp66 |
VF0591 |
Cwp66 |
Adherence |
VFC0001 |
|
(cwp66) cell wall-binding protein Cwp66 [Cwp66 (VF0591) - Adherence (VFC0001)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01001222.1_1 |
99.569 |
2.67E-161 |
groEL |
VF0594 |
GroEL |
Adherence |
VFC0001 |
GroEL of numerous bacteria, such as L. pneumophila, H. pylori, H. ducreyi, M. avium, S. typhimurium, A. actinomycetemcomitans and B. burgdorferi, has been shown to be involved in adhesion or invasion of various target cells or tissues. |
(groEL) chaperonin GroEL [GroEL (VF0594) - Adherence (VFC0001)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01001133.1_1 |
99.145 |
1.31E-77 |
fbpA/fbp68 |
VF0595 |
FbpA/Fbp68 |
Adherence |
VFC0001 |
Fibronectin is a dimeric glycoprotein (~440 kDa) which is present in a soluble form in plasma and in an immobilized form on cell surfaces and in extracellular matrix. It is an important target for bacterial attachment in many pathogens, such as S. pyogenes, S. pneumoniae and L. monocytogenes, where fibronectin-binding proteins are important virulence factors. |
(fbpA/fbp68) fibronectin-binding protein FbpA [FbpA/Fbp68 (VF0595) - Adherence (VFC0001)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01001133.1_2 |
99.507 |
4.72E-143 |
fbpA/fbp68 |
VF0595 |
FbpA/Fbp68 |
Adherence |
VFC0001 |
Fibronectin is a dimeric glycoprotein (~440 kDa) which is present in a soluble form in plasma and in an immobilized form on cell surfaces and in extracellular matrix. It is an important target for bacterial attachment in many pathogens, such as S. pyogenes, S. pneumoniae and L. monocytogenes, where fibronectin-binding proteins are important virulence factors. |
(fbpA/fbp68) fibronectin-binding protein FbpA [FbpA/Fbp68 (VF0595) - Adherence (VFC0001)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01001133.1_3 |
98.913 |
4.67E-57 |
fbpA/fbp68 |
VF0595 |
FbpA/Fbp68 |
Adherence |
VFC0001 |
Fibronectin is a dimeric glycoprotein (~440 kDa) which is present in a soluble form in plasma and in an immobilized form on cell surfaces and in extracellular matrix. It is an important target for bacterial attachment in many pathogens, such as S. pyogenes, S. pneumoniae and L. monocytogenes, where fibronectin-binding proteins are important virulence factors. |
(fbpA/fbp68) fibronectin-binding protein FbpA [FbpA/Fbp68 (VF0595) - Adherence (VFC0001)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01001113.1_5 |
62.5 |
8.19E-9 |
purM |
VF0559 |
Purine biosynthesis |
Nutritional/Metabolic factor |
VFC0272 |
The purMCD locus encodes three enzymes (phosphoribosylaminoimidazol synthetase, SAICAR synthetase, and phosphoribosylamine-glycine ligase) required for the de novo synthesis of purine nucleotides. |
(purM) phosphoribosylaminoimidazole synthetase [Purine biosynthesis (VF0559) - Nutritional/Metabolic factor (VFC0272)] [Francisella tularensis subsp. tularensis SCHU S4] |
Francisella tularensis |
| ADEH01001038.1_1 |
100.0 |
0.0 |
toxB |
VF0377 |
TcdB |
Exotoxin |
VFC0235 |
Many forms of variant toxin B have been identified, which are functional chimeras of toxin B (reference strain VPI 10463) and C. sordellii lethal toxin, e.g., C. difficile toxin B from strain 1470 and strain 8864. Their substrate specificities resemble that of lethal toxin. C. difficile strain C34 produces a toxin B variant modifying Rho, Rac, and Cdc42 as well as R-Ras, Ral, and Rap. |
(toxB) toxin B [TcdB (VF0377) - Exotoxin (VFC0235)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01001038.1_2 |
100.0 |
2.5E-90 |
toxB |
VF0377 |
TcdB |
Exotoxin |
VFC0235 |
