Q9KPV9
Gene name |
VC_2253 |
Protein name |
Putative zinc metalloprotease VC_2253 |
Names |
|
Species |
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) |
KEGG Pathway |
vch:VC_2253 |
EC number |
|
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q9KPV9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9KPV9-F1 | Predicted | AlphaFoldDB |
No variants for Q9KPV9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9KPV9 | |||||
No associated diseases with Q9KPV9
5 regional properties for Q9KPV9
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | PDZ domain | 115 - 186 | IPR001478-1 |
| domain | PDZ domain | 212 - 292 | IPR001478-2 |
| domain | Peptidase M50 | 10 - 184 | IPR008915-1 |
| domain | Peptidase M50 | 220 - 440 | IPR008915-2 |
| domain | PDZ domain 6 | 228 - 279 | IPR041489 |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| integral component of membrane | The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| metal ion binding | Binding to a metal ion. |
| metalloendopeptidase activity | Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| proteolysis | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTDILWNFIA | FIIALGILVA | VHEFGHFWVA | RRCGVKVEKF | SIGFGKSIWK | RVGHDGTEYS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ISMIPLGGYV | KMLDGRVDDV | PAEQQAMAFD | KQSLWKRSAI | VSAGPIFNFL | FAIFAYWLVF |
| 130 | 140 | 150 | 160 | 170 | 180 |
| MIGVPAVKPV | IGEVTPYSIA | AQAGLEPGME | IKAVSGVNTP | DWESVNMGLI | GHIGDDSMTI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| TVSSAEGVGL | NEIKTINLRD | WNFDPETESA | MGALGFKPFT | PEISNQLTNV | SAQGAGERAG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LQVGDTVLQI | NGQAVEAWQQ | VVNAIQSHPN | APIAVMVERA | GQQVELTLIP | DSRELSQGKV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| IGFAGIAPKV | AEWPQNYRFE | LQFGVFESLG | KAVEKSGQVI | DLTVSMLKKL | LVGDVGLNNL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| SGPISIAKGA | GTTADYGFVY | FLGFLALISI | NLGIINLVPL | PMLDGGHLLF | FMIEAVIRRP |
| 430 | 440 | 450 | |||
| VPEKVQEMGY | RIGGAIIFSL | MAVAIFNDFT | RL |