(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 119.
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}.
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   SMR; P37568; -.
DR   IntAct; P37568; 5.
DR   STRING; 224308.BSU00830; -.
DR   iPTMnet; P37568; -.
DR   PaxDb; P37568; -.
DR   PRIDE; P37568; -.
DR   EnsemblBacteria; CAB11859; CAB11859; BSU00830.
DR   GeneID; 936883; -.
DR   KEGG; bsu:BSU00830; -.
DR   PATRIC; fig|224308.179.peg.84; -.
DR   eggNOG; COG4463; LUCA.
DR   HOGENOM; HOG000217970; -.
DR   KO; K03708; -.
DR   OMA; FRCAPSQ; -.
DR   PhylomeDB; P37568; -.
DR   BioCyc; BSUB:BSU00830-MONOMER; -.
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; 1.10.10.1240; -; 1.
DR   Gene3D; 1.10.1200.150; -; 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;
DR   PRODOM; P37568.
DR   SWISS-2DPAGE; P37568.
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
//

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