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