Many forms of variant toxin B have been identified, which are functional chimeras of toxin B (reference strain VPI 10463) and C. sordellii lethal toxin, e.g., C. difficile toxin B from strain 1470 and strain 8864. Their substrate specificities resemble that of lethal toxin. C. difficile strain C34 produces a toxin B variant modifying Rho, Rac, and Cdc42 as well as R-Ras, Ral, and Rap. |
(toxB) toxin B [TcdB (VF0377) - Exotoxin (VFC0235)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01000968.1_1 |
97.72 |
0.0 |
toxA |
VF0376 |
TcdA |
Exotoxin |
VFC0235 |
The toxin genes tcdA and tcdB are situated on the C. difficile chromosome in a 19.6-kilobase (kb) pathogenicity locus (PaLoc), along with the three accessory genes tcdC, tcdR and tcdE.; TcdA and TcdB are homologous to each other, to TcsH and TcsL of C. sordellii and to Tcnalpha of C. novyi. Because of their sequence homology, similar domain structure and glycosyltransferase properties these toxins are designated 'large clostridial cytotoxins'. |
(toxA) toxin A [TcdA (VF0376) - Exotoxin (VFC0235)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01000894.1_1 |
66.48 |
3.34E-81 |
cwp66 |
VF0591 |
Cwp66 |
Adherence |
VFC0001 |
|
(cwp66) cell wall-binding protein Cwp66 [Cwp66 (VF0591) - Adherence (VFC0001)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01000689.1_4 |
65.263 |
2.57E-93 |
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 |
| ADEH01000655.1_2 |
64.103 |
5.24E-13 |
pilR |
VF0082 |
Type IV pili |
Adherence |
VFC0001 |
PilA, B, C, D, E, F, M, N, O, P, Q, T, U, V, W, X, Y1, Y2, Z, and fimT, U, V are involved in the biogenesis and mechanical function of pili, pilG, H, I, K, chpA, B, C, D, E, pilS, R, fimS, rpoN, algR, algU, and vfr are involved in transcriptional regulation and chemosensory pathways that control the expression or activity of the twitching motility of the pili |
(pilR) two-component response regulator PilR [Type IV pili (VF0082) - Adherence (VFC0001)] [Pseudomonas aeruginosa PAO1] |
Pseudomonas aeruginosa |
| ADEH01000641.1_1 |
97.842 |
2.48E-84 |
cbpA |
VF0592 |
CbpA |
Adherence |
VFC0001 |
MSCRAMMs have a common surface localization that in Gram-positive bacteria is usually mediated by a cell wall sorting signal through which they are covalently anchored to the cell wall peptidoglycan by sortase. |
(cbpA) collagen-binding adhesin CbpA [CbpA (VF0592) - Adherence (VFC0001)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01000641.1_2 |
93.141 |
0.0 |
cbpA |
VF0592 |
CbpA |
Adherence |
VFC0001 |
MSCRAMMs have a common surface localization that in Gram-positive bacteria is usually mediated by a cell wall sorting signal through which they are covalently anchored to the cell wall peptidoglycan by sortase. |
(cbpA) collagen-binding adhesin CbpA [CbpA (VF0592) - Adherence (VFC0001)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01000641.1_3 |
100.0 |
2.38E-83 |
cbpA |
VF0592 |
CbpA |
Adherence |
VFC0001 |
MSCRAMMs have a common surface localization that in Gram-positive bacteria is usually mediated by a cell wall sorting signal through which they are covalently anchored to the cell wall peptidoglycan by sortase. |
(cbpA) collagen-binding adhesin CbpA [CbpA (VF0592) - Adherence (VFC0001)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01000563.1_2 |
62.141 |
2.03E-169 |
clpC |
VF0072 |
ClpC |
Stress survival |
VFC0282 |
27-kDa stress protein belongs to the Hsp100/Clp family; Regulation of Clp protease expression is mediated by CtsR, the product of the first gene in the ClpC operon |
(clpC) endopeptidase Clp ATP-binding chain C [ClpC (VF0072) - Stress survival (VFC0282)] [Listeria monocytogenes EGD-e] |
Listeria monocytogenes |
| ADEH01000424.1_2 |
96.203 |
1.4E-167 |
CD3246 |
VF0599 |
CD3246 |
Adherence |
VFC0001 |
Cell surface protein cleaved and covalently anchored to m-DAP in the peptidoglycan by SrtB |
