ID   TAUR_RHOCB              Reviewed;         484 AA.
AC   D5AKX9;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=HTH-type transcriptional regulator TauR {ECO:0000305};
GN   Name=tauR {ECO:0000303|PubMed:17981966};
GN   OrderedLocusNames=RCAP_rcc02239 {ECO:0000312|EMBL:ADE85969.1};
OS   Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=272942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX   PubMed=20418398; DOI=10.1128/jb.00366-10;
RA   Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA   Haselkorn R.;
RT   "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT   Rhodobacter capsulatus SB 1003.";
RL   J. Bacteriol. 192:3545-3546(2010).
RN   [2]
RP   FUNCTION, DNA-BINDING, AND INDUCTION.
RC   STRAIN=B10S;
RX   PubMed=17981966; DOI=10.1128/jb.01510-07;
RA   Wiethaus J., Schubert B., Pfaender Y., Narberhaus F., Masepohl B.;
RT   "The GntR-like regulator TauR activates expression of taurine utilization
RT   genes in Rhodobacter capsulatus.";
RL   J. Bacteriol. 190:487-493(2008).
CC   -!- FUNCTION: Transcriptional activator, which is essential for taurine-
CC       dependent expression of the tpa-tauR-xsc operon. Acts by binding to
CC       direct repeats in the promoter region. {ECO:0000269|PubMed:17981966}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P94426};
CC   -!- INDUCTION: Induced by taurine. Positively autoregulated.
CC       {ECO:0000269|PubMed:17981966}.
CC   -!- MISCELLANEOUS: In vitro, taurine does not influence the binding of TauR
CC       to the tpa promoter. {ECO:0000269|PubMed:17981966}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the class-I
CC       pyridoxal-phosphate-dependent aminotransferase family. {ECO:0000305}.
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DR   EMBL; CP001312; ADE85969.1; -; Genomic_DNA.
DR   RefSeq; WP_013067948.1; NC_014034.1.
DR   AlphaFoldDB; D5AKX9; -.
DR   SMR; D5AKX9; -.
DR   STRING; 272942.RCAP_rcc02239; -.
DR   PRIDE; D5AKX9; -.
DR   EnsemblBacteria; ADE85969; ADE85969; RCAP_rcc02239.
DR   GeneID; 31491081; -.
DR   KEGG; rcp:RCAP_rcc02239; -.
DR   eggNOG; COG1167; Bacteria.
DR   HOGENOM; CLU_017584_0_1_5; -.
DR   OMA; CDYVYVT; -.
DR   OrthoDB; 1320028at2; -.
DR   Proteomes; UP000002361; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   CDD; cd07377; WHTH_GntR; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR000524; Tscrpt_reg_HTH_GntR.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   Pfam; PF00392; GntR; 1.
DR   SMART; SM00345; HTH_GNTR; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS50949; HTH_GNTR; 1.
PE   1: Evidence at protein level;
KW   Activator; Aminotransferase; DNA-binding; Pyridoxal phosphate;
KW   Reference proteome; Transcