ID AMPM_MYCBO Reviewed; 285 AA.
AC P0A5J3; O33343;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 01-MAY-2013, entry version 62.
DE RecName: Full=Methionine aminopeptidase;
DE Short=MAP;
DE EC=3.4.11.18;
DE AltName: Full=Peptidase M;
GN Name=map; Synonyms=mapB; OrderedLocusNames=Mb2886c;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Corynebacterineae; Mycobacteriaceae; Mycobacterium;
OC Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H.,
RA Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S.,
RA Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R.,
RA Parkhill J., Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
CC -!- FUNCTION: Removes the N-terminal methionine from nascent proteins
CC (By similarity).
CC -!- CATALYTIC ACTIVITY: Release of N-terminal amino acids,
CC preferentially methionine, from peptides and arylamides.
CC -!- COFACTOR: Binds 2 cobalt ions per subunit. The true nature of the
CC physiological cofactor is under debate. The enzyme is also active
CC with zinc, manganese or divalent iron ions (By similarity).
CC -!- SIMILARITY: Belongs to the peptidase M24A family.
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DR EMBL; BX248344; CAD96573.1; -; Genomic_DNA.
DR RefSeq; NP_856531.1; NC_002945.3.
DR ProteinModelPortal; P0A5J3; -.
DR SMR; P0A5J3; 2-285.
DR STRING; 233413.Mb2886c; -.
DR EnsemblBacteria; CAD96573; CAD96573; Mb2886c.
DR GeneID; 1092223; -.
DR KEGG; mbo:Mb2886c; -.
DR PATRIC; 18008068; VBIMycBov88188_3166.
DR eggNOG; COG0024; -.
DR HOGENOM; HOG000030427; -.
DR KO; K01265; -.
DR OMA; GEVIQKH; -.
DR ProtClustDB; PRK12896; -.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR GO; GO:0009987; P:cellular process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.90.230.10; -; 1.
DR InterPro; IPR001714; Pept_M24_MAP.
DR InterPro; IPR000994; Pept_M24_structural-domain.
DR InterPro; IPR002467; Pept_M24A_MAP1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR PRINTS; PR00599; MAPEPTIDASE.
DR SUPFAM; SSF55920; Peptidase_M24_cat_core; 1.
DR TIGRFAMs; TIGR00500; met_pdase_I; 1.
DR PROSITE; PS00680; MAP_1; 1.
PE 3: Inferred from homology;
KW Aminopeptidase; Cobalt; Complete proteome; Hydrolase; Metal-binding;
KW Protease.
FT CHAIN 1 285 Methionine aminopeptidase.
FT /FTId=PRO_0000148949.
FT METAL 131 131 Cobalt 1 (By similarity).
FT METAL 142 142 Cobalt 1 (By similarity).
FT METAL 142 142 Cobalt 2 (By similarity).
FT METAL 205 205 Cobalt 2 (By similarity).
FT METAL 238 238 Cobalt 2 (By similarity).
FT METAL 269 269 Cobalt 1 (By similarity).
FT METAL 269 269 Cobalt 2 (By similarity).
FT BINDING 114 114 Substrate (By similarity).
FT BINDING 212 212 Substrate (By similarity).
SQ SEQUENCE 285 AA; 30891 MW; E69831250E6C6130 CRC64;
MPSRTALSPG VLSPTRPVPN WIARPEYVGK PAAQEGSEPW VQTPEVIEKM RVAGRIAAGA
LAEAGKAVAP GVTTDELDRI AHEYLVDNGA YPSTLGYKGF PKSCCTSLNE VICHGIPDST
VITDGDIVNI DVTAYIGGVH GDTNATFPAG DVADEHRLLV DRTREATMRA INTVKPGRAL
SVIGRVIESY ANRFGYNVVR DFTGHGIGTT FHNGLVVLHY DQPAVETIMQ PGMTFTIEPM
INLGALDYEI WDDGWTVVTK DRKWTAQFEH TLLVTDTGVE ILTCL
//
