Reviewed, UniProtKB/Swiss-Prot Q59509 (AMPM_MYCCT)

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:	MCAP_0675

Organism

Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343 / NCTC 10154) [Complete proteome] [HAMAP]

Taxonomic identifier

340047 [NCBI]

Taxonomic lineage

Bacteria › Tenericutes › Mollicutes › Mycoplasmataceae › Mycoplasma

Protein attributes

Sequence length	251 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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. The true nature of the physiological cofactor is under debate. The enzyme is also active with zinc, manganese or divalent iron ions By similarity.
Subunit structure	Monomer 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: InterPro
Molecular function	aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW cobalt 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 – 251	251	Methionine aminopeptidase		PRO_0000148944
Sites
	Metal binding	94	1	Cobalt 1 By similarity
	Metal binding	105	1	Cobalt 1 By similarity
	Metal binding	105	1	Cobalt 2 By similarity
	Metal binding	169	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	77	1	Substrate By similarity
	Binding site	176	1	Substrate By similarity
Experimental info
	Sequence conflict	113 – 115	3	GIA → EIR in CAA83714. Ref.2
	Sequence conflict	125	1	R → G in CAA83714. Ref.2
	Sequence conflict	161	1	S → N in CAA83714. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q59509-1 [UniParc]. Last modified March 21, 2006. Version 2. Checksum: 6AD06BE56A670EF9	FASTA	251	28,036
	10 20 30 40 50 60 MITIKNQEQI QKMKIAGQVL AKGLNLLKSM IKPGVNCLDL DKAFEEFIKQ NGCESNFKNY 70 80 90 100 110 120 QGFPKTICIS INDQLIHGIP RDRVLLDGDV VSIDAGCMYE KWHADSAFTM VCGIAKNKKN 130 140 150 160 170 180 DILIRVTEEA LELAIAELKP GIRVGTIGSI IQNYVESFDF SVPRDYTGHG IGLALHEDPY 190 200 210 220 230 240 IPNYGIPNTG IRLQEGMVIC IEPMVQMGTY KTKIADDKWT VYSADHSITA HFEHTILITK 250 DGCEVLTKTE R

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Glass J.I., Lartigue C., Pfannkoch C., Baden-Tillson H., Smith H.O., Venter J.C., Roske K., Wise K.S., Calcutt M.J., Nelson W.C., Nierman W.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"Exploring the Mycoplasma capricolum genome: a minimal cell reveals its physiology." Bork P., Ouzounis C., Casari G., Schneider R., Sander C., Dolan M., Gilbert W., Gillevet P.M. Mol. Microbiol. 16:955-967(1995) [PubMed: 7476192] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 111-251.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000123 Genomic DNA. Translation: ABC01688.1. Z33034 Genomic DNA. Translation: CAA83714.1.
PIR	S48593. S77843.
RefSeq	YP_424639.1.
3D structure databases
HSSP	HSSP built from PDB template 1O0X based on UniProtKB Q9X1I7.
ModBase	Search...
Protein-protein interaction databases
STRING	Q59509.
Protein family/group databases
MEROPS	M24.001.
Genome annotation databases
GeneID	3829108.
GenomeReviews	Gene locus MCAP_0675 in contig CP000123_GR.
KEGG	mcp:MCAP_0675.
TIGR	MCAP_0675.
Phylogenomic databases
HOGENOM	Q59509.
Enzyme and pathway databases
BioCyc	MCAP340047:MCAP_0675-MON.
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.
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.
PROSITE	PS00680. MAP_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMPM_MYCCT

Accession

Primary (citable) accession number: Q59509
Secondary accession number(s): Q2SRH4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	March 21, 2006
Last modified:	September 1, 2009
This is version 66 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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