MEC_MYCTU
ID MEC_MYCTU Reviewed; 146 AA.
AC P9WHS1; 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 45.
DE RecName: Full=CysO-cysteine peptidase;
DE EC=3.13.1.6 {ECO:0000269|PubMed:16104727};
DE AltName: Full=Metallocarboxypeptidase Mec;
GN Name=mec; Synonyms=mec+; OrderedLocusNames=Rv1334; ORFNames=MTCY130.19;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP INDUCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=12123450; DOI=10.1046/j.1365-2958.2002.03005.x;
RA Manganelli R., Voskuil M.I., Schoolnik G.K., Dubnau E., Gomez M., Smith I.;
RT "Role of the extracytoplasmic-function sigma factor sigma(H) in
RT Mycobacterium tuberculosis global gene expression.";
RL Mol. Microbiol. 45:365-374(2002).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND ACTIVITY REGULATION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16104727; DOI=10.1021/ja053476x;
RA Burns K.E., Baumgart S., Dorrestein P.C., Zhai H., McLafferty F.W.,
RA Begley T.P.;
RT "Reconstitution of a new cysteine biosynthetic pathway in Mycobacterium
RT tuberculosis.";
RL J. Am. Chem. Soc. 127:11602-11603(2005).
RN [4]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=15928073; DOI=10.1073/pnas.0503272102;
RA Rengarajan J., Bloom B.R., Rubin E.J.;
RT "Genome-wide requirements for Mycobacterium tuberculosis adaptation and
RT survival in macrophages.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:8327-8332(2005).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Protease that hydrolyzes the covalent CysO-cysteine adduct
CC synthesized by CysM to release L-cysteine and regenerate CysO.
CC {ECO:0000269|PubMed:16104727}.
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:0000269|PubMed:16104727};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:16104727};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA in vitro.
CC {ECO:0000269|PubMed:16104727}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis.
CC -!- INDUCTION: Up-regulated under oxidative stress conditions.
CC {ECO:0000269|PubMed:12123450}.
CC -!- DISRUPTION PHENOTYPE: Strains lacking this gene are shown to be
CC attenuated in macrophages. {ECO:0000269|PubMed:15928073}.
CC -!- SIMILARITY: Belongs to the peptidase M67A family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL123456; CCP44092.1; -; Genomic_DNA.
DR PIR; B70771; B70771.
DR RefSeq; NP_215850.1; NC_000962.3.
DR RefSeq; WP_003898830.1; NZ_NVQJ01000031.1.
DR AlphaFoldDB; P9WHS1; -.
DR SMR; P9WHS1; -.
DR STRING; 83332.Rv1334; -.
DR MEROPS; M67.009; -.
DR PaxDb; P9WHS1; -.
DR DNASU; 886875; -.
DR GeneID; 45425312; -.
DR GeneID; 886875; -.
DR KEGG; mtu:Rv1334; -.
DR PATRIC; fig|83332.111.peg.1489; -.
DR TubercuList; Rv1334; -.
DR eggNOG; COG1310; Bacteria.
DR OMA; GAHYVLV; -.
DR PhylomeDB; P9WHS1; -.
DR BioCyc; MetaCyc:G185E-5513-MON; -.
DR BRENDA; 3.13.1.6; 3445.
DR Reactome; R-MTU-936654; Cysteine synthesis from O-phosphoserine.
DR UniPathway; UPA00136; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR GO; GO:0008235; F:metalloexopeptidase activity; IDA:MTBBASE.
DR GO; GO:0008270; F:zinc ion binding; IDA:MTBBASE.
DR GO; GO:0019344; P:cysteine biosynthetic process; IDA:MTBBASE.
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 1: Evidence at protein level;
KW Amino-acid biosynthesis; Cysteine biosynthesis; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Zinc.
FT CHAIN 1..146
FT /note="CysO-cysteine peptidase"
FT /id="PRO_0000014095"
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
