ID   Q167P6_ROSDO            Unreviewed;       468 AA.
AC   Q167P6;
DT   25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   25-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   SubName: Full=Transcriptional regulator, putative {ECO:0000313|EMBL:ABG31797.1};
GN   OrderedLocusNames=RD1_2203 {ECO:0000313|EMBL:ABG31797.1};
OS   Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp.
OS   (strain OCh 114)) (Roseobacter denitrificans).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseobacter.
OX   NCBI_TaxID=375451 {ECO:0000313|EMBL:ABG31797.1, ECO:0000313|Proteomes:UP000007029};
RN   [1] {ECO:0000313|EMBL:ABG31797.1, ECO:0000313|Proteomes:UP000007029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33942 / OCh 114 {ECO:0000313|Proteomes:UP000007029};
RX   PubMed=17098896; DOI=10.1128/JB.01390-06;
RA   Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., Ramos H.,
RA   Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., Shah M.K.,
RA   O'huallachain M.E., Lince M.T., Blankenship R.E., Beatty J.T.,
RA   Touchman J.W.;
RT   "The complete genome sequence of Roseobacter denitrificans reveals a
RT   mixotrophic rather than photosynthetic metabolism.";
RL   J. Bacteriol. 189:683-690(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; CP000362; ABG31797.1; -; Genomic_DNA.
DR   RefSeq; WP_011568414.1; NZ_FOOO01000003.1.
DR   AlphaFoldDB; Q167P6; -.
DR   STRING; 375451.RD1_2203; -.
DR   KEGG; rde:RD1_2203; -.
DR   eggNOG; COG1396; Bacteria.
DR   eggNOG; COG3800; Bacteria.
DR   HOGENOM; CLU_046383_0_0_5; -.
DR   OrthoDB; 1123084at2; -.
DR   Proteomes; UP000007029; 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:SF23; HTH-TYPE TRANSCRIPTIONAL REGULATOR PRPR; 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:UP000007029};
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   468 AA;  52317 MW;  85321A1465D8971B CRC64;
     MSKTLVGPQL RQLRRSFNHT QAEMARQLGV SAAYINLLEN NQRSLSVKML MELTESYGID
     WRSLVNDSEI THLADLRTAV RDPIFEGDTP DLQEMRAALD HAPKLVDLFL QLYRNHAKLR
     DNMRSVTAAG GVAEMMVTSP ETAIYDFFRN HANYFSDLEL AADSARSAVG GRQDDIYGNL
     KRHLKNAFGI EVEIMGVDKM PEALRIFAED QGRVELSEAL DQINRNFQLA HVLALVSCAG
     LLDKLSASAQ IPTQKGQARC RVELANYFAA AFMMPYDDVL RVARDTQYDI DRIATTFGVS
     FEQACQRLTT LQRKGAQGVP FFFLRTDTSG NVTKRFNATA FTLAEQGGSC PVWNIHSAFI
     SPGRIVAQMV ELPDAGQFFT ISRTSDRPVV SRHTPDRRRV VTLGCERAHV DQIGYAAPLN
     IEDRANIAKI GINCHICPRQ ACSERAHEPL HVNLPVDANR RGSTRYES
//