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APEB_MYCBO
ID   APEB_MYCBO              Reviewed;         433 AA.
AC   P59951; A0A1R3XYK0; X2BG29;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Probable M18 family aminopeptidase 2;
DE            EC=3.4.11.-;
GN   Name=apeB; Synonyms=pepC; OrderedLocusNames=BQ2027_MB0823;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; 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., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family. {ECO:0000305}.
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DR   EMBL; LT708304; SIT99422.1; -; Genomic_DNA.
DR   RefSeq; NP_854481.1; NC_002945.3.
DR   RefSeq; WP_003404103.1; NC_002945.4.
DR   AlphaFoldDB; P59951; -.
DR   SMR; P59951; -.
DR   EnsemblBacteria; SIT99422; SIT99422; BQ2027_MB0823.
DR   PATRIC; fig|233413.5.peg.895; -.
DR   OMA; GPILKVN; -.
DR   Proteomes; UP000001419; Chromosome.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.30.250.10; -; 1.
DR   HAMAP; MF_00467; Aminopeptidase_M18_2; 1.
DR   InterPro; IPR022984; M18_aminopeptidase_2.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023358; Peptidase_M18_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase; Hydrolase; Metal-binding; Metalloprotease; Protease; Zinc.
FT   CHAIN           1..433
FT                   /note="Probable M18 family aminopeptidase 2"
FT                   /id="PRO_0000173462"
FT   BINDING         79
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         153
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         404
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   433 AA;  46056 MW;  228424208638F68C CRC64;
     MAATAHGLCE FIDASPSPFH VCATVAGRLL GAGYRELREA DRWPDKPGRY FTVRAGSLVA
     WNAEQSGHTQ VPFRIVGAHT DSPNLRVKQH PDRLVAGWHV VALQPYGGVW LHSWLDRDLG
     ISGRLSVRDG TGVSHRLVRI DDPILRVPQL AIHLAEDRKS LTLDPQRHIN AVWGVGERVE
     SFVGYVAQRA GVAAADVLAA DLMTHDLTPS ALIGASVNGT ASLLSAPRLD NQASCYAGME
     ALLAVDVDSA SSGFVPVLAI FDHEEVGSAS GHGAQSDLLS SVLERIVLAA GGTREDFLRR
     LTTSMLASAD MAHATHPNYP DRHEPSHPIE VNAGPVLKVH PNLRYATDGR TAAAFALACQ
     RAGVPMQRYE HRADLPCGST IGPLAAARTG IPTVDVGAAQ LAMHSARELM GAHDVAAYSA
     ALQAFLSAEL SEA
 
 
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