ID CLGR_MYCTU Reviewed; 112 AA.
AC P9WMH7; F2GPH7; O33287; Q7D6N6;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Transcriptional regulator ClgR {ECO:0000305};
DE AltName: Full=ClpR-like regulator {ECO:0000303|PubMed:21771781};
DE AltName: Full=clp gene regulator {ECO:0000303|PubMed:20688819};
GN Name=clgR; OrderedLocusNames=Rv2745c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; 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 BY SIGE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=11489128; DOI=10.1046/j.1365-2958.2001.02525.x;
RA Manganelli R., Voskuil M.I., Schoolnik G.K., Smith I.;
RT "The Mycobacterium tuberculosis ECF sigma factor sigmaE: role in global
RT gene expression and survival in macrophages.";
RL Mol. Microbiol. 41:423-437(2001).
RN [3]
RP INDUCTION.
RX PubMed=20386700; DOI=10.1371/journal.pone.0010069;
RA Dutta N.K., Mehra S., Kaushal D.;
RT "A Mycobacterium tuberculosis sigma factor network responds to cell-
RT envelope damage by the promising anti-mycobacterial thioridazine.";
RL PLoS ONE 5:e10069-e10069(2010).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=H37Rv;
RX PubMed=20688819; DOI=10.1099/mic.0.042275-0;
RA Estorninho M., Smith H., Thole J., Harders-Westerveen J., Kierzek A.,
RA Butler R.E., Neyrolles O., Stewart G.R.;
RT "ClgR regulation of chaperone and protease systems is essential for
RT Mycobacterium tuberculosis parasitism of the macrophage.";
RL Microbiology 156:3445-3455(2010).
RN [5]
RP FUNCTION.
RX PubMed=21771781; DOI=10.1074/jbc.m111.241802;
RA Wang Y., Huang Y., Xue C., He Y., He Z.G.;
RT "ClpR protein-like regulator specifically recognizes RecA protein-
RT independent promoter motif and broadly regulates expression of DNA damage-
RT inducible genes in mycobacteria.";
RL J. Biol. Chem. 286:31159-31167(2011).
RN [6]
RP FUNCTION.
RC STRAIN=H37Rv;
RX PubMed=23560081; DOI=10.1371/journal.pone.0060228;
RA Personne Y., Brown A.C., Schuessler D.L., Parish T.;
RT "Mycobacterium tuberculosis ClpP proteases are co-transcribed but exhibit
RT different substrate specificities.";
RL PLoS ONE 8:e60228-e60228(2013).
RN [7]
RP FUNCTION, INTERACTION WITH PSPA, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25899163; DOI=10.1111/mmi.13037;
RA Datta P., Ravi J., Guerrini V., Chauhan R., Neiditch M.B., Shell S.S.,
RA Fortune S.M., Hancioglu B., Igoshin O.A., Gennaro M.L.;
RT "The Psp system of Mycobacterium tuberculosis integrates envelope stress-
RT sensing and envelope-preserving functions.";
RL Mol. Microbiol. 97:408-422(2015).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011445;
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: Key stress-response regulator that plays an important role in
CC multiple regulatory networks in response to different stress conditions
CC (PubMed:20688819, PubMed:25899163). Involved in preservation of
CC envelope integrity and tolerance to surface stress (PubMed:25899163).
CC Essential for macrophage infection and facilitates intracellular growth
CC of M.tuberculosis (PubMed:25899163, PubMed:20688819). Controls the
CC expression of several protease and chaperone systems, including clpP1,
CC clpP2, clpC1, ptrB, Rv1043c, acr2, clpB, Rv3269 and the clgR-pspA-
CC rv2743c-rv2742c region (PubMed:20688819, PubMed:25899163,
CC PubMed:23560081). Also plays an essential role in RecA/LexA-independent
CC DNA repair mechanism by inducing expression of DNA repair genes in
CC response to DNA damage (PubMed:21771781). {ECO:0000269|PubMed:20688819,
CC ECO:0000269|PubMed:21771781, ECO:0000269|PubMed:23560081,
CC ECO:0000269|PubMed:25899163}.
CC -!- SUBUNIT: Interacts with PspA. {ECO:0000269|PubMed:25899163}.
CC -!- INDUCTION: Expression requires SigE (PubMed:11489128, PubMed:25899163).
CC Induced by carbonyl cyanide m-chlorophenyl hydrazone (CCCP)
CC (PubMed:25899163). Induced in response to thioridazine (THZ)
CC (PubMed:20386700). {ECO:0000269|PubMed:11489128,
CC ECO:0000269|PubMed:20386700, ECO:0000269|PubMed:25899163}.
CC -!- DISRUPTION PHENOTYPE: Inactivation of the gene increases M.tuberculosis
CC susceptibility to the intramacrophage environment (PubMed:25899163,
CC PubMed:20688819). Deletion mutant shows a significantly reduced ability
CC to arrest the acidification of the phagosome (PubMed:20688819).
CC {ECO:0000269|PubMed:20688819, ECO:0000269|PubMed:25899163}.
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DR EMBL; AL123456; CCP45544.1; -; Genomic_DNA.
DR PIR; H70878; H70878.
DR RefSeq; NP_217261.1; NC_000962.3.
DR RefSeq; WP_003414032.1; NZ_NVQJ01000020.1.
DR AlphaFoldDB; P9WMH7; -.
DR SMR; P9WMH7; -.
DR STRING; 83332.Rv2745c; -.
DR PaxDb; 83332-Rv2745c; -.
DR DNASU; 888315; -.
DR GeneID; 45426732; -.
DR GeneID; 888315; -.
DR KEGG; mtu:Rv2745c; -.
DR TubercuList; Rv2745c; -.
DR eggNOG; COG1396; Bacteria.
DR InParanoid; P9WMH7; -.
DR OrthoDB; 3188736at2; -.
DR PhylomeDB; P9WMH7; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0003677; F:DNA binding; IDA:MTBBASE.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MTBBASE.
DR GO; GO:0051701; P:biological process involved in interaction with host; IDA:MTBBASE.
DR GO; GO:0085016; P:dormancy exit of symbiont in host; IDA:MTBBASE.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:MTBBASE.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:UniProtKB.
DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IEP:MTBBASE.
DR GO; GO:0090062; P:regulation of trehalose metabolic process; IEP:MTBBASE.
DR GO; GO:0010447; P:response to acidic pH; IEP:UniProtKB.
DR GO; GO:0009408; P:response to heat; IEP:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IEP:UniProtKB.
DR GO; GO:0052170; P:suppression of host innate immune response; IDA:MTBBASE.
DR CDD; cd00093; HTH_XRE; 1.
DR Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 1.
DR InterPro; IPR049655; ClgR-like.
DR InterPro; IPR001387; Cro/C1-type_HTH.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR NCBIfam; NF041677; trans_regClgR; 1.
DR Pfam; PF01381; HTH_3; 1.
DR SMART; SM00530; HTH_XRE; 1.
DR SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 1.
DR PROSITE; PS50943; HTH_CROC1; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Reference proteome; Stress response; Transcription;
KW Transcription regulation.
FT CHAIN 1..112
FT /note="Transcriptional regulator ClgR"
FT /id="PRO_0000423653"
FT DOMAIN 13..67
FT /note="HTH cro/C1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT DNA_BIND 24..43
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
SQ SEQUENCE 112 AA; 11786 MW; 0CAF56AACE6AD372 CRC64;
MAALVREVVG DVLRGARMSQ GRTLREVSDS ARVSLGYLSE IERGRKEPSS ELLSAICTAL
QLPLSVVLID AGERMARQER LARATPAGRA TGATIDASTK VVIAPVVSLA VA
//
