CRP_THET8
ID CRP_THET8 Reviewed; 216 AA.
AC Q5SID7;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Cyclic AMP receptor protein {ECO:0000303|PubMed:17369302};
DE AltName: Full=Cyclic AMP receptor protein/Fumarate and nitrate reduction regulator superfamily protein TTHA1437 {ECO:0000303|PubMed:17369302};
DE Short=CRP/FNR superfamily protein TTHA1437 {ECO:0000303|PubMed:17369302};
DE AltName: Full=cAMP receptor protein {ECO:0000303|PubMed:17369302};
DE Short=CRP {ECO:0000303|PubMed:17369302};
GN OrderedLocusNames=TTHA1437 {ECO:0000312|EMBL:BAD71260.1};
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852 {ECO:0000312|EMBL:BAD71260.1};
RN [1] {ECO:0000312|EMBL:BAD71260.1, 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]
RP PROTEIN SEQUENCE OF 1-5 AND 77-81, FUNCTION, CAMP-BINDING, SUBUNIT, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 27634 / DSM 579 / HB8 {ECO:0000312|Proteomes:UP000000532};
RX PubMed=17369302; DOI=10.1128/jb.01739-06;
RA Shinkai A., Kira S., Nakagawa N., Kashihara A., Kuramitsu S., Yokoyama S.;
RT "Transcription activation mediated by a cyclic AMP receptor protein from
RT Thermus thermophilus HB8.";
RL J. Bacteriol. 189:3891-3901(2007).
RN [3] {ECO:0007744|PDB:4EV0}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH CAMP.
RC STRAIN=ATCC 27634 / DSM 579 / HB8 {ECO:0000312|PDB:4EV0};
RA Hudson B.P., Turo K., Birktoft J.J., Ebright R.H., Lawson C.L.;
RT "Crystal Structure of T. thermophilius catabolite activator protein.";
RL Submitted (APR-2012) to the PDB data bank.
CC -!- FUNCTION: Activates transcription. Positively regulates six promoters
CC upstream of the TTHB186, TTHB147, TTHB178, TTHB159, TTHA0771 and
CC TTHA0176 genes in a cAMP-dependent manner. Regulated genes include
CC clustered regularly interspaced short palindromic repeat (CRISPR)
CC associated (Cas) genes, and the genes encoding a putative
CC transcriptional regulator, a protein containing the exonuclease III-
CC like domain of DNA polymerase, a GCN5-related acetyltransferase
CC homolog, and some T.thermophilus-specific proteins of unknown function.
CC The consensus DNA-binding site of this transcriptional regulator is 5'-
CC (CT)NNG(G/T)(G/T)C(A/C)N(A/T)NNTCACAN(G/C)(G/C)-3' in which N is G, A,
CC T or C. {ECO:0000269|PubMed:17369302}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17369302}.
CC -!- DISRUPTION PHENOTYPE: Decreased expression of genes downstream of the
CC TTHB186, TTHB147 and TTHB159 genes. Decreased expression of TTHB178,
CC TTHA0771 and TTHA0176 genes. {ECO:0000269|PubMed:17369302}.
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DR EMBL; AP008226; BAD71260.1; -; Genomic_DNA.
DR RefSeq; WP_011228681.1; NC_006461.1.
DR RefSeq; YP_144703.1; NC_006461.1.
DR PDB; 4EV0; X-ray; 2.40 A; A/D=1-216.
DR PDBsum; 4EV0; -.
DR AlphaFoldDB; Q5SID7; -.
DR SMR; Q5SID7; -.
DR STRING; 300852.55772819; -.
DR EnsemblBacteria; BAD71260; BAD71260; BAD71260.
DR GeneID; 3169761; -.
DR KEGG; ttj:TTHA1437; -.
DR PATRIC; fig|300852.9.peg.1411; -.
DR eggNOG; COG0664; Bacteria.
DR HOGENOM; CLU_075053_3_4_0; -.
DR OMA; VLCRDFG; -.
DR PhylomeDB; Q5SID7; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0030552; F:cAMP binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA: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; IPR018488; cNMP-bd_CS.
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; SM00100; cNMP; 1.
DR SMART; SM00419; HTH_CRP; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF51206; SSF51206; 1.
DR PROSITE; PS00889; CNMP_BINDING_2; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS51063; HTH_CRP_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; cAMP; Direct protein sequencing; DNA-binding;
KW Nucleotide-binding; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..216
FT /note="Cyclic AMP receptor protein"
FT /id="PRO_0000436193"
FT DOMAIN 140..206
FT /note="HTH crp-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00387"
FT DNA_BIND 166..185
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00387"
FT BINDING 6..126
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00060"
FT BINDING 75..78
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:4EV0"
FT BINDING 85..86
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:4EV0"
FT HELIX 5..7
FT /evidence="ECO:0007829|PDB:4EV0"
FT HELIX 12..19
FT /evidence="ECO:0007829|PDB:4EV0"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:4EV0"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:4EV0"
FT STRAND 42..49
FT /evidence="ECO:0007829|PDB:4EV0"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:4EV0"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:4EV0"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:4EV0"
FT HELIX 76..81
FT /evidence="ECO:0007829|PDB:4EV0"
FT STRAND 86..101
FT /evidence="ECO:0007829|PDB:4EV0"
FT HELIX 102..111
FT /evidence="ECO:0007829|PDB:4EV0"
FT HELIX 113..155
FT /evidence="ECO:0007829|PDB:4EV0"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:4EV0"
FT HELIX 166..173
FT /evidence="ECO:0007829|PDB:4EV0"
FT HELIX 177..189
FT /evidence="ECO:0007829|PDB:4EV0"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:4EV0"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:4EV0"
FT HELIX 205..212
FT /evidence="ECO:0007829|PDB:4EV0"
SQ SEQUENCE 216 AA; 23819 MW; A89F76CB48D6410F CRC64;
MKGSPLFHGL APEEVDLALS YFQRRLYPQG KPIFYQGDLG QALYLVASGK VRLFRTHLGG
QERTLALLGP GELFGEMSLL DEGERSASAV AVEDTELLAL FREDYLALIR RLPLVAHNLA
ALLARRLREA DLELDLLSFE EARNRVAYAL LKLLRQGLGP LFQIRHHELA ALAGTSRETV
SRVLHALAEE GVVRLGPGTV EVREAALLEE IAFGLA
