CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003440
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Methionine aminopeptidase 
Protein Synonyms/Alias
 MAP; MetAP; Peptidase M 
Gene Name
 map 
Gene Synonyms/Alias
 b0168; JW0163 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
13KTPEDIEKMRVAGRLacetylation[1]
89PDDAKLLKDGDIVNIacetylation[1]
117SKMFIVGKPTIMGERacetylation[1]
141YLALRMVKPGINLREacetylation[1]
155EIGAAIQKFVEAEGFacetylation[1]
196RETNVVLKPGMTFTIacetylation[1]
218KKEIRTMKDGWTVKTacetylation[1]
224MKDGWTVKTKDRSLSacetylation[1]
226DGWTVKTKDRSLSAQacetylation[1]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618
Functional Description
 Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed. 
Sequence Annotation
 METAL 97 97 Divalent metal cation 1.
 METAL 108 108 Divalent metal cation 1.
 METAL 108 108 Divalent metal cation 2; catalytic.
 METAL 171 171 Divalent metal cation 2; catalytic; via
 METAL 204 204 Divalent metal cation 2; catalytic.
 METAL 235 235 Divalent metal cation 1.
 METAL 235 235 Divalent metal cation 2; catalytic.
 BINDING 79 79 Substrate.
 BINDING 99 99 Substrate.
 BINDING 178 178 Substrate.  
Keyword
 3D-structure; Aminopeptidase; Complete proteome; Direct protein sequencing; Hydrolase; Metal-binding; Protease; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 264 AA 
Protein Sequence
MAISIKTPED IEKMRVAGRL AAEVLEMIEP YVKPGVSTGE LDRICNDYIV NEQHAVSACL 60
GYHGYPKSVC ISINEVVCHG IPDDAKLLKD GDIVNIDVTV IKDGFHGDTS KMFIVGKPTI 120
MGERLCRITQ ESLYLALRMV KPGINLREIG AAIQKFVEAE GFSVVREYCG HGIGRGFHEE 180
PQVLHYDSRE TNVVLKPGMT FTIEPMVNAG KKEIRTMKDG WTVKTKDRSL SAQYEHTIVV 240
TDNGCEILTL RKDDTIPAII SHDE 264 
Gene Ontology
 GO:0005829; C:cytosol; IDA:EcoCyc.
 GO:0008198; F:ferrous iron binding; IDA:EcoCyc.
 GO:0070006; F:metalloaminopeptidase activity; IDA:EcoCyc.
 GO:0070084; P:protein initiator methionine removal; IDA:EcoCyc.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 
Interpro
 IPR001714; Pept_M24_MAP.
 IPR000994; Pept_M24_structural-domain.
 IPR002467; Pept_M24A_MAP1. 
Pfam
 PF00557; Peptidase_M24 
SMART
  
PROSITE
 PS00680; MAP_1 
PRINTS
 PR00599; MAPEPTIDASE.