※ Protein Information
Tag Content
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Methionine aminopeptidase
Protein Synonyms/Alias
 MAP;  MetAP
Gene Name
 map
Gene Synonyms/Alias
 b0168, JW0163
Created Date
 3-June-2014
Organism
 Escherichia coli (strain K12)
NCBI Taxa ID
 83333
Phosphorylation
Position
Peptide
Code
Type
References
261 DTIPAIISHDEMAIS S HTP [1]
65 ACLGYHGYPKSVCIS Y HTP [2]
62 AVSACLGYHGYPKSV Y HTP [2]
Reference
 [1]Global dynamics of the Escherichia coli proteome and phosphoproteome during growth in minimal medium.
 Soares NC,Spät P,Krug K,Macek B
 J. Proteome Res. 2013, Jun, 7;12(6):2611-21. [PMID:23590516]
 [2]The Escherichia coli phosphotyrosine proteome relates to core pathways and virulence.
 Hansen AM,Chaerkady R,Sharma J,Díaz-Mejía JJ,Tyagi N,Renuse S,Jacob HK,Pinto SM,Sahasrabuddhe NA,Kim MS,Delanghe B,Srinivasan N,Emili A,Kaper JB,Pandey A
 PLoS Pathog. 2013;9(6):e1003403. [PMID:23785281]
Functional Description From UniProt
 FUNCTION: 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 From UniProt
 
Key Word From UniProt
 3D-structure; Aminopeptidase; Completeproteome; Directproteinsequencing; Hydrolase; Metal-binding; Protease; Referenceproteome
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
  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
  IPR001714   Pept_M24_MAP.
  IPR000994   Pept_M24_structural-domain.
  IPR002467   Pept_M24A_MAP1.
  PF00557   Peptidase_M24.
  PS00680   MAP_1.
  PR00599   MAPEPTIDASE.