SDRP_THET8
ID SDRP_THET8 Reviewed; 202 AA.
AC Q5SIL0;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Transcriptional regulator SdrP {ECO:0000303|PubMed:18699868};
DE AltName: Full=Cyclic AMP receptor protein/Fumarate and nitrate reduction regulator superfamily protein SdrP {ECO:0000303|PubMed:18699868};
DE Short=CRP/FNR superfamily protein SdrP {ECO:0000303|PubMed:18699868};
DE AltName: Full=Oxidative stress-responsive transcriptional activator SdrP {ECO:0000303|PubMed:21054499};
DE AltName: Full=Stationary phase-dependent regulatory protein {ECO:0000303|PubMed:21054499};
DE Short=SdrP {ECO:0000303|PubMed:21054499};
GN OrderedLocusNames=TTHA1359 {ECO:0000312|EMBL:BAD71182.1};
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852 {ECO:0000312|EMBL:BAD71182.1};
RN [1] {ECO:0000312|EMBL:BAD71182.1, ECO:0000312|Proteomes:UP000000532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8 {ECO:0000312|Proteomes:UP000000532};
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:2ZCW}
RP PROTEIN SEQUENCE OF 2-6, X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS), FUNCTION,
RP SUBUNIT, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18699868; DOI=10.1111/j.1365-2958.2008.06388.x;
RA Agari Y., Kashihara A., Yokoyama S., Kuramitsu S., Shinkai A.;
RT "Global gene expression mediated by Thermus thermophilus SdrP, a CRP/FNR
RT family transcriptional regulator.";
RL Mol. Microbiol. 70:60-75(2008).
RN [3]
RP FUNCTION, AND INDUCTION.
RX PubMed=21054499; DOI=10.1111/j.1574-6968.2010.02133.x;
RA Agari Y., Kuramitsu S., Shinkai A.;
RT "Identification of novel genes regulated by the oxidative stress-responsive
RT transcriptional activator SdrP in Thermus thermophilus HB8.";
RL FEMS Microbiol. Lett. 313:127-134(2010).
CC -!- FUNCTION: Activates transcription. The consensus DNA-binding site of
CC this transcriptional regulator is 5'-WWGTGAN(5-7)ACACWW-3' in which W
CC is A or T and N is G, A, T or C. Regulated genes include those encoding
CC proteins involved in nutrient and energy supply, redox control and
CC polyadenylation of mRNA (PubMed:18699868). Also regulates genes
CC involved in oxidative stress response such as genes encoding manganese
CC superoxide dismutase and catalase, and genes encoding a protein
CC involved in nucleotide excision repair of damaged DNA and putative
CC proteins involved in redox control, protein degradation and
CC transcriptional regulation (PubMed:21054499).
CC {ECO:0000269|PubMed:18699868, ECO:0000269|PubMed:21054499}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18699868}.
CC -!- INDUCTION: Increased expression during the stationary phase when grown
CC at 70 degrees Celsius (PubMed:18699868). Increased expression during
CC the logarithmic growth phase in oxidative stress and upon treatment
CC with diamide. Increased expression by heavy metal ion, antibiotic, high
CC salt and organic solvent stresses (PubMed:21054499).
CC {ECO:0000269|PubMed:18699868, ECO:0000269|PubMed:21054499}.
CC -!- DISRUPTION PHENOTYPE: Viable, but has growth defects, particularly when
CC grown in a synthetic medium. Increased sensitivity to disulfide stress.
CC Decreased expression of TTHA0986, TTHA0770, TTHA0337, TTHA1028,
CC TTHA0654, TTHA0655, TTHA0769, TTHA0425, TTHA0634, TTHA0635, TTHA0636,
CC TTHA0637, TTHA0638, TTHA0570, TTHA0030, TTHA0460, TTHB243, TTHA1128,
CC TTHA0035, TTHA0520 and TTHA1803 genes. {ECO:0000269|PubMed:18699868}.
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DR EMBL; AP008226; BAD71182.1; -; Genomic_DNA.
DR RefSeq; WP_011173413.1; NC_006461.1.
DR RefSeq; YP_144625.1; NC_006461.1.
DR PDB; 2ZCW; X-ray; 1.50 A; A=1-202.
DR PDBsum; 2ZCW; -.
DR AlphaFoldDB; Q5SIL0; -.
DR SMR; Q5SIL0; -.
DR STRING; 300852.55772741; -.
DR EnsemblBacteria; BAD71182; BAD71182; BAD71182.
DR GeneID; 3169114; -.
DR KEGG; ttj:TTHA1359; -.
DR PATRIC; fig|300852.9.peg.1336; -.
DR eggNOG; COG0664; Bacteria.
DR HOGENOM; CLU_075053_3_1_0; -.
DR OMA; MIYATHD; -.
DR PhylomeDB; Q5SIL0; -.
DR EvolutionaryTrace; Q5SIL0; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IMP:UniProtKB.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR012318; HTH_CRP.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF13545; HTH_Crp_2; 1.
DR SMART; SM00419; HTH_CRP; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF51206; SSF51206; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS51063; HTH_CRP_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA-binding; Reference proteome;
KW Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:18699868"
FT CHAIN 2..202
FT /note="Transcriptional regulator SdrP"
FT /id="PRO_0000436259"
FT DOMAIN 117..189
FT /note="HTH crp-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00387"
FT DNA_BIND 149..168
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00387"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:2ZCW"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:2ZCW"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:2ZCW"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:2ZCW"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:2ZCW"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:2ZCW"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:2ZCW"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:2ZCW"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:2ZCW"
FT HELIX 90..116
FT /evidence="ECO:0007829|PDB:2ZCW"
FT HELIX 119..130
FT /evidence="ECO:0007829|PDB:2ZCW"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:2ZCW"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:2ZCW"
FT HELIX 149..156
FT /evidence="ECO:0007829|PDB:2ZCW"
FT HELIX 160..172
FT /evidence="ECO:0007829|PDB:2ZCW"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:2ZCW"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:2ZCW"
FT HELIX 188..195
FT /evidence="ECO:0007829|PDB:2ZCW"
SQ SEQUENCE 202 AA; 22317 MW; 5B2D974220CAFFD2 CRC64;
MTQVRETVSF KAGDVILYPG VPGPRDRAYR VLEGLVRLEA VDEEGNALTL RLVRPGGFFG
EEALFGQERI YFAEAATDVR LEPLPENPDP ELLKDLAQHL SQGLAEAYRR IERLATQRLK
NRMAAALLEL SETPLAHEEE GKVVLKATHD ELAAAVGSVR ETVTKVIGEL AREGYIRSGY
GKIQLLDLKG LKELAESRGQ GR
