Reviewed, UniProtKB/Swiss-Prot P0A080 (AMPM_STAA1)

Names and origin

Protein names

Methionine aminopeptidase
Also known as:
     EC 3.4.11.18
     MAP
     Peptidase M

Gene names

Name:	map
Ordered Locus Names:	SAHV_1873

Organism

Staphylococcus aureus (strain Mu3 / ATCC 700698) [Complete proteome] [HAMAP]

Taxonomic identifier

418127 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein existence

Inferred 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 By similarity.
Sequence similarities	Belongs to the peptidase M24A family.

Ontologies

Keywords
Ligand	Cobalt Metal-binding
Molecular function	Aminopeptidase Hydrolase Protease
Technical term	Complete proteome
Gene Ontology (GO)
None. [Check GOA]

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 252	252	Methionine aminopeptidase
Sites
	Metal binding	93	1	Cobalt 2 By similarity
	Metal binding	104	1	Cobalt 1 By similarity
	Metal binding	104	1	Cobalt 2 By similarity
	Metal binding	168	1	Cobalt 1 By similarity
	Metal binding	202	1	Cobalt 1 By similarity
	Metal binding	233	1	Cobalt 1 By similarity
	Metal binding	233	1	Cobalt 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0A080-1 [UniParc]. Last modified March 1, 2005. Version 1. Checksum: 3E42E623286B537B	FASTA	252	27,502
	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

References

	« Hide 'large scale' referencesShow '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].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB035448 Genomic DNA. Translation: BAB03321.1. AP009324 Genomic DNA. Translation: BAF78756.1.
RefSeq	YP_001442463.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5560524.
GenomeReviews	Gene locus SAHV_1873 in contig AP009324_GR.
KEGG	saw:SAHV_1873.
Organism-specific databases
CMR	Search...
Family and domain databases
InterPro	IPR001714. Pept_M24_MAP. IPR002467. Pept_M24A_MAP1. IPR000994. Peptidase_M24_cat_core. [Graphical view]
Gene3D	G3DSA:3.90.230.10. Peptidase_M24_cat_core. 1 hit.
PANTHER	PTHR10804:SF13. Pept_M24A_MAP1. 1 hit. PTHR10804. Peptidase_M24_cat_core. 1 hit.
Pfam	PF00557. Peptidase_M24. 1 hit. [Graphical view]
PRINTS	PR00599. MAPEPTIDASE.
TIGRFAMs	TIGR00500. met_pdase_I. 1 hit.
ProDom	P0A080. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
ProtoNet	Search...

Entry information

Entry name

AMPM_STAA1

Accession

Primary (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:	May 20, 2008
This is version 26 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)