Q9PL68 (AMPM_CHLMU) 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:	TC_0240

Organism

Chlamydia muridarum [Complete proteome] [HAMAP]

Taxonomic identifier

83560 [NCBI]

Taxonomic lineage

Bacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydia/Chlamydophila group › Chlamydia

Protein attributes

Sequence length	291 AA.
Sequence status	Complete.
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. Binds 1 sodium ion per subunit. The sodium ion has a structural role By similarity.
Sequence similarities	Belongs to the peptidase M24A family.
Sequence caution	The sequence AAF39111.1 differs from that shown. Reason: Erroneous initiation.

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 – 291	291	Methionine aminopeptidase		PRO_0000148932
Sites
	Metal binding	135	1	Cobalt 1 By similarity
	Metal binding	146	1	Cobalt 1 By similarity
	Metal binding	146	1	Cobalt 2 By similarity
	Metal binding	209	1	Cobalt 2 By similarity
	Metal binding	241	1	Cobalt 2 By similarity
	Metal binding	273	1	Cobalt 1 By similarity
	Metal binding	273	1	Cobalt 2 By similarity
	Binding site	118	1	Substrate By similarity
	Binding site	216	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9PL68 [UniParc]. Last modified April 27, 2001. Version 2. Checksum: BAA33E190FC6160E	FASTA	291	32,646
	10 20 30 40 50 60 MKRNDPCWCG SQKKWKHCHY PTKPERPSDN LRQLYASRYD IIIKTPDQIE KIRKACQVTA 70 80 90 100 110 120 RILDALCKAA KEGVTTNELD QLSCNLHKQY NAIPAPLNYG QPPFPKTICT SLNEVICHGI 130 140 150 160 170 180 PNDTPLQNGD IMNIDVSCIV DGFYGDCSRM VMIGEVPEIK KKVCEASLEA LNAAIAILEP 190 200 210 220 230 240 NLPLYEIGEV IENCAARYGF SVVDQFVGHG VGVRFHENPY VAHHRNSCKI PLAPGMTFTI 250 260 270 280 290 EPMINVGKKE GFIDPTNHWE ARTCDHQPSA QWEHTVLITD SGYEILTLLD N

References

[1]

"Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39." Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., Gwinn M.L. , Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M. Nucleic Acids Res. 28:1397-1406(2000) [PubMed: 10684935] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MoPn / Nigg.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE002160 Genomic DNA. Translation: AAF39111.1. Different initiation.
PIR	G81724.
RefSeq	NP_296619.2. NC_002620.2.
3D structure databases
ProteinModelPortal	Q9PL68.
ModBase	Search...
Protein family/group databases
MEROPS	M24.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1246409.
GenomeReviews	Gene locus TC_0240 in contig AE002160_GR.
KEGG	cmu:TC0240.
PATRIC	20371872. VBIChlMur19118_0263.
TIGR	TC_0240.
Phylogenomic databases
HOGENOM	HBG299384.
ProtClustDB	PRK12318.
Enzyme and pathway databases
BioCyc	CMUR243161:TC_0240-MONOMER.
Family and domain databases
InterPro	IPR001714. Pept_M24_MAP. IPR000994. Pept_M24_structural-domain. IPR002467. Pept_M24A_MAP1. IPR004027. SEC_C_motif. [Graphical view]
Gene3D	G3DSA:3.90.230.10. Peptidase_M24_cat_core. 1 hit.
KO	K01265.
Pfam	PF00557. Peptidase_M24. 1 hit. PF02810. SEC-C. 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_CHLMU

Accession

Primary (citable) accession number: Q9PL68

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	April 27, 2001
Last modified:	January 25, 2012
This is version 74 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program