Q13D27
Gene name |
htpX |
Protein name |
Protease HtpX homolog |
Names |
|
Species |
Rhodopseudomonas palustris (strain BisB5) |
KEGG Pathway |
rpd:RPD_0774 |
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 Q13D27
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q13D27-F1 | Predicted | AlphaFoldDB |
No variants for Q13D27
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q13D27 | |||||
No associated diseases with Q13D27
1 regional properties for Q13D27
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Peptidase M48 | 66 - 277 | IPR001915 |
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 |
|---|---|
| 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. |
| zinc ion binding | Binding to a zinc ion (Zn). |
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 |
| MSYFKTAMLL | AGLTALFMGI | GYLIGGASGA | LIALVVAAAM | NVFTYWNSDR | MVLSMYGAQE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VDVRSAPDLV | RMVAELAGRA | GLPMPRVFIM | DNPQPNAFAT | GRNPENAAVA | VTTGLMQQLS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| REELAGVIAH | ELAHVKNHDT | LLMTITATIA | GAISMVAQFG | MFFGGNRENN | NGPGLIGSLA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LMILAPLGAM | LVQMAISRTR | EYAADEMGAR | ICGQPMWLAS | ALGRIDAAAH | QVPNVEAERA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| PATAHMFIIN | PLSGQGMDNL | FATHPSTQNR | IAALQRLTGE | IGGGGASIGR | PAGPSPRGAP |
| 310 | |||||
| RSPWSGQPRA | RGPWG |