methionine aminopeptidase
function
removal of N-terminal methionine from nascent proteins
product
methionine aminopeptidase
Genomic Context
categories
[category|SW 3|Information processing] → [category|SW 3.3|Protein synthesis, modification and degradation] → [category|SW 3.3.1|Translation] → [category|SW 3.3.1.12|Translation/ other][category|SW 3|Information processing] → [category|SW 3.3|Protein synthesis, modification and degradation] → [category|SW 3.3.4|Protein modification] → [category|SW 3.3.4.1|Protein maturation][SW|Categories] containing this gene/protein
[SW|translation], [SW|protein modification], [SW|essential genes]This gene is a member of the following [SW|regulons]
[SW|stringent response]Gene
Coordinates on the chromosome (coding sequence)
146,527 -> 147,273
Phenotypes of a mutant
essential [Pubmed|12682299], non-essential according to [Pubmed|28189581]The protein
Catalyzed reaction/ biological activity
Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides (according to Swiss-Prot)Protein family
peptidase M24A family (according to Swiss-Prot)Paralogous protein(s)
[protein|search|YflG]Structure
[PDB|2MAT] (from ''Escherichia coli'', 46% identity, 65% similarity) [Pubmed|10387007][SW|Localization]
cytoplasm (according to Swiss-Prot)[SW|Interactions]
[protein|search|Map]-[protein|search|RplQ] [Pubmed|23770820][protein|search|Map]-[protein|search|RplW] [Pubmed|23770820][protein|search|Map] competes with peptide deformylase ([protein|search|DefA]), the first enzyme to act on nascent chains, for binding sites at the ribosomal tunnel exit [Pubmed|23770820]Expression and Regulation
Regulation
[protein|search|RelA] dependent downregulation (Class I) during stringent response [Pubmed|11948165]Additional information
strongly expressedReferences
16207374,8635744,23770820,28189581 
