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Database: UniProt
Entry: P0A5J3
LinkDB: P0A5J3
Original site: P0A5J3 
ID   MAP1_MYCBO              Reviewed;         285 AA.
AC   P0A5J3; O33343; X2BLS3;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   11-JUN-2014, entry version 69.
DE   RecName: Full=Methionine aminopeptidase;
DE            Short=MAP;
DE            Short=MetAP;
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       The N-terminal methionine is often cleaved when the second residue
CC       in the primary sequence is small and uncharged (Met-Ala-, Cys,
CC       Gly, Pro, Ser, Thr, or Val). Requires deformylation of the
CC       N(alpha)-formylated initiator methionine before it can be
CC       hydrolyzed (By similarity).
CC   -!- CATALYTIC ACTIVITY: Release of N-terminal amino acids,
CC       preferentially methionine, from peptides and arylamides.
CC   -!- COFACTOR: Binds 2 divalent metal cations per subunit. Has a high-
CC       affinity and a low affinity metal-binding site. The true nature of
CC       the physiological cofactor is under debate. The enzyme is active
CC       with cobalt, zinc, manganese or divalent iron ions. Most likely,
CC       methionine aminopeptidases function as mononuclear Fe(2+)-
CC       metalloproteases under physiological conditions, and the
CC       catalytically relevant metal-binding site has been assigned to the
CC       histidine-containing high-affinity site (By similarity).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine
CC       aminopeptidase type 1 subfamily.
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DR   EMBL; BX248333; CDO44152.1; -; 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; PAFHTGL; -.
DR   OrthoDB; EOG6MWNDS; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0070084; P:protein initiator methionine removal; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.90.230.10; -; 1.
DR   HAMAP; MF_01974; MetAP_1; 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; SSF55920; 1.
DR   TIGRFAMs; TIGR00500; met_pdase_I; 1.
DR   PROSITE; PS00680; MAP_1; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Complete proteome; Hydrolase; Metal-binding; Protease.
FT   CHAIN         1    285       Methionine aminopeptidase.
FT                                /FTId=PRO_0000148949.
FT   METAL       131    131       Divalent metal cation 1 (By similarity).
FT   METAL       142    142       Divalent metal cation 1 (By similarity).
FT   METAL       142    142       Divalent metal cation 2; catalytic (By
FT                                similarity).
FT   METAL       205    205       Divalent metal cation 2; catalytic; via
FT                                tele nitrogen (By similarity).
FT   METAL       238    238       Divalent metal cation 2; catalytic (By
FT                                similarity).
FT   METAL       269    269       Divalent metal cation 1 (By similarity).
FT   METAL       269    269       Divalent metal cation 2; catalytic (By
FT                                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
//
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