ID   APEB_MYCTO              Reviewed;         433 AA.
AC   P9WHT0; L0T7J1; O06634;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Probable M18 family aminopeptidase 2;
DE            EC=3.4.11.-;
GN   Name=apeB; Synonyms=pepC; OrderedLocusNames=MT0821;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000516; AAK45063.1; -; Genomic_DNA.
DR   PIR; A70536; A70536.
DR   RefSeq; WP_003404103.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WHT0; -.
DR   SMR; P9WHT0; -.
DR   EnsemblBacteria; AAK45063; AAK45063; MT0821.
DR   KEGG; mtc:MT0821; -.
DR   PATRIC; fig|83331.31.peg.882; -.
DR   HOGENOM; CLU_019532_2_0_11; -.
DR   Proteomes; UP000001020; 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_0000428129"
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