|
|
||
|
|
|
|
|
UniProt functional annotation for P04825 | ||
|
|
|
|
|
|
||
| UniProt code: P04825. |
|
||
| Organism: | |
Escherichia coli (strain K12). |
| Taxonomy: | |
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia. |
|
||
|
||
| Function: | |
Aminopeptidase N is involved in the degradation of intracellular peptides generated by protein breakdown during normal growth as well as in response to nutrient starvation. {ECO:0000269|PubMed:16885166, ECO:0000269|PubMed:18416562, ECO:0000269|PubMed:19622865, ECO:0000305|PubMed:20067529}. |
|
||
| Catalytic activity: | |
Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.; EC=3.4.11.2; Evidence={ECO:0000269|PubMed:16885166, ECO:0000269|PubMed:18416562, ECO:0000269|PubMed:19622865}; |
| Cofactor: | |
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:16885166, ECO:0000269|PubMed:18416562, ECO:0000269|PubMed:19622865}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:16885166, ECO:0000269|PubMed:18416562, ECO:0000269|PubMed:19622865}; |
| Subcellular location: | |
Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. |
| Disruption phenotype: | |
A quadruple peptidase disruption (pepA, pepB, pepD and pepN) does not grow in M9 minimal medium, does grow better when supplemented with casamino acids (PubMed:20067529). {ECO:0000269|PubMed:20067529}. |
| Similarity: | |
Belongs to the peptidase M1 family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.