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P0A080 (AMPM_STAA1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methionine aminopeptidase

Short name=MAP
EC=3.4.11.18
Alternative name(s):
Peptidase M
Gene names
Name:map
Ordered Locus Names:SAHV_1873
OrganismStaphylococcus aureus (strain Mu3 / ATCC 700698) [Complete proteome] [HAMAP]
Taxonomic identifier418127 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length252 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Removes the amino-terminal methionine from nascent proteins By similarity.

Catalytic activity

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

Cofactor

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 By similarity.

Sequence similarities

Belongs to the peptidase M24A family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 252252Methionine aminopeptidase
PRO_0000148960

Sites

Metal binding931Cobalt 1 By similarity
Metal binding1041Cobalt 1 By similarity
Metal binding1041Cobalt 2 By similarity
Metal binding1681Cobalt 2 By similarity
Metal binding2021Cobalt 2 By similarity
Metal binding2331Cobalt 1 By similarity
Metal binding2331Cobalt 2 By similarity
Binding site761Substrate By similarity
Binding site1751Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P0A080 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: 3E42E623286B537B

FASTA25227,502
        10         20         30         40         50         60 
MIVKTEEELQ ALKEIGYICA KVRNTMQAAT KPGITTKELD NIAKELFEEY GAISAPIHDE 

        70         80         90        100        110        120 
NFPGQTCISV NEEVAHGIPS KRVIREGDLV NIDVSALKNG YYADTGISFV VGESDDPMKQ 

       130        140        150        160        170        180 
KVCDVATMAF ENAIAKVKPG TKLSNIGKAV HNTARQNDLK VIKNLTGHGV GLSLHEAPAH 

       190        200        210        220        230        240 
VLNYFDPKDK TLLTEGMVLA IEPFISSNAS FVTEGKNEWA FETSDKSFVA QIEHTVIVTK 

       250 
DGPILTTKIE EE 

« Hide

References

« Hide 'large scale' references
[1]"Identification of the up- and down-regulated genes in vancomycin-resistant Staphylococcus aureus strains Mu3 and Mu50 by cDNA differential hybridization method."
Kuroda M., Kuwahara-Arai K., Hiramatsu K.
Biochem. Biophys. Res. Commun. 269:485-490(2000) [PubMed: 10708580] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Mutated response regulator graR is responsible for phenotypic conversion of Staphylococcus aureus from heterogeneous vancomycin-intermediate resistance to vancomycin-intermediate resistance."
Neoh H.-M., Cui L., Yuzawa H., Takeuchi F., Matsuo M., Hiramatsu K.
Antimicrob. Agents Chemother. 52:45-53(2008) [PubMed: 17954695] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Mu3 / ATCC 700698.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB035448 Genomic DNA. Translation: BAB03321.1.
AP009324 Genomic DNA. Translation: BAF78756.1.
RefSeqYP_001442463.1. NC_009782.1.

3D structure databases

ProteinModelPortalP0A080.
SMRP0A080. Positions 1-249.
ModBaseSearch...

Protein-protein interaction databases

STRINGP0A080.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTAT00000003491; EBSTAP00000003390; EBSTAG00000003491.
GeneID5560524.
GenomeReviewsGene locus SAHV_1873 in contig AP009324_GR.
KEGGsaw:SAHV_1873.
PATRIC19558890. VBIStaAur127830_1924.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0024.
GeneTreeEBGT00050000023792.
HOGENOMHBG299384.
OMAVFTVEPF.
ProtClustDBPRK05716.

Enzyme and pathway databases

BioCycSAUR418127:SAHV_1873-MONOMER.
BRENDA3.4.11.18. 5870.

Family and domain databases

InterProIPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002467. Pept_M24A_MAP1.
[Graphical view]
Gene3DG3DSA:3.90.230.10. Peptidase_M24_cat_core. 1 hit.
KOK01265.
PfamPF00557. Peptidase_M24. 1 hit.
[Graphical view]
PRINTSPR00599. MAPEPTIDASE.
SUPFAMSSF55920. Peptidase_M24_cat_core. 1 hit.
TIGRFAMsTIGR00500. Met_pdase_I. 1 hit.
ProtoNetSearch...

Other

BindingDBP0A080.

Entry information

Entry nameAMPM_STAA1
AccessionPrimary (citable) accession number: P0A080
Secondary accession number(s): A7X411, Q9KWL1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2005
Last modified: January 25, 2012
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families