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A1A7L2 (A1A7L2_ECOK1) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Methionine aminopeptidase HAMAP-Rule MF_01974

Short name=MAP HAMAP-Rule MF_01974
Short name=MetAP HAMAP-Rule MF_01974
EC=3.4.11.18 HAMAP-Rule MF_01974
Alternative name(s):
Peptidase M HAMAP-Rule MF_01974
Gene names
Name:map HAMAP-Rule MF_01974 EMBL ABI99651.1
ORF Names:APECO1_1819 EMBL ABI99651.1
OrganismEscherichia coli O1:K1 / APEC [Complete proteome] [HAMAP] EMBL ABI99651.1
Taxonomic identifier405955 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length264 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Removes the N-terminal methionine from nascent proteins By similarity. RuleBase RU003653

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 By similarity. HAMAP-Rule MF_01974

Catalytic activity

Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides. HAMAP-Rule MF_01974 RuleBase RU003653

Cofactor

Binds 2 cobalt ions per subunit By similarity. RuleBase RU003653

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 By similarity. HAMAP-Rule MF_01974

Subunit structure

Monomer By similarity. HAMAP-Rule MF_01974

Sequence similarities

Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. HAMAP-Rule MF_01974

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Metal binding971Divalent metal cation 1 By similarity HAMAP-Rule MF_01974
Metal binding1081Divalent metal cation 1 By similarity HAMAP-Rule MF_01974
Metal binding1081Divalent metal cation 2; catalytic By similarity HAMAP-Rule MF_01974
Metal binding1711Divalent metal cation 2; catalytic; via tele nitrogen By similarity HAMAP-Rule MF_01974
Metal binding2041Divalent metal cation 2; catalytic By similarity HAMAP-Rule MF_01974
Metal binding2351Divalent metal cation 1 By similarity HAMAP-Rule MF_01974
Metal binding2351Divalent metal cation 2; catalytic By similarity HAMAP-Rule MF_01974
Binding site791Substrate By similarity HAMAP-Rule MF_01974
Binding site1781Substrate By similarity HAMAP-Rule MF_01974

Sequences

Sequence LengthMass (Da)Tools
A1A7L2 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: F2D0B57715A67851

FASTA26429,331
        10         20         30         40         50         60 
MAISIKTPED IEKMRVAGRL AAEVLEMIEP YVKPGVSTGE LDRICNDYIV NEQHAVSACL 

        70         80         90        100        110        120 
GYHGYPKSVC ISINEVVCHG IPDDAKLLKD GDIVNIDVTV IKDGFHGDTS KMFIVGKPTI 

       130        140        150        160        170        180 
MGERLCRITQ ESLYLALRMV KPGINLREIG AAIQKFVEAE GFSVVREYCG HGIGRGFHEE 

       190        200        210        220        230        240 
PQVLHYDSRE TNVVLKPGMT FTIEPMVNAG KKEIRTMKDG WTVKTKDRSL SAQYEHTIVV 

       250        260 
TDNGCEILTL RKDDTIPAII SHDE 

« Hide

References

[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 O1 EMBL ABI99651.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000468 Genomic DNA. Translation: ABI99651.1.
RefSeqYP_851366.1. NC_008563.1.

3D structure databases

ProteinModelPortalA1A7L2.
SMRA1A7L2. Positions 2-264.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING405955.APECO1_1819.

Chemistry

BindingDBA1A7L2.

Proteomic databases

PRIDEA1A7L2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI99651; ABI99651; APECO1_1819.
GeneID4493689.
KEGGecv:APECO1_1819.
PATRIC18211731. VBIEscCol127180_0179.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0024.
HOGENOMHOG000030427.
KOK01265.
OMACEVLTLR.
OrthoDBEOG6MWNDS.
ProtClustDBPRK05716.

Family and domain databases

Gene3D3.90.230.10. 1 hit.
HAMAPMF_01974. MetAP_1.
InterProIPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002467. Pept_M24A_MAP1.
[Graphical view]
PfamPF00557. Peptidase_M24. 1 hit.
[Graphical view]
PRINTSPR00599. MAPEPTIDASE.
SUPFAMSSF55920. SSF55920. 1 hit.
TIGRFAMsTIGR00500. met_pdase_I. 1 hit.
PROSITEPS00680. MAP_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameA1A7L2_ECOK1
AccessionPrimary (citable) accession number: A1A7L2
Entry history
Integrated into UniProtKB/TrEMBL: January 23, 2007
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)