ID   Y2782_MYCTO             Reviewed;         438 AA.
AC   P9WHT4; L0TAV3; O33324; P0A5S8;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Uncharacterized zinc protease MT2852;
DE            EC=3.4.24.-;
GN   OrderedLocusNames=MT2852;
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       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK47171.1; -; Genomic_DNA.
DR   PIR; E70883; E70883.
DR   RefSeq; WP_003899479.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WHT4; -.
DR   SMR; P9WHT4; -.
DR   EnsemblBacteria; AAK47171; AAK47171; MT2852.
DR   KEGG; mtc:MT2852; -.
DR   PATRIC; fig|83331.31.peg.3075; -.
DR   HOGENOM; CLU_009902_3_3_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; SSF63411; 2.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Zinc.
FT   CHAIN           1..438
FT                   /note="Uncharacterized zinc protease MT2852"
FT                   /id="PRO_0000428127"
FT   ACT_SITE        62
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         59
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         63
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         139
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
SQ   SEQUENCE   438 AA;  47103 MW;  61670688EAB006C7 CRC64;
     MPRRSPADPA AALAPRRTTL PGGLRVVTEF LPAVHSASVG VWVGVGSRDE GATVAGAAHF
     LEHLLFKSTP TRSAVDIAQA MDAVGGELNA FTAKEHTCYY AHVLGSDLPL AVDLVADVVL
     NGRCAADDVE VERDVVLEEI AMRDDDPEDA LADMFLAALF GDHPVGRPVI GSAQSVSVMT
     RAQLQSFHLR RYTPEWMVVA AAGNVDHDGL VALVREHFGS RLVRGRRPVA PRKGTGRVNG
     SPRLTLVSRD AEQTHVSLGI RTPGRGWEHR WALSVLHTAL GGGLSSRLFQ EVRETRGLAY
     SVYSALDLFA DSGALSVYAA CLPERFADVM RVTADVLESV ARDGITEAEC GIAKGSLRGG
     LVLGLEDSSS RMSRLGRSEL NYGKHRSIEH TLRQIEQVTV EEVNAVARHL LSRRYGAAVL
     GPHGSKRSLP QQLRAMVG