ID   APEB_MYCTA              Reviewed;         433 AA.
AC   A5U0I9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Probable M18 family aminopeptidase 2 {ECO:0000255|HAMAP-Rule:MF_00467};
DE            EC=3.4.11.- {ECO:0000255|HAMAP-Rule:MF_00467};
GN   Name=apeB {ECO:0000255|HAMAP-Rule:MF_00467}; OrderedLocusNames=MRA_0810;
OS   Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=419947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25177 / H37Ra;
RX   PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA   Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA   Wang H., Wang S., Zhao G., Zhang Y.;
RT   "Genetic basis of virulence attenuation revealed by comparative genomic
RT   analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL   PLoS ONE 3:E2375-E2375(2008).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00467};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00467}.
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DR   EMBL; CP000611; ABQ72539.1; -; Genomic_DNA.
DR   RefSeq; WP_003916725.1; NZ_CP016972.1.
DR   AlphaFoldDB; A5U0I9; -.
DR   SMR; A5U0I9; -.
DR   STRING; 419947.MRA_0810; -.
DR   EnsemblBacteria; ABQ72539; ABQ72539; MRA_0810.
DR   KEGG; mra:MRA_0810; -.
DR   eggNOG; COG1362; Bacteria.
DR   HOGENOM; CLU_019532_2_0_11; -.
DR   OMA; GPILKVN; -.
DR   OrthoDB; 304020at2; -.
DR   Proteomes; UP000001988; 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_1000013699"
FT   BINDING         79
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00467"
FT   BINDING         153
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00467"
FT   BINDING         404
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00467"
SQ   SEQUENCE   433 AA;  46013 MW;  E51C3494D7735252 CRC64;
     MAATAHGLCE FIDASPSPFH VCATVAGRLL GAGYRELREA DRWPDKPGRY FTVRAGSLVA
     WNAEQSGHTQ VPFRIVGAHT DSPNLRVKQH PDRLVAGWHV VALQPYGGVW LHSWLDRDLG
     ISGRLSVRDG TGVSHRLVLI 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