P99121 (AMPM_STAAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Methionine aminopeptidase
Short name=MAP
EC=3.4.11.18

Alternative name(s):
Peptidase M

Gene names

Name:	map
Ordered Locus Names:	SA1704

Organism

Staphylococcus aureus (strain N315) [Complete proteome] [HAMAP]

Taxonomic identifier

158879 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	252 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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

Keywords
Ligand	Cobalt Metal-binding
Molecular function	Aminopeptidase Hydrolase Protease
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cellular process Inferred from electronic annotation. Source: InterPro proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloexopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 252	252	Methionine aminopeptidase		PRO_0000148956
Sites
	Metal binding	93	1	Cobalt 1 By similarity
	Metal binding	104	1	Cobalt 1 By similarity
	Metal binding	104	1	Cobalt 2 By similarity
	Metal binding	168	1	Cobalt 2 By similarity
	Metal binding	202	1	Cobalt 2 By similarity
	Metal binding	233	1	Cobalt 1 By similarity
	Metal binding	233	1	Cobalt 2 By similarity
	Binding site	76	1	Substrate By similarity
	Binding site	175	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P99121 [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]	"Whole genome sequencing of meticillin-resistant Staphylococcus aureus." Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. , Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., Hiramatsu K. Lancet 357:1225-1240(2001) [PubMed: 11418146] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: N315.
[2]	"Correlation of proteomic and transcriptomic profiles of Staphylococcus aureus during the post-exponential phase of growth." Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y., Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D., Sanchez J.-C., Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F., Schrenzel J. J. Microbiol. Methods 60:247-257(2005) [PubMed: 15590099] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY. Strain: N315.
[3]	"Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315." Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F. Submitted (OCT-2007) to UniProtKB Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Strain: N315.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000018 Genomic DNA. Translation: BAB42974.1.
PIR	G89976.
RefSeq	NP_374995.1. NC_002745.2.
3D structure databases
ProteinModelPortal	P99121.
SMR	P99121. Positions 1-249.
ModBase	Search...
Protein-protein interaction databases
STRING	P99121.
2D gel databases
SWISS-2DPAGE	P99121.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBSTAT00000002409; EBSTAP00000002409; EBSTAG00000002409.
GeneID	1124588.
GenomeReviews	Gene locus SA1704 in contig BA000018_GR.
KEGG	sau:SA1704.
PATRIC	19575808. VBIStaAur116463_1835.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0024.
GeneTree	EBGT00050000023792.
HOGENOM	HBG299384.
OMA	VFTVEPF.
ProtClustDB	PRK05716.
Enzyme and pathway databases
BioCyc	SAUR158879:SA1704-MONOMER.
Family and domain databases
InterPro	IPR001714. Pept_M24_MAP. IPR000994. Pept_M24_structural-domain. IPR002467. Pept_M24A_MAP1. [Graphical view]
Gene3D	G3DSA:3.90.230.10. Peptidase_M24_cat_core. 1 hit.
KO	K01265.
Pfam	PF00557. Peptidase_M24. 1 hit. [Graphical view]
PRINTS	PR00599. MAPEPTIDASE.
SUPFAM	SSF55920. Peptidase_M24_cat_core. 1 hit.
TIGRFAMs	TIGR00500. Met_pdase_I. 1 hit.
ProtoNet	Search...
Other
BindingDB	P99121.

Entry information

Entry name

AMPM_STAAN

Accession

Primary (citable) accession number: P99121
Secondary accession number(s): 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 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program