ID   A0A0H3N0Q1_MYCLB        Unreviewed;       443 AA.
AC   A0A0H3N0Q1;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Probable M18 family aminopeptidase 2 {ECO:0000256|HAMAP-Rule:MF_00467};
DE            EC=3.4.11.- {ECO:0000256|HAMAP-Rule:MF_00467};
GN   Name=pepC {ECO:0000313|EMBL:CAR72310.1};
GN   Synonyms=apeB {ECO:0000256|HAMAP-Rule:MF_00467};
GN   OrderedLocusNames=MLBr02213 {ECO:0000313|EMBL:CAR72310.1};
OS   Mycobacterium leprae (strain Br4923).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=561304 {ECO:0000313|EMBL:CAR72310.1, ECO:0000313|Proteomes:UP000006900};
RN   [1] {ECO:0000313|EMBL:CAR72310.1, ECO:0000313|Proteomes:UP000006900}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Br4923 {ECO:0000313|Proteomes:UP000006900};
RX   PubMed=19881526; DOI=10.1038/ng.477;
RA   Monot M., Honore N., Garnier T., Zidane N., Sherafi D., Paniz-Mondolfi A.,
RA   Matsuoka M., Taylor G.M., Donoghue H.D., Bouwman A., Mays S., Watson C.,
RA   Lockwood D., Khamispour A., Dowlati Y., Jianping S., Rea T.H.,
RA   Vera-Cabrera L., Stefani M.M., Banu S., Macdonald M., Sapkota B.R.,
RA   Spencer J.S., Thomas J., Harshman K., Singh P., Busso P., Gattiker A.,
RA   Rougemont J., Brennan P.J., Cole S.T.;
RT   "Comparative genomic and phylogeographic analysis of Mycobacterium
RT   leprae.";
RL   Nat. Genet. 41:1282-1289(2009).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004387};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|ARBA:ARBA00008290, ECO:0000256|HAMAP-Rule:MF_00467,
CC       ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; FM211192; CAR72310.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0H3N0Q1; -.
DR   SMR; A0A0H3N0Q1; -.
DR   KEGG; mlb:MLBr02213; -.
DR   HOGENOM; CLU_019532_2_0_11; -.
DR   OMA; GPILKVN; -.
DR   Proteomes; UP000006900; 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   CDD; cd05658; M18_DAP; 1.
DR   Gene3D; 2.30.250.10; Aminopeptidase i, Domain 2; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 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; ASPARTYL AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR28570:SF3; ASPARTYL AMINOPEPTIDASE; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438, ECO:0000256|HAMAP-
KW   Rule:MF_00467};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00467};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00467};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|HAMAP-
KW   Rule:MF_00467};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_00467};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00467}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..443
FT                   /note="Probable M18 family aminopeptidase 2"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002616066"
FT   BINDING         96
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00467"
FT   BINDING         173
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00467"
FT   BINDING         416
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00467"
SQ   SEQUENCE   443 AA;  47273 MW;  D559DDAFFAD87AD3 CRC64;
     MPTLASTTSS PTAMMLGMPA SAADLCEFIN ASPSPFHVCA TVAGRLLDAG YAELSEVERW
     PDHPGRYFIV RAGSLVAWSA GQGVKAHAPF RIVGAHTDSP NLRVKQHPDL LVAGWRVVAL
     QPYGGAWLNS WLDRDLGVSG RLSVRSAGKG SEITDRLVRI DDPILRVPQL AIHLAEDRKS
     LTLDPQRHVN AVWGVGDKAG SLLEYVAERT GVAVADVLAV DLMTHDLVPS MVIGADANLL
     SAPRLDNQVS CYAGMEALLA SVPHDCLPVL ALFDHEEVGS TSDRGARSNL LSTVLERIVL
     AAGGGRDDYL RRLPASLLVS ADMAHATHPN YPECHEPSHL IEVNAGPVLK VHPNLRYATD
     GRTAAAFEVA CQQAGVRLQR YEHRADRPCG STIGPLASAR TGIPTVDVGA AQLAMHSARE
     LMGAHDVAVY SAALQAFFSA DLF
//