(CD3246) Cys-Gln thioester bond-forming surface protein [CD3246 (VF0599) - Adherence (VFC0001)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01000406.1_1 |
85.714 |
4.74E-108 |
cwp66 |
VF0591 |
Cwp66 |
Adherence |
VFC0001 |
|
(cwp66) cell wall-binding protein Cwp66 [Cwp66 (VF0591) - Adherence (VFC0001)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01000375.1_1 |
100.0 |
4.02E-157 |
groEL |
VF0594 |
GroEL |
Adherence |
VFC0001 |
GroEL of numerous bacteria, such as L. pneumophila, H. pylori, H. ducreyi, M. avium, S. typhimurium, A. actinomycetemcomitans and B. burgdorferi, has been shown to be involved in adhesion or invasion of various target cells or tissues. |
(groEL) chaperonin GroEL [GroEL (VF0594) - Adherence (VFC0001)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01000358.1_3 |
68.293 |
3.55E-16 |
feoB |
VF0160 |
FeoAB |
Nutritional/Metabolic factor |
VFC0272 |
|
(feoB) ferrous iron transporter B [FeoAB (VF0160) - Nutritional/Metabolic factor (VFC0272)] [Legionella pneumophila subsp. pneumophila str. Philadelphia 1] |
Legionella pneumophila |
| ADEH01000331.1_2 |
97.849 |
1.05E-60 |
cwp84 |
VF0590 |
Cwp84 |
Exoenzyme |
VFC0251 |
|
(cwp84) cell wall-binding cysteine protease Cwp84 [Cwp84 (VF0590) - Exoenzyme (VFC0251)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01000331.1_3 |
100.0 |
3.05E-157 |
cwp84 |
VF0590 |
Cwp84 |
Exoenzyme |
VFC0251 |
|
(cwp84) cell wall-binding cysteine protease Cwp84 [Cwp84 (VF0590) - Exoenzyme (VFC0251)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01000331.1_4 |
96.68 |
1.41E-164 |
cwp84 |
VF0590 |
Cwp84 |
Exoenzyme |
VFC0251 |
|
(cwp84) cell wall-binding cysteine protease Cwp84 [Cwp84 (VF0590) - Exoenzyme (VFC0251)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01000331.1_5 |
95.588 |
1.61E-37 |
cwp84 |
VF0590 |
Cwp84 |
Exoenzyme |
VFC0251 |
|
(cwp84) cell wall-binding cysteine protease Cwp84 [Cwp84 (VF0590) - Exoenzyme (VFC0251)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01000331.1_6 |
97.887 |
1.26E-90 |
cwp84 |
VF0590 |
Cwp84 |
Exoenzyme |
VFC0251 |
|
(cwp84) cell wall-binding cysteine protease Cwp84 [Cwp84 (VF0590) - Exoenzyme (VFC0251)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01000223.1_14 |
73.3 |
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 |
| ADEH01000186.1_1 |
98.765 |
6.09E-51 |
CD2831 |
VF0598 |
CD2831 |
Adherence |
VFC0001 |
Cell surface protein cleaved and covalently anchored to m-DAP in the peptidoglycan by SrtB |
(CD2831) SrtB-anchored collagen-binding adhesin [CD2831 (VF0598) - Adherence (VFC0001)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01000186.1_2 |
99.578 |
1.6E-164 |
CD2831 |
VF0598 |
CD2831 |
Adherence |
VFC0001 |
Cell surface protein cleaved and covalently anchored to m-DAP in the peptidoglycan by SrtB |
(CD2831) SrtB-anchored collagen-binding adhesin [CD2831 (VF0598) - Adherence (VFC0001)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01000186.1_3 |
100.0 |
9.86E-14 |
CD2831 |
VF0598 |
CD2831 |
Adherence |
VFC0001 |
Cell surface protein cleaved and covalently anchored to m-DAP in the peptidoglycan by SrtB |
(CD2831) SrtB-anchored collagen-binding adhesin [CD2831 (VF0598) - Adherence (VFC0001)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01000186.1_4 |
93.478 |
1.7E-53 |
CD2831 |
VF0598 |
CD2831 |
Adherence |
VFC0001 |
Cell surface protein cleaved and covalently anchored to m-DAP in the peptidoglycan by SrtB |
(CD2831) SrtB-anchored collagen-binding adhesin [CD2831 (VF0598) - Adherence (VFC0001)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01000186.1_5 |
90.909 |
4.51E-23 |
CD2831 |
VF0598 |
CD2831 |
Adherence |
VFC0001 |
Cell surface protein cleaved and covalently anchored to m-DAP in the peptidoglycan by SrtB |
(CD2831) SrtB-anchored collagen-binding adhesin [CD2831 (VF0598) - Adherence (VFC0001)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01000165.1_1 |
100.0 |
1.03E-36 |
toxA |
VF0376 |
TcdA |
Exotoxin |
VFC0235 |
The toxin genes tcdA and tcdB are situated on the C. difficile chromosome in a 19.6-kilobase (kb) pathogenicity locus (PaLoc), along with the three accessory genes tcdC, tcdR and tcdE.; TcdA and TcdB are homologous to each other, to TcsH and TcsL of C. sordellii and to Tcnalpha of C. novyi. Because of their sequence homology, similar domain structure and glycosyltransferase properties these toxins are designated 'large clostridial cytotoxins'. |
(toxA) toxin A [TcdA (VF0376) - Exotoxin (VFC0235)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01000163.1_1 |
99.206 |
3.86E-83 |
toxA |
VF0376 |
TcdA |
Exotoxin |
VFC0235 |
The toxin genes tcdA and tcdB are situated on the C. difficile chromosome in a 19.6-kilobase (kb) pathogenicity locus (PaLoc), along with the three accessory genes tcdC, tcdR and tcdE.; TcdA and TcdB are homologous to each other, to TcsH and TcsL of C. sordellii and to Tcnalpha of C. novyi. Because of their sequence homology, similar domain structure and glycosyltransferase properties these toxins are designated 'large clostridial cytotoxins'. |
(toxA) toxin A [TcdA (VF0376) - Exotoxin (VFC0235)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01000162.1_1 |
100.0 |
1.06E-53 |
toxA |
VF0376 |
TcdA |
Exotoxin |
VFC0235 |
The toxin genes tcdA and tcdB are situated on the C. difficile chromosome in a 19.6-kilobase (kb) pathogenicity locus (PaLoc), along with the three accessory genes tcdC, tcdR and tcdE.; TcdA and TcdB are homologous to each other, to TcsH and TcsL of C. sordellii and to Tcnalpha of C. novyi. Because of their sequence homology, similar domain structure and glycosyltransferase properties these toxins are designated 'large clostridial cytotoxins'. |
(toxA) toxin A [TcdA (VF0376) - Exotoxin (VFC0235)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01000161.1_1 |
99.038 |
3.15E-70 |
toxB |
VF0377 |
TcdB |
Exotoxin |
VFC0235 |
Many forms of variant toxin B have been identified, which are functional chimeras of toxin B (reference strain VPI 10463) and C. sordellii lethal toxin, e.g., C. difficile toxin B from strain 1470 and strain 8864. Their substrate specificities resemble that of lethal toxin. C. difficile strain C34 produces a toxin B variant modifying Rho, Rac, and Cdc42 as well as R-Ras, Ral, and Rap. |
(toxB) toxin B [TcdB (VF0377) - Exotoxin (VFC0235)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01000161.1_2 |
100.0 |
4.48E-84 |
toxB |
VF0377 |
TcdB |
Exotoxin |
VFC0235 |
Many forms of variant toxin B have been identified, which are functional chimeras of toxin B (reference strain VPI 10463) and C. sordellii lethal toxin, e.g., C. difficile toxin B from strain 1470 and strain 8864. Their substrate specificities resemble that of lethal toxin. C. difficile strain C34 produces a toxin B variant modifying Rho, Rac, and Cdc42 as well as R-Ras, Ral, and Rap. |
(toxB) toxin B [TcdB (VF0377) - Exotoxin (VFC0235)] [Clostridium difficile 630] |
Clostridium difficile |
| ADEH01000096.1_2 |
71.779 |
6.53E-87 |
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 |
| ADEH01000061.1_1 |
71.429 |
1.68E-41 |
ibp |
VF0381 |
Iota-toxin |
Exotoxin |
VFC0235 |
