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Database: UniProt
Entry: Q0BUW7_GRABC
LinkDB: Q0BUW7_GRABC
Original site: Q0BUW7_GRABC 
ID   Q0BUW7_GRABC            Unreviewed;       464 AA.
AC   Q0BUW7;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   24-JAN-2024, entry version 87.
DE   SubName: Full=Transcriptional regulator, MerR family {ECO:0000313|EMBL:ABI61385.1};
GN   OrderedLocusNames=GbCGDNIH1_0487 {ECO:0000313|EMBL:ABI61385.1};
OS   Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Granulibacter.
OX   NCBI_TaxID=391165 {ECO:0000313|EMBL:ABI61385.1, ECO:0000313|Proteomes:UP000001963};
RN   [1] {ECO:0000313|EMBL:ABI61385.1, ECO:0000313|Proteomes:UP000001963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1260 / CGDNIH1 {ECO:0000313|Proteomes:UP000001963};
RX   PubMed=17827295; DOI=10.1128/JB.00793-07;
RA   Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E.,
RA   Kupko J.J.III., Barbian K.D., Babar A., Dorward D.W., Holland S.M.;
RT   "Genome sequence analysis of the emerging human pathogenic acetic acid
RT   bacterium Granulibacter bethesdensis.";
RL   J. Bacteriol. 189:8727-8736(2007).
CC   -!- SIMILARITY: Belongs to the short-chain fatty acyl-CoA assimilation
CC       regulator (ScfR) family. {ECO:0000256|ARBA:ARBA00007227}.
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DR   EMBL; CP000394; ABI61385.1; -; Genomic_DNA.
DR   RefSeq; WP_011631195.1; NC_008343.2.
DR   AlphaFoldDB; Q0BUW7; -.
DR   STRING; 391165.GbCGDNIH1_0487; -.
DR   GeneID; 69744744; -.
DR   KEGG; gbe:GbCGDNIH1_0487; -.
DR   eggNOG; COG1396; Bacteria.
DR   eggNOG; COG3800; Bacteria.
DR   HOGENOM; CLU_046383_0_0_5; -.
DR   OMA; AGTFWCS; -.
DR   OrthoDB; 1123084at2; -.
DR   Proteomes; UP000001963; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd00093; HTH_XRE; 1.
DR   Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 1.
DR   InterPro; IPR001387; Cro/C1-type_HTH.
DR   InterPro; IPR026281; HTH_RamB.
DR   InterPro; IPR010359; IrrE_HExxH.
DR   InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR   InterPro; IPR018653; ScfR_C.
DR   PANTHER; PTHR46797; HTH-TYPE TRANSCRIPTIONAL REGULATOR; 1.
DR   PANTHER; PTHR46797:SF1; METHYLPHOSPHONATE SYNTHASE; 1.
DR   Pfam; PF01381; HTH_3; 1.
DR   Pfam; PF06114; Peptidase_M78; 1.
DR   Pfam; PF09856; ScfRs; 1.
DR   PIRSF; PIRSF019251; Rv0465c; 1.
DR   SMART; SM00530; HTH_XRE; 1.
DR   SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 1.
DR   PROSITE; PS50943; HTH_CROC1; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001963};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          10..64
FT                   /note="HTH cro/C1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50943"
SQ   SEQUENCE   464 AA;  51286 MW;  A9296280BC657373 CRC64;
     MSRPLIGRTV RRLRQERGES QQSLAVRLGI SASYLNLIEH DQRGVTASLL IKLAETLRVD
     LRALSGQQER HLQTGLREVF ADPMLANESV SVEEVEQLAA ASPNAARAIL TLYRSWRVAR
     EDAGGIALPS GRRILLPNEE VRDLFAERQN YFAELEAAAG AICADLRTTP AEANHAIAER
     LRARHGLTIR VGPSEGVHRR YDPSGSNLLL SEQLPRESRG FHMAFQLALM ETREAVEGVI
     TASRLSTPEA EGLLRIGLLN YTAAAILMPY EAFRHAALEL RHDMDLLAAR FCVSFEQACQ
     RLASLQRPEA RGVPFFFLRT DAAGNVSKRF SAAGFPFARF GGSCPRWVVH EAFTSPGAIR
     VQVARLPDGA TFLCFARCVR GVAERWGDPP PLHVVAMGCD IAHAPDIIYG DGIDIERAAV
     GIGLSCRLCD RRDCRSRAFP PLEHRIAIDP NTTAESPYRF QEQH
//
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