CTSR_GEOSE
ID CTSR_GEOSE Reviewed; 153 AA.
AC C3W947;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 25-MAY-2022, entry version 35.
DE RecName: Full=Transcriptional regulator CtsR;
DE AltName: Full=Class three stress gene repressor;
GN Name=ctsr;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 12980 / DSM 22 / CCM 2062 / JCM 2501 / NBRC 12550 / NCIMB 8923
RC / NCTC 10339 / R-35646 / VKM B-510;
RA Fuhrmann J.;
RT "Characterization of CtsR from Bacillus stearothermophilus.";
RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 2-153 IN COMPLEX WITH DNA,
RP REGULATION, SUBUNIT, DOMAIN, PHOSPHORYLATION AT ARG-28; ARG-49 AND ARG-62,
RP AND MUTAGENESIS OF ARG-62.
RC STRAIN=ATCC 12980 / DSM 22 / CCM 2062 / JCM 2501 / NBRC 12550 / NCIMB 8923
RC / NCTC 10339 / R-35646 / VKM B-510;
RX PubMed=19498169; DOI=10.1126/science.1170088;
RA Fuhrmann J., Schmidt A., Spiess S., Lehner A., Turgay K., Mechtler K.,
RA Charpentier E., Clausen T.;
RT "McsB is a protein arginine kinase that phosphorylates and inhibits the
RT heat-shock regulator CtsR.";
RL Science 324:1323-1327(2009).
CC -!- FUNCTION: Controls the expression of the cellular protein quality
CC control genes clpC, clpE and clpP, as well as mcsA and mcsB, by acting
CC as a repressor of these class III stress genes. After heat shock, CtsR
CC is degraded by the ClpCP and ClpEP proteolytic systems, ensuring the
CC derepression of clpE, clpP and the clpC operon. CtsR negatively
CC autoregulates its own synthesis (By similarity). {ECO:0000250}.
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
CC (PubMed:19498169). {ECO:0000269|PubMed:19498169}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19498169}.
CC -!- INDUCTION: CtsR autoinduces its own synthesis by derepression of the
CC clpC operon after heat shock. {ECO:0000250}.
CC -!- DOMAIN: Is composed of two distinct domains: an N-terminal DNA binding
CC domain that adopts the winged HTH fold (residues 2-72) and a C-terminal
CC dimerization domain (residues 79-153) that consists of four alpha
CC helices organized in a four-helix bundle.
CC {ECO:0000269|PubMed:19498169}.
CC -!- PTM: Phosphorylated on Arg-28, Arg-49 and Arg-62 by McsB.
CC {ECO:0000269|PubMed:19498169}.
CC -!- SIMILARITY: Belongs to the CtsR family. {ECO:0000305}.
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DR EMBL; FN376878; CAY26036.1; -; Genomic_DNA.
DR RefSeq; WP_033017268.1; NZ_RCTK01000011.1.
DR PDB; 3H0D; X-ray; 2.40 A; A/B=2-153.
DR PDBsum; 3H0D; -.
DR AlphaFoldDB; C3W947; -.
DR SMR; C3W947; -.
DR iPTMnet; C3W947; -.
DR GeneID; 58573131; -.
DR EvolutionaryTrace; C3W947; -.
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 3D-structure; DNA-binding; Phosphoprotein; Repressor; Stress response;
KW Transcription; Transcription regulation.
FT CHAIN 1..153
FT /note="Transcriptional regulator CtsR"
FT /id="PRO_0000430098"
FT REGION 4..5
FT /note="Interaction with DNA"
FT REGION 27..29
FT /note="Interaction with DNA"
FT REGION 40..44
FT /note="Interaction with DNA"
FT REGION 60..61
FT /note="Interaction with DNA"
FT SITE 49
FT /note="Interaction with DNA"
FT SITE 62
FT /note="Important for DNA binding"
FT MOD_RES 28
FT /note="Phosphoarginine"
FT /evidence="ECO:0000269|PubMed:19498169"
FT MOD_RES 49
FT /note="Phosphoarginine"
FT /evidence="ECO:0000269|PubMed:19498169"
FT MOD_RES 62
FT /note="Phosphoarginine"
FT /evidence="ECO:0000269|PubMed:19498169"
FT MUTAGEN 62
FT /note="R->E: Loss of the capability to bind DNA."
FT /evidence="ECO:0000269|PubMed:19498169"
FT MUTAGEN 62
FT /note="R->K: No alteration of the capability to bind DNA."
FT /evidence="ECO:0000269|PubMed:19498169"
FT HELIX 4..16
FT /evidence="ECO:0007829|PDB:3H0D"
FT STRAND 19..26
FT /evidence="ECO:0007829|PDB:3H0D"
FT HELIX 28..34
FT /evidence="ECO:0007829|PDB:3H0D"
FT HELIX 40..49
FT /evidence="ECO:0007829|PDB:3H0D"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:3H0D"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:3H0D"
FT STRAND 67..75
FT /evidence="ECO:0007829|PDB:3H0D"
FT HELIX 79..86
FT /evidence="ECO:0007829|PDB:3H0D"
FT HELIX 95..107
FT /evidence="ECO:0007829|PDB:3H0D"
FT HELIX 113..122
FT /evidence="ECO:0007829|PDB:3H0D"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:3H0D"
FT HELIX 134..150
FT /evidence="ECO:0007829|PDB:3H0D"
SQ SEQUENCE 153 AA; 17872 MW; 4C37E27E00CEA061 CRC64;
MPNISDIIEQ YLKQVLNMSD QDIVEIKRSE IANKFRCVPS QINYVINTRF TLERGYIVES
KRGGGGYIRI MKVKTKSEAQ LIDQLLELID HRISQSSAED VIKRLMEEKV ISEREAKMML
SVMDRSVLYI DLPERDELRA RMLKAMLTSL KYK
