P50614 (AMPM_CLOPE) 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:	CPE2383

Organism

Clostridium perfringens [Complete proteome] [HAMAP]

Taxonomic identifier

1502 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	249 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Removes the amino-terminal methionine from nascent proteins.
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 – 249	249	Methionine aminopeptidase		PRO_0000148936
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	168	1	Cobalt 2 By similarity
	Metal binding	201	1	Cobalt 2 By similarity
	Metal binding	232	1	Cobalt 1 By similarity
	Metal binding	232	1	Cobalt 2 By similarity
	Binding site	77	1	Substrate By similarity
	Binding site	175	1	Substrate By similarity
Experimental info
	Sequence conflict	30	1	K → Q in CAA60211. Ref.2
	Sequence conflict	104	1	S → R in CAA60211. Ref.2
	Sequence conflict	148	1	N → K in CAA60211. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P50614 [UniParc]. Last modified January 31, 2002. Version 2. Checksum: 7FDC5CD82CEAFAC7	FASTA	249	27,323
	10 20 30 40 50 60 MIILKNENEI DLMRKAGKIL GETLNLLKEK VRPGITTTEL DRIAEEFITK HGATPSFKGL 70 80 90 100 110 120 YGFPASLCIS VNNQVIHGFP GSYELKDGDI VSIDCGVCLN GFHSDAARTF GVGNISEEAE 130 140 150 160 170 180 KLIRITEESF FKGIEKAYVD NRLTDISNEI QQYVEANGFS VVRDFVGHGI GRKVHEDPEV 190 200 210 220 230 240 PNFGRPGRGP KLMAGMVLAI EPMVNMGSYR VKTLDDGWTV VTADGKLSAH YENTVAILPN GPEILTLIK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of Clostridium perfringens, an anaerobic flesh-eater." Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T., Ogasawara N., Hattori M., Kuhara S., Hayashi H. Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002) [PubMed: 11792842] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 13 / Type A.
[2]	"Rapid expansion of the physical and genetic map of the chromosome of Clostridium perfringens CPN50." Katayama S., Dupuy B., Garnier T., Cole S.T. J. Bacteriol. 177:5680-5685(1995) [PubMed: 7559358] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 6-148. Strain: CPN50.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000016 Genomic DNA. Translation: BAB82089.1. X86486 Genomic DNA. Translation: CAA60211.1.
RefSeq	NP_563299.1. NC_003366.1.
3D structure databases
ProteinModelPortal	P50614.
ModBase	Search...
Protein family/group databases
MEROPS	M24.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	990744.
GenomeReviews	Gene locus CPE2383 in contig BA000016_GR.
KEGG	cpe:CPE2383.
NMPDR	fig|195102.1.peg.2446.
PATRIC	19498821. VBICloPer59675_2453.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG299384.
OMA	CEILTDR.
PhylomeDB	P50614.
ProtClustDB	CLSK811239.
Enzyme and pathway databases
BioCyc	CPER195102:CPE2383-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.
PROSITE	PS00680. MAP_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMPM_CLOPE

Accession

Primary (citable) accession number: P50614

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 31, 2002
Last modified:	January 25, 2012
This is version 86 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program