O51132 (AMPM_BORBU) 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:	BB_0105

Organism

Borrelia burgdorferi (Lyme disease spirochete)

Taxonomic identifier

139 [NCBI]

Taxonomic lineage

Bacteria › Spirochaetes › Spirochaetales › Spirochaetaceae › Borrelia › Borrelia burgdorferi group

Protein attributes

Sequence length	251 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 Reference 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 – 251	251	Methionine aminopeptidase		PRO_0000148928
Sites
	Metal binding	96	1	Cobalt 1 By similarity
	Metal binding	107	1	Cobalt 1 By similarity
	Metal binding	107	1	Cobalt 2 By similarity
	Metal binding	170	1	Cobalt 2 By similarity
	Metal binding	204	1	Cobalt 2 By similarity
	Metal binding	235	1	Cobalt 1 By similarity
	Metal binding	235	1	Cobalt 2 By similarity
	Binding site	79	1	Substrate By similarity
	Binding site	177	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	O51132 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 807996A2B082BC1C	FASTA	251	27,711
	10 20 30 40 50 60 MTKLRLKSKD EIKKIKASAS LLALTLLEVE RNIVPGISTK ELDLIAYDFI IKNRAKPAFK 70 80 90 100 110 120 GYRGFKGTIC ASVNEEVIHG IPGKRKLADG DIVSIDCGVI LDGFYSDMAK TFKVGNVDSS 130 140 150 160 170 180 IDKLLEVTNA SLYKGIAEMK VGNRILNISK AIEDYIKPFG FGIVREYTGH GVGFELHEEP 190 200 210 220 230 240 SVPNYYAPFF KNIRIQEGMV LAIEPMVNLR GHKVSIKSDG WTVFASDLSY SAHFEHTVAV 250 VDGLPLILSE V

References

[1]

"Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi." Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J. , Salzberg S.L., Hanson M., van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F., Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C., Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B., Smith H.O., Venter J.C. Nature 390:580-586(1997) [PubMed: 9403685] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35210 / B31 / CIP 102532 / DSM 4680.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000783 Genomic DNA. Translation: AAC66499.1.
PIR	A70113.
RefSeq	NP_212239.1. NC_001318.1.
3D structure databases
ProteinModelPortal	O51132.
ModBase	Search...
Protein family/group databases
MEROPS	M24.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBORT00000008780; EBBORP00000008110; EBBORG00000008779.
GeneID	1194941.
GenomeReviews	Gene locus BB_0105 in contig AE000783_GR.
KEGG	bbu:BB0105.
NMPDR	fig|224326.1.peg.489.
PATRIC	20556816. VBIBorBur75917_0503.
TIGR	BB_0105.
Phylogenomic databases
GeneTree	EBGT00050000006914.
HOGENOM	HBG299384.
OMA	CEILTDR.
PhylomeDB	O51132.
ProtClustDB	CLSK507358.
Enzyme and pathway databases
BioCyc	BBUR224326:BB_0105-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.
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_BORBU

Accession

Primary (citable) accession number: O51132

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	June 1, 1998
Last modified:	January 25, 2012
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program