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 24-JAN-2024, entry version 38.
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; Actinomycetota; Actinomycetes; Mycobacteriales; 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}.
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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 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 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; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; 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
//
