ID   MEC_MYCTO               Reviewed;         146 AA.
AC   P9WHS0; L0T6J9; P64813; Q10645;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=CysO-cysteine peptidase;
DE            EC=3.13.1.6 {ECO:0000250|UniProtKB:P9WHS1};
DE   AltName: Full=Metallocarboxypeptidase Mec;
GN   Name=mec; Synonyms=mec+; OrderedLocusNames=MT1376;
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   -!- FUNCTION: Protease that hydrolyzes the covalent CysO-cysteine adduct
CC       synthesized by CysM to release L-cysteine and regenerate CysO.
CC       {ECO:0000250|UniProtKB:P9WHS1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)-S-L-Cys + H2O =
CC         [CysO sulfur-carrier protein]-C-terminal Gly-Gly + H(+) + L-cysteine;
CC         Xref=Rhea:RHEA:48732, Rhea:RHEA-COMP:12207, Rhea:RHEA-COMP:12212,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:35235,
CC         ChEBI:CHEBI:90778, ChEBI:CHEBI:90783; EC=3.13.1.6;
CC         Evidence={ECO:0000250|UniProtKB:P9WHS1};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P9WHS1};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis.
CC   -!- SIMILARITY: Belongs to the peptidase M67A family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK45640.1; -; Genomic_DNA.
DR   PIR; B70771; B70771.
DR   RefSeq; WP_003898830.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WHS0; -.
DR   SMR; P9WHS0; -.
DR   MEROPS; M67.009; -.
DR   EnsemblBacteria; AAK45640; AAK45640; MT1376.
DR   GeneID; 45425312; -.
DR   KEGG; mtc:MT1376; -.
DR   PATRIC; fig|83331.31.peg.1483; -.
DR   HOGENOM; CLU_116765_1_0_11; -.
DR   UniPathway; UPA00136; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR   GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR028090; JAB_dom_prok.
DR   InterPro; IPR000555; JAMM/MPN+_dom.
DR   InterPro; IPR037518; MPN.
DR   Pfam; PF14464; Prok-JAB; 1.
DR   SMART; SM00232; JAB_MPN; 1.
DR   PROSITE; PS50249; MPN; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cysteine biosynthesis; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease; Zinc.
FT   CHAIN           1..146
FT                   /note="CysO-cysteine peptidase"
FT                   /id="PRO_0000428134"
FT   DOMAIN          11..134
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   MOTIF           88..101
FT                   /note="JAMM motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         88
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         90
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         101
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ   SEQUENCE   146 AA;  16530 MW;  333945ED84CF2D5E CRC64;
     MLLRKGTVYV LVIRADLVNA MVAHARRDHP DEACGVLAGP EGSDRPERHI PMTNAERSPT
     FYRLDSGEQL KVWRAMEDAD EVPVVIYHSH TATEAYPSRT DVKLATEPDA HYVLVSTRDP
     HRHELRSYRI VDGAVTEEPV NVVEQY