ADP-ribosylating toxin (ADPRT) family can be classified into four groups, at least with respect to their protein acceptors, as follows:; (I) heterotrimeric GTP-binding protein ADPRT (e.g. cholera toxin, B. pertussis pertussis toxin, E. coli heat-labile enterotoxin); (II) elongation factor 2 ADPRT (e.g. diphtheria toxin, P. aeruginosa exotoxin A); (III) small GTP-binding protein ADPRT (e.g. C. botulinum C3 exoenzyme, P. aeruginosa exoenzyme S); (IV) actin ADPRT. (e.g. B. cereus VIP, C. perfringens iota-toxin, C. botulinum C2 toxin, C. spiroforme toxin, and C. difficile toxin.); The binary iota toxin is produced exclusively by C. perfringens type E strains; The two proteins that comprise iota toxin were designated iota a or Ia (slower moving) and iota b or Ib (faster moving), based on electrophoretic mobility in crossed immunoelectrophoresis; Iota toxin requires proteolytic activation. The proteolytic activation of Ib precursor into Ib occurs at A211, which then facilitates Ia docking, formation of voltage-dependent ion-permeable channels in membranes, and formation of heptamers on cell membrane. Ia is also proteolytically activated by proteases, with a resultant loss of 9 to 13 amino acids from the N terminus. Proteolytic activation of Ia is unique among the 'A' components from binary toxins |
(ibp) iota toxin component Ib [Iota-toxin (VF0381) - Exotoxin (VFC0235)] [Clostridium perfringens E str. NCIB 10748] |
Clostridium perfringens |
| ADEH01000061.1_2 |
77.778 |
9.59E-29 |
ibp |
VF0381 |
Iota-toxin |
Exotoxin |
VFC0235 |
ADP-ribosylating toxin (ADPRT) family can be classified into four groups, at least with respect to their protein acceptors, as follows:; (I) heterotrimeric GTP-binding protein ADPRT (e.g. cholera toxin, B. pertussis pertussis toxin, E. coli heat-labile enterotoxin); (II) elongation factor 2 ADPRT (e.g. diphtheria toxin, P. aeruginosa exotoxin A); (III) small GTP-binding protein ADPRT (e.g. C. botulinum C3 exoenzyme, P. aeruginosa exoenzyme S); (IV) actin ADPRT. (e.g. B. cereus VIP, C. perfringens iota-toxin, C. botulinum C2 toxin, C. spiroforme toxin, and C. difficile toxin.); The binary iota toxin is produced exclusively by C. perfringens type E strains; The two proteins that comprise iota toxin were designated iota a or Ia (slower moving) and iota b or Ib (faster moving), based on electrophoretic mobility in crossed immunoelectrophoresis; Iota toxin requires proteolytic activation. The proteolytic activation of Ib precursor into Ib occurs at A211, which then facilitates Ia docking, formation of voltage-dependent ion-permeable channels in membranes, and formation of heptamers on cell membrane. Ia is also proteolytically activated by proteases, with a resultant loss of 9 to 13 amino acids from the N terminus. Proteolytic activation of Ia is unique among the 'A' components from binary toxins |
(ibp) iota toxin component Ib [Iota-toxin (VF0381) - Exotoxin (VFC0235)] [Clostridium perfringens E str. NCIB 10748] |
Clostridium perfringens |
| ADEH01000018.1_1 |
60.465 |
2.08E-12 |
flgR |
VF0114 |
Flagella |
Motility |
VFC0204 |
Two different (approximately 59-kDa) flagellin subunits, FlaA and FlaB are subject to both antigenic variation and phase variation; The expression of FlaA and FlaB is controlled by different transcription factors, namely the alternative sigma28 (FlaA) and sigma54 (FlaB) transcription factors; post-translationally modified through O-linked glycosylation. The major modification are pseudaminic acid (Pse5Ac7Ac), a nine carbon sugar that is similar to sialic acid, and an acetamidino-substituted pseudaminic acid (PseAm). There are also minor amounts of a dihydroxyproprionyl form (Pse5Pr7Pr) and an O-acetylated form (Pse5Ac7Ac8OAc); the exact role of glycosylation is unknown. The modification appears to be important for flagellar assembly and may be required for recognition by the flagellar secretion/assembly apparatus |
(flgR) sigma-54 associated transcriptional activator [Flagella (VF0114) - Motility (VFC0204)] [Campylobacter jejuni subsp. jejuni NCTC 11168] |
Campylobacter jejuni |