Q9RRU7
Gene name |
lspA |
Protein name |
Lipoprotein signal peptidase |
Names |
Prolipoprotein signal peptidase, Signal peptidase II, SPase II |
Species |
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422) |
KEGG Pathway |
dra:DR_2388 |
EC number |
3.4.23.36: Aspartic 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 Q9RRU7
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9RRU7-F1 | Predicted | AlphaFoldDB |
No variants for Q9RRU7
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9RRU7 | |||||
No associated diseases with Q9RRU7
No regional properties for Q9RRU7
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q9RRU7 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 3.4.23.36 | Aspartic endopeptidases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
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. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| aspartic-type endopeptidase activity | Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which a water molecule bound by the side chains of aspartic residues at the active center acts as a nucleophile. |
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 |
| MWPFSRQQNV | SRILPIVPTA | PRRFPVWFPA | VLVLVLIALD | QWLKAWALAH | LQLNAPAIPV |
| 70 | 80 | 90 | 100 | 110 | 120 |
| IPGVLDWELT | FNTGAAWSMF | SGSAVPLALG | RILVGLGILS | YLLWKPQGRF | LTVVLSMIAA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GAIGNSIDGL | QRGQVTDMIH | SPLLSAVTEA | INGTRFPIFN | IADMCVVGGT | ILLLVASLLP |
| 190 | |||||
| ERKREKAVPE | A |