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Protein

Methionine aminopeptidase

Gene

map

Organism
Escherichia coli O1:K1 / APEC
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Removes the N-terminal methionine from nascent proteins.UniRule annotation
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.UniRule annotation

Catalytic activityi

Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.UniRule annotation

Cofactori

Protein has several cofactor binding sites:
  • Note: Binds 2 cobalt ions per subunit.UniRule annotation
  • Co2+UniRule annotation, Zn2+UniRule annotation, Mn2+UniRule annotation, Fe2+UniRule annotationNote: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe2+-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei79 – 791SubstrateUniRule annotation
Metal bindingi97 – 971Divalent metal cation 1UniRule annotation
Metal bindingi108 – 1081Divalent metal cation 1UniRule annotation
Metal bindingi108 – 1081Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi171 – 1711Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei178 – 1781SubstrateUniRule annotation
Metal bindingi204 – 2041Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi235 – 2351Divalent metal cation 1UniRule annotation
Metal bindingi235 – 2351Divalent metal cation 2; catalyticUniRule annotation

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-HAMAP
  2. metalloaminopeptidase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. protein initiator methionine removal Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

AminopeptidaseUniRule annotation, Hydrolase, Protease

Keywords - Ligandi

Metal-bindingUniRule annotation

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidaseUniRule annotation (EC:3.4.11.18UniRule annotation)
Short name:
MAPUniRule annotation
Short name:
MetAPUniRule annotation
Alternative name(s):
Peptidase MUniRule annotation
Gene namesi
Name:mapUniRule annotationImported
ORF Names:APECO1_1819Imported
OrganismiEscherichia coli O1:K1 / APECImported
Taxonomic identifieri405955 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000008216: Chromosome

PTM / Processingi

Proteomic databases

PRIDEiA1A7L2.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi405955.APECO1_1819.

Structurei

3D structure databases

ProteinModelPortaliA1A7L2.
SMRiA1A7L2. Positions 2-264.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000030427.
KOiK01265.
OMAiPTIQGER.
OrthoDBiEOG6MWNDS.

Family and domain databases

Gene3Di3.90.230.10. 1 hit.
HAMAPiMF_01974. MetAP_1.
InterProiIPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002467. Pept_M24A_MAP1.
[Graphical view]
PfamiPF00557. Peptidase_M24. 1 hit.
[Graphical view]
PRINTSiPR00599. MAPEPTIDASE.
SUPFAMiSSF55920. SSF55920. 1 hit.
TIGRFAMsiTIGR00500. met_pdase_I. 1 hit.
PROSITEiPS00680. MAP_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A1A7L2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAISIKTPED IEKMRVAGRL AAEVLEMIEP YVKPGVSTGE LDRICNDYIV
60 70 80 90 100
NEQHAVSACL GYHGYPKSVC ISINEVVCHG IPDDAKLLKD GDIVNIDVTV
110 120 130 140 150
IKDGFHGDTS KMFIVGKPTI MGERLCRITQ ESLYLALRMV KPGINLREIG
160 170 180 190 200
AAIQKFVEAE GFSVVREYCG HGIGRGFHEE PQVLHYDSRE TNVVLKPGMT
210 220 230 240 250
FTIEPMVNAG KKEIRTMKDG WTVKTKDRSL SAQYEHTIVV TDNGCEILTL
260
RKDDTIPAII SHDE
Length:264
Mass (Da):29,331
Last modified:January 23, 2007 - v1
Checksum:iF2D0B57715A67851
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000468 Genomic DNA. Translation: ABI99651.1.
RefSeqiYP_851366.1. NC_008563.1.

Genome annotation databases

EnsemblBacteriaiABI99651; ABI99651; APECO1_1819.
GeneIDi4493689.
KEGGiecv:APECO1_1819.
PATRICi18211731. VBIEscCol127180_0179.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000468 Genomic DNA. Translation: ABI99651.1.
RefSeqiYP_851366.1. NC_008563.1.

3D structure databases

ProteinModelPortaliA1A7L2.
SMRiA1A7L2. Positions 2-264.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi405955.APECO1_1819.

Chemistry

BindingDBiA1A7L2.

Proteomic databases

PRIDEiA1A7L2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABI99651; ABI99651; APECO1_1819.
GeneIDi4493689.
KEGGiecv:APECO1_1819.
PATRICi18211731. VBIEscCol127180_0179.

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000030427.
KOiK01265.
OMAiPTIQGER.
OrthoDBiEOG6MWNDS.

Family and domain databases

Gene3Di3.90.230.10. 1 hit.
HAMAPiMF_01974. MetAP_1.
InterProiIPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002467. Pept_M24A_MAP1.
[Graphical view]
PfamiPF00557. Peptidase_M24. 1 hit.
[Graphical view]
PRINTSiPR00599. MAPEPTIDASE.
SUPFAMiSSF55920. SSF55920. 1 hit.
TIGRFAMsiTIGR00500. met_pdase_I. 1 hit.
PROSITEiPS00680. MAP_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7 shares strong similarities with human extraintestinal pathogenic E. coli genomes."
    Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J., Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.
    J. Bacteriol. 189:3228-3236(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: APEC O1Imported.

Entry informationi

Entry nameiA1A7L2_ECOK1
AccessioniPrimary (citable) accession number: A1A7L2
Entry historyi
Integrated into UniProtKB/TrEMBL: January 23, 2007
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.