Q824C7
Gene name |
clpP1 |
Protein name |
ATP-dependent Clp protease proteolytic subunit 1 |
Names |
Endopeptidase Clp 1 |
Species |
Chlamydia caviae (strain ATCC VR-813 / DSM 19441 / 03DC25 / GPIC) (Chlamydophila caviae) |
KEGG Pathway |
cca:CCA_00225 |
EC number |
3.4.21.92: Serine endopeptidases |
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 Q824C7
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q824C7-F1 | Predicted | AlphaFoldDB |
No variants for Q824C7
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q824C7 | |||||
No associated diseases with Q824C7
1 regional properties for Q824C7
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| active_site | ClpP, histidine active site | 105 - 118 | IPR033135 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.4.21.92 | Serine endopeptidases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP-dependent peptidase activity | Catalysis of the hydrolysis of peptide bonds, driven by ATP hydrolysis. |
| serine-type endopeptidase activity | Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine). |
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 |
| MPDGEVNKLR | DVIDKKILDA | RRVFFSEPVT | DKSAADAIKK | LWYLELSHPG | QPIVFVINSP |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GGSVDAGFAV | WDQIKMMTSP | VTTVVTGLAA | SMGSVLSLCA | APGRRFATPH | SRIMIHQPSI |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GGPITGQATD | LDIHAREILK | TKKRIVDVYL | EATGQPREVI | EKAIDRDMWM | TADEAKDFGL |
| 190 | |||||
| LDGILFSFDD | L |