P32762
Gene name |
HBL |
Protein name |
Lytic amidase |
Names |
N-acetylmuramoyl-L-alanine amidase |
Species |
Streptococcus pneumoniae phage HB-3 |
KEGG Pathway |
|
EC number |
3.5.1.28: In linear amides |
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
0 structures for P32762
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|
No variants for P32762
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P32762 | |||||
No associated diseases with P32762
4 regional properties for P32762
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | N-acetylmuramoyl-L-alanine amidase domain | 10 - 153 | IPR002502 |
| repeat | Cell wall/choline-binding repeat | 196 - 215 | IPR018337-1 |
| repeat | Cell wall/choline-binding repeat | 217 - 237 | IPR018337-2 |
| repeat | Cell wall/choline-binding repeat | 238 - 283 | IPR018337-3 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.5.1.28 | In linear amides |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| extracellular region | The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| N-acetylmuramoyl-L-alanine amidase activity | Catalysis of the hydrolysis of the link between N-acetylmuramoyl residues and L-amino acid residues in certain bacterial cell-wall glycopeptides. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| cell wall organization | A process that results in the assembly, arrangement of constituent parts, or disassembly of the cell wall, the rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal and most prokaryotic cells, maintaining their shape and protecting them from osmotic lysis. |
| cytolysis | The rupture of cell membranes and the loss of cytoplasm. |
| defense response to bacterium | Reactions triggered in response to the presence of a bacterium that act to protect the cell or organism. |
| peptidoglycan catabolic process | The chemical reactions and pathways resulting in the breakdown of peptidoglycans, any of a class of glycoconjugates found in bacterial cell walls. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MDIDRNRLRT | GLPQVGVQPY | RQVHAHSTGN | RNSTVQNEAD | YHWRKDPELG | FFSHVVGNFR |
| 70 | 80 | 90 | 100 | 110 | 120 |
| IMQVGPVNNG | SWDVGGGWNA | ETYAAVELIE | SHSTKEEFMA | DYRLYIELLR | NLADEAGLPK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| TLDTDDLAGI | KTHEYCTNNQ | PNNHSDHVDP | YPYLASWGIS | REQFKQDIEN | GLSAATGWQK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| NGTGYWYVHS | DGSYSKDKFE | KINGTWYYFD | GSGYMLSDRW | KKHTDGNWYY | FDQSGEMATG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| WKKIADKWYY | FDVEGAMKTG | WVKYKDTWYY | LDAKEGAMVS | NAFIQSADGT | GWYYLKPDGT |
| 310 | |||||
| LADKPEFTVE | PDGLITVK |