SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P0AE20

- MAP1_ECO57

UniProt

P0AE20 - MAP1_ECO57

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Methionine aminopeptidase

Gene
map, Z0178, ECs0170
Organism
Escherichia coli O157:H7
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

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

Cofactori

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei79 – 791Substrate By similarity
Metal bindingi97 – 971Divalent metal cation 1 By similarity
Metal bindingi108 – 1081Divalent metal cation 1 By similarity
Metal bindingi108 – 1081Divalent metal cation 2; catalytic By similarity
Metal bindingi171 – 1711Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei178 – 1781Substrate By similarity
Metal bindingi204 – 2041Divalent metal cation 2; catalytic By similarity
Metal bindingi235 – 2351Divalent metal cation 1 By similarity
Metal bindingi235 – 2351Divalent metal cation 2; catalytic By similarity

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

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

BioCyciECOL386585:GJFA-168-MONOMER.
ECOO157:MAP-MONOMER.
SABIO-RKP0AE20.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase (EC:3.4.11.18)
Short name:
MAP
Short name:
MetAP
Alternative name(s):
Peptidase M
Gene namesi
Name:map
Ordered Locus Names:Z0178, ECs0170
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000558: Chromosome, UP000002519: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 264264Methionine aminopeptidaseUniRule annotationPRO_0000148938Add
BLAST

Proteomic databases

PRIDEiP0AE20.

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

MINTiMINT-1219550.
STRINGi155864.Z0178.

Structurei

3D structure databases

ProteinModelPortaliP0AE20.
SMRiP0AE20. Positions 2-264.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000030427.
KOiK01265.
OMAiEGMCFTI.
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.

P0AE20-1 [UniParc]FASTAAdd to Basket

« Hide

MAISIKTPED IEKMRVAGRL AAEVLEMIEP YVKPGVSTGE LDRICNDYIV    50
NEQHAVSACL GYHGYPKSVC ISINEVVCHG IPDDAKLLKD GDIVNIDVTV 100
IKDGFHGDTS KMFIVGKPTI MGERLCRITQ ESLYLALRMV KPGINLREIG 150
AAIQKFVEAE GFSVVREYCG HGIGRGFHEE PQVLHYDSRE TNVVLKPGMT 200
FTIEPMVNAG KKEIRTMKDG WTVKTKDRSL SAQYEHTIVV TDNGCEILTL 250
RKDDTIPAII SHDE 264
Length:264
Mass (Da):29,331
Last modified:August 1, 1988 - v1
Checksum:iF2D0B57715A67851
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005174 Genomic DNA. Translation: AAG54470.1.
BA000007 Genomic DNA. Translation: BAB33593.1.
PIRiB85501.
B90650.
RefSeqiNP_285862.1. NC_002655.2.
NP_308197.1. NC_002695.1.

Genome annotation databases

EnsemblBacteriaiAAG54470; AAG54470; Z0178.
BAB33593; BAB33593; BAB33593.
GeneIDi913847.
956892.
KEGGiece:Z0178.
ecs:ECs0170.
PATRICi18349282. VBIEscCol44059_0171.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005174 Genomic DNA. Translation: AAG54470.1 .
BA000007 Genomic DNA. Translation: BAB33593.1 .
PIRi B85501.
B90650.
RefSeqi NP_285862.1. NC_002655.2.
NP_308197.1. NC_002695.1.

3D structure databases

ProteinModelPortali P0AE20.
SMRi P0AE20. Positions 2-264.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-1219550.
STRINGi 155864.Z0178.

Chemistry

BindingDBi P0AE20.

Proteomic databases

PRIDEi P0AE20.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAG54470 ; AAG54470 ; Z0178 .
BAB33593 ; BAB33593 ; BAB33593 .
GeneIDi 913847.
956892.
KEGGi ece:Z0178.
ecs:ECs0170.
PATRICi 18349282. VBIEscCol44059_0171.

Phylogenomic databases

eggNOGi COG0024.
HOGENOMi HOG000030427.
KOi K01265.
OMAi EGMCFTI.
OrthoDBi EOG6MWNDS.

Enzyme and pathway databases

BioCyci ECOL386585:GJFA-168-MONOMER.
ECOO157:MAP-MONOMER.
SABIO-RK P0AE20.

Family and domain databases

Gene3Di 3.90.230.10. 1 hit.
HAMAPi MF_01974. MetAP_1.
InterProi IPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002467. Pept_M24A_MAP1.
[Graphical view ]
Pfami PF00557. Peptidase_M24. 1 hit.
[Graphical view ]
PRINTSi PR00599. MAPEPTIDASE.
SUPFAMi SSF55920. SSF55920. 1 hit.
TIGRFAMsi TIGR00500. met_pdase_I. 1 hit.
PROSITEi PS00680. MAP_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
  2. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
    Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
    , Kuhara S., Shiba T., Hattori M., Shinagawa H.
    DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Entry informationi

Entry nameiMAP1_ECO57
AccessioniPrimary (citable) accession number: P0AE20
Secondary accession number(s): P07906
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: May 14, 2014
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi