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Q6G846

- MAP1_STAAS

UniProt

Q6G846 - MAP1_STAAS

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Protein
Methionine aminopeptidase
Gene
map, SAS1810
Organism
Staphylococcus aureus (strain MSSA476)
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 sitei76 – 761Substrate By similarity
Metal bindingi93 – 931Divalent metal cation 1 By similarity
Metal bindingi104 – 1041Divalent metal cation 1 By similarity
Metal bindingi104 – 1041Divalent metal cation 2; catalytic By similarity
Metal bindingi168 – 1681Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei175 – 1751Substrate By similarity
Metal bindingi202 – 2021Divalent metal cation 2; catalytic By similarity
Metal bindingi233 – 2331Divalent metal cation 1 By similarity
Metal bindingi233 – 2331Divalent metal cation 2; catalytic By similarity

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Protein family/group databases

MEROPSiM24.036.

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:SAS1810
OrganismiStaphylococcus aureus (strain MSSA476)
Taxonomic identifieri282459 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000002201: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 252252Methionine aminopeptidaseUniRule annotation
PRO_0000148958Add
BLAST

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi282459.SAS1810.

Structurei

3D structure databases

ProteinModelPortaliQ6G846.
SMRiQ6G846. Positions 1-249.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000030426.
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.

Sequencei

Sequence statusi: Complete.

Q6G846-1 [UniParc]FASTAAdd to Basket

« Hide

MIVKTEEELQ ALKEIGYICA KVRNTMQAAT KPGITTKELD NIAKELFEEY    50
GAISAPIHDE NFPGQTCISV NEEVAHGIPS KRVIREGDLV NIDVSALKNG 100
YYADTGISFV VGESDDPMKQ KVCDVATMAF ENAIAKVKPG TKLSNIGKAV 150
HNTARQNDLK VIKNLTGHGV GLSLHEAPAH VLNYFDPKDK TLLTEGMVLA 200
IEPFISSNAS FVTEGKNEWA FETSDKSFVA QIEHTVIVTK DGPILTTKIE 250
EE 252
Length:252
Mass (Da):27,502
Last modified:July 19, 2004 - v1
Checksum:i3E42E623286B537B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX571857 Genomic DNA. Translation: CAG43615.1.
RefSeqiYP_043927.1. NC_002953.3.

Genome annotation databases

GeneIDi2863190.
KEGGisas:SAS1810.
PATRICi19553203. VBIStaAur96780_1882.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX571857 Genomic DNA. Translation: CAG43615.1 .
RefSeqi YP_043927.1. NC_002953.3.

3D structure databases

ProteinModelPortali Q6G846.
SMRi Q6G846. Positions 1-249.
ModBasei Search...

Protein-protein interaction databases

STRINGi 282459.SAS1810.

Chemistry

BindingDBi Q6G846.

Protein family/group databases

MEROPSi M24.036.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 2863190.
KEGGi sas:SAS1810.
PATRICi 19553203. VBIStaAur96780_1882.

Phylogenomic databases

eggNOGi COG0024.
HOGENOMi HOG000030426.
KOi K01265.
OMAi EGMCFTI.
OrthoDBi EOG6MWNDS.

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.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MSSA476.

Entry informationi

Entry nameiMAP1_STAAS
AccessioniPrimary (citable) accession number: Q6G846
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: July 19, 2004
Last modified: May 14, 2014
This is version 73 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

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