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VIBCH:Q9KSQ6
Contents
Species (Taxon ID) | Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961). (243277) | |
Gene Name(s) | No Information Provided. | |
Protein Name(s) | Trypsin, putative (ECO:0000313 with EMBL:AAF94359.1) | |
External Links | ||
UniProt | Q9KSQ6 | |
EMBL | AE003852 | |
PIR | C82228 | |
RefSeq | NP_230845.1 | |
PDB | 4LK4 | |
PDBsum | 4LK4 | |
ProteinModelPortal | Q9KSQ6 | |
STRING | 243277.VC1200 | |
MEROPS | S01.516 | |
DNASU | 2614633 | |
EnsemblBacteria | AAF94359 | |
GeneID | 2614633 | |
KEGG | vch:VC1200 | |
PATRIC | 20081488 | |
OMA | WIKSNLV | |
OrthoDB | EOG6VMTQS | |
BioCyc | VCHO:VC1200-MONOMER | |
Proteomes | UP000000584 | |
GO | GO:0004252 GO:0006508 | |
InterPro | IPR020008 IPR001254 IPR018114 IPR001314 IPR009003 | |
Pfam | PF00089 | |
PRINTS | PR00722 | |
SMART | SM00020 | |
SUPFAM | SSF50494 | |
TIGRFAMs | TIGR03501 | |
PROSITE | PS50240 PS00134 PS00135 |
Annotations
Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|---|---|
GO:0008236 |
serine-type peptidase activity |
ECO:0000315 |
F |
Figure 2B shows that there is a dramatic decrease in hydrolase activity when VesB is knocked out. This indicates that VesB is responsible for the hydrolase activity in the wild type Vibrio cholerae. Hydrolysis was tested for using a peptide as substrate, and therefore it is a peptidase. In addition Figure 3B show that the serine protease inhibitor AEBSF and the serine/cysteine protease inhibitor significantly inhibited the VesB protein. |
complete | |||||
GO:0051605 |
protein maturation by peptide bond cleavage |
ECO:0000315 |
P |
Figures 5 & 6 show that VesB is involved in processing the cholera toxin A subunit. In absence of VesB, the cholera toxin A subunit remained largely uncleaved. This is also discussed in results and discussion |
complete | |||||
GO:0005615 |
extracellular space |
ECO:0000314 |
C |
Supernatant and cell extracts from three different bacteria culture strains(VesA,VesB,VesC) were subject to SDS-Page and Western blot using anti-VesB antibodies to demonstrate secretion. Figure 4b |
complete | |||||
GO:0008236 |
serine-type peptidase activity |
ECO:0000315 |
F |
When subjected to serine protease inhibitors, its protease activity was effected.Figure 2 Protease activity was measured using different commercially available synthetic peptides to determine substrate specificity and subjected to a serine peptidase specific inhibitor. Figure 3A and 3B |
complete | |||||
enables |
GO:0008236 |
serine-type peptidase activity |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0006508 |
proteolysis |
ECO:0000250 |
sequence similarity evidence used in manual assertion |
P |
Seeded From UniProt |
Missing: with/from | |||
enables |
GO:0004252 |
serine-type endopeptidase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0006508 |
proteolysis |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
part_of |
GO:0016020 |
membrane |
ECO:0000323 |
imported automatically asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
involved_in |
GO:0006508 |
proteolysis |
ECO:0000323 |
imported automatically asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0008233 |
peptidase activity |
ECO:0000323 |
imported automatically asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
part_of |
GO:0016021 |
integral component of membrane |
ECO:0000323 |
imported automatically asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
enables |
GO:0008236 |
serine-type peptidase activity |
ECO:0000323 |
imported automatically asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0016787 |
hydrolase activity |
ECO:0000323 |
imported automatically asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 Sikora, AE et al. (2011) Proteomic analysis of the Vibrio cholerae type II secretome reveals new proteins, including three related serine proteases. J. Biol. Chem. 286 16555-66 PubMed GONUTS page
- ↑ 2.0 2.1 2.2 Gadwal, S et al. (2014) Functional and structural characterization of Vibrio cholerae extracellular serine protease B, VesB. J. Biol. Chem. 289 8288-98 PubMed GONUTS page
- ↑ Heidelberg, JF et al. (2000) DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae. Nature 406 477-83 PubMed GONUTS page