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P0A078

- MAP1_STAAM

UniProt

P0A078 - MAP1_STAAM

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Protein
Methionine aminopeptidase
Gene
map, SAV1888
Organism
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

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 cobalt ions per subunit. The true nature of the physiological cofactor is under debate. The enzyme is also active with zinc, manganese or divalent iron ions.
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
Metal bindingi93 – 931Divalent metal cation 1
Metal bindingi104 – 1041Divalent metal cation 1
Metal bindingi104 – 1041Divalent metal cation 2; catalytic
Metal bindingi168 – 1681Divalent metal cation 2; catalytic; via tele nitrogen
Binding sitei175 – 1751Substrate
Metal bindingi202 – 2021Divalent metal cation 2; catalytic
Metal bindingi233 – 2331Divalent metal cation 1
Metal bindingi233 – 2331Divalent metal cation 2; catalytic

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

BioCyciSAUR158878:GJJ5-1943-MONOMER.

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:SAV1888
OrganismiStaphylococcus aureus (strain Mu50 / ATCC 700699)
Taxonomic identifieri158878 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000002481: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 252252Methionine aminopeptidaseUniRule annotation
PRO_0000148955Add
BLAST

2D gel databases

World-2DPAGE0002:P0A078.

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi158878.SAV1888.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 2924
Helixi36 – 5015
Helixi55 – 606
Beta strandi63 – 708
Beta strandi73 – 753
Beta strandi89 – 9810
Beta strandi101 – 11010
Helixi118 – 13417
Helixi144 – 15613
Beta strandi167 – 1693
Beta strandi171 – 18111
Beta strandi197 – 2015
Beta strandi204 – 2085
Beta strandi216 – 2194
Beta strandi229 – 2379

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QXWX-ray1.67A1-252[»]
1QXYX-ray1.04A1-252[»]
1QXZX-ray1.68A1-252[»]
ProteinModelPortaliP0A078.
SMRiP0A078. Positions 1-249.

Miscellaneous databases

EvolutionaryTraceiP0A078.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000030426.
KOiK01265.
OMAiFHEMIDI.
OrthoDBiEOG6MWNDS.
PhylomeDBiP0A078.

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.

P0A078-1 [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:March 1, 2005 - v1
Checksum:i3E42E623286B537B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000017 Genomic DNA. Translation: BAB58050.1.
RefSeqiNP_372412.1. NC_002758.2.

Genome annotation databases

EnsemblBacteriaiBAB58050; BAB58050; SAV1888.
GeneIDi1121901.
KEGGisav:SAV1888.
PATRICi19564622. VBIStaAur52173_1950.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000017 Genomic DNA. Translation: BAB58050.1 .
RefSeqi NP_372412.1. NC_002758.2.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1QXW X-ray 1.67 A 1-252 [» ]
1QXY X-ray 1.04 A 1-252 [» ]
1QXZ X-ray 1.68 A 1-252 [» ]
ProteinModelPortali P0A078.
SMRi P0A078. Positions 1-249.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 158878.SAV1888.

Chemistry

BindingDBi P0A078.

2D gel databases

World-2DPAGE 0002:P0A078.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAB58050 ; BAB58050 ; SAV1888 .
GeneIDi 1121901.
KEGGi sav:SAV1888.
PATRICi 19564622. VBIStaAur52173_1950.

Phylogenomic databases

eggNOGi COG0024.
HOGENOMi HOG000030426.
KOi K01265.
OMAi FHEMIDI.
OrthoDBi EOG6MWNDS.
PhylomeDBi P0A078.

Enzyme and pathway databases

BioCyci SAUR158878:GJJ5-1943-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A078.

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

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Mu50 / ATCC 700699.
  2. "Crystal structures of Staphylococcus aureus methionine aminopeptidase complexed with keto heterocycle and aminoketone inhibitors reveal the formation of a tetrahedral intermediate."
    Douangamath A., Dale G.E., D'Arcy A., Almstetter M., Eckl R., Frutos-Hoener A., Henkel B., Illgen K., Nerdinger S., Schulz H., Mac Sweeney A., Thormann M., Treml A., Pierau S., Wadman S., Oefner C.
    J. Med. Chem. 47:1325-1328(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.04 ANGSTROMS) IN COMPLEXES WITH COBALT IONS AND INHIBITOR.

Entry informationi

Entry nameiMAP1_STAAM
AccessioniPrimary (citable) accession number: P0A078
Secondary accession number(s): Q9KWL1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2005
Last modified: July 9, 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

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi