CTSR_BACSU
ID CTSR_BACSU Reviewed; 154 AA.
AC P37568;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Transcriptional regulator CtsR;
DE AltName: Full=Class three stress gene repressor;
GN Name=ctsR; Synonyms=yacG; OrderedLocusNames=BSU00830;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA Ogasawara N., Nakai S., Yoshikawa H.;
RT "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT chromosome containing the replication origin.";
RL DNA Res. 1:1-14(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION AS A REPRESSOR.
RX PubMed=9987115; DOI=10.1046/j.1365-2958.1999.01152.x;
RA Derre I., Rapoport G., Msadek T.;
RT "CtsR, a novel regulator of stress and heat shock response, controls clp
RT and molecular chaperone gene expression in gram-positive bacteria.";
RL Mol. Microbiol. 31:117-131(1999).
RN [4]
RP SUBUNIT, DOMAIN, AND MUTAGENESIS OF GLU-10; VAL-16; CYS-38; SER-41 AND
RP GLY-65.
RC STRAIN=168;
RX PubMed=11069659; DOI=10.1046/j.1365-2958.2000.02124.x;
RA Derre I., Rapoport G., Msadek T.;
RT "The CtsR regulator of stress response is active as a dimer and
RT specifically degraded in vivo at 37 degrees C.";
RL Mol. Microbiol. 38:335-347(2000).
RN [5]
RP DEGRADATION BY CLPCP AND CLPEP, AND INDUCTION.
RC STRAIN=168;
RX PubMed=16788169; DOI=10.1128/jb.00287-06;
RA Miethke M., Hecker M., Gerth U.;
RT "Involvement of Bacillus subtilis ClpE in CtsR degradation and protein
RT quality control.";
RL J. Bacteriol. 188:4610-4619(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND PHOSPHORYLATION AT ARG-15.
RC STRAIN=168;
RX PubMed=22517742; DOI=10.1073/pnas.1117483109;
RA Elsholz A.K., Turgay K., Michalik S., Hessling B., Gronau K., Oertel D.,
RA Mader U., Bernhardt J., Becher D., Hecker M., Gerth U.;
RT "Global impact of protein arginine phosphorylation on the physiology of
RT Bacillus subtilis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:7451-7456(2012).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND PHOSPHORYLATION AT ARG-55.
RC STRAIN=168;
RX PubMed=24263382; DOI=10.1074/mcp.m113.032292;
RA Schmidt A., Trentini D.B., Spiess S., Fuhrmann J., Ammerer G., Mechtler K.,
RA Clausen T.;
RT "Quantitative phosphoproteomics reveals the role of protein arginine
RT phosphorylation in the bacterial stress response.";
RL Mol. Cell. Proteomics 13:537-550(2014).
CC -!- FUNCTION: Controls the expression of the cellular protein quality
CC control genes clpC, clpE and clpP, as well as mcsA and mcsB. Acts as a
CC repressor of these class III stress genes by binding to a directly
CC repeated heptanucleotide operator sequence (A/GGTCAAA NAN A/GGTCAAA).
CC After heat shock, CtsR is degraded by the ClpCP and ClpEP proteolytic
CC systems, ensuring the derepression of clpE, clpP and the clpC operon.
CC CtsR negatively autoregulates its own synthesis.
CC {ECO:0000269|PubMed:9987115}.
CC -!- ACTIVITY REGULATION: Repressor activity is controlled via
CC phosphorylation on arginine residues. Unphosphorylated CtsR binds with
CC high affinity to its DNA consensus site and inhibits transcription of
CC downstream genes, whereas the McsB-phosphorylated CtsR repressor is not
CC able to bind to DNA, thus allowing heat-shock gene expression (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11069659}.
CC -!- INDUCTION: CtsR autoinduces its own synthesis by derepression of the
CC clpC operon after heat shock. {ECO:0000269|PubMed:16788169}.
CC -!- PTM: Is degraded by ClpXP at 37 degrees Celsius, which maintains a
CC basal level of the regulator within the cell. Is phosphorylated on Arg
CC residues by McsB. {ECO:0000269|PubMed:22517742,
CC ECO:0000269|PubMed:24263382}.
CC -!- SIMILARITY: Belongs to the CtsR family. {ECO:0000305}.
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DR EMBL; D26185; BAA05317.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB11859.1; -; Genomic_DNA.
DR PIR; S66112; S66112.
DR RefSeq; NP_387964.1; NC_000964.3.
DR RefSeq; WP_003225724.1; NZ_JNCM01000029.1.
DR AlphaFoldDB; P37568; -.
DR SMR; P37568; -.
DR IntAct; P37568; 5.
DR STRING; 224308.BSU00830; -.
DR iPTMnet; P37568; -.
DR PaxDb; P37568; -.
DR PRIDE; P37568; -.
DR EnsemblBacteria; CAB11859; CAB11859; BSU_00830.
DR GeneID; 64301921; -.
DR GeneID; 936883; -.
DR KEGG; bsu:BSU00830; -.
DR PATRIC; fig|224308.179.peg.84; -.
DR eggNOG; COG4463; Bacteria.
DR OMA; FRCAPSQ; -.
DR PhylomeDB; P37568; -.
DR BioCyc; BSUB:BSU00830-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 1.10.1200.150; -; 1.
DR Gene3D; 3.30.56.130; -; 1.
DR InterPro; IPR008463; CtsR.
DR InterPro; IPR041473; CtsR_C.
DR InterPro; IPR041908; CtsR_C_sf.
DR InterPro; IPR040465; CtsR_N.
DR InterPro; IPR041902; CtsR_N_sf.
DR PANTHER; PTHR40028; PTHR40028; 1.
DR Pfam; PF05848; CtsR; 1.
DR Pfam; PF17727; CtsR_C; 1.
DR PIRSF; PIRSF010607; Txn_repr_CtsR; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Phosphoprotein; Reference proteome; Repressor;
KW Stress response; Transcription; Transcription regulation.
FT CHAIN 1..154
FT /note="Transcriptional regulator CtsR"
FT /id="PRO_0000079499"
FT MOD_RES 15
FT /note="Phosphoarginine"
FT /evidence="ECO:0000269|PubMed:22517742"
FT MOD_RES 55
FT /note="Phosphoarginine"
FT /evidence="ECO:0000269|PubMed:24263382"
FT MUTAGEN 10
FT /note="E->K: Loss of DNA-binding capacity."
FT /evidence="ECO:0000269|PubMed:11069659"
FT MUTAGEN 16
FT /note="V->M: Prevents inactivation of CtsR at high
FT temperature."
FT /evidence="ECO:0000269|PubMed:11069659"
FT MUTAGEN 38
FT /note="C->Y: Loss of DNA-binding capacity."
FT /evidence="ECO:0000269|PubMed:11069659"
FT MUTAGEN 41
FT /note="S->F: Loss of DNA-binding capacity."
FT /evidence="ECO:0000269|PubMed:11069659"
FT MUTAGEN 65
FT /note="G->S: Prevents inactivation of CtsR at high
FT temperature."
FT /evidence="ECO:0000269|PubMed:11069659"
SQ SEQUENCE 154 AA; 17744 MW; 11A2B4EC15809CF6 CRC64;
MGHNISDIIE QYLKRVLDQN GKEILEIKRS EIADKFQCVP SQINYVINTR FTSERGYIVE
SKRGGGGYIR IIKIKMNNEV VLINNIISQI NTHLSQAASD DIILRLLEDK VISEREAKMM
VSVMDRSVLH IDLPERDELR ARMMKAMLTS LKLK
