| AM180355.1_62 |
74.559 |
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 |
| AM180355.1_76 |
74.559 |
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 |
| AM180355.1_206 |
100.0 |
0.0 |
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 |
| AM180355.1_528 |
100.0 |
0.0 |
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 |
| AM180355.1_674 |
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 |
| AM180355.1_677 |
100.0 |
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 |
| AM180355.1_889 |
100.0 |
0.0 |
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 |
| AM180355.1_892 |
69.501 |
1.22E-175 |
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 |
| AM180355.1_1059 |
60.833 |
4.79E-169 |
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 |
| AM180355.1_1812 |
63.057 |
0.0 |
cwp84 |
VF0590 |
Cwp84 |
Exoenzyme |
VFC0251 |
|
(cwp84) cell wall-binding cysteine protease Cwp84 [Cwp84 (VF0590) - Exoenzyme (VFC0251)] [Clostridium difficile 630] |
Clostridium difficile |
| AM180355.1_2687 |
100.0 |
0.0 |
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 |
| AM180355.1_2699 |
100.0 |
1.06E-40 |
cdtA |
VF0385 |
CDT |
Exotoxin |
VFC0235 |
CDT is an iota-like toxin, consisting of CDTa and CDTb components that respectively share 80 and 82% amino acid sequence identity to C. perfringens Ia and Ib.; The binding component CDTb becomes active only after trypsinization. The N terminal part of CDTa is involved in interaction with the binding component. The C-terminal part of CDTa harbours the enzymatic activity. |
(cdtA) CdtA [CDT (VF0385) - Exotoxin (VFC0235)] [Clostridium difficile 630] |
Clostridium difficile |
| AM180355.1_2700 |
79.365 |
1.44E-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 |
| AM180355.1_2701 |
73.171 |
5.46E-38 |
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 |
| AM180355.1_2702 |
63.83 |
9.33E-34 |
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 |
| AM180355.1_2883 |
100.0 |
0.0 |
cwp84 |
VF0590 |
Cwp84 |
Exoenzyme |
VFC0251 |
|
(cwp84) cell wall-binding cysteine protease Cwp84 [Cwp84 (VF0590) - Exoenzyme (VFC0251)] [Clostridium difficile 630] |
Clostridium difficile |
| AM180355.1_2885 |
100.0 |
0.0 |
cwp66 |
VF0591 |
Cwp66 |
Adherence |
VFC0001 |
|
(cwp66) cell wall-binding protein Cwp66 [Cwp66 (VF0591) - Adherence (VFC0001)] [Clostridium difficile 630] |
Clostridium difficile |
| AM180355.1_2889 |
100.0 |
0.0 |
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 |
| AM180355.1_2926 |
100.0 |
1.92E-165 |
zmp1 |
VF0600 |
Zmp1 |
Exoenzyme |
VFC0251 |
|
(zmp1) zinc metalloprotease Zmp1 [Zmp1 (VF0600) - Exoenzyme (VFC0251)] [Clostridium difficile 630] |
Clostridium difficile |
| AM180355.1_2927 |
100.0 |
0.0 |
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 |
| AM180355.1_3256 |
100.0 |
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 |
| AM180355.1_3367 |
100.0 |
0.0 |
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 |
| AM180355.1_3427 |
69.43 |
7.02E-101 |
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 |
| AM180355.1_3473 |
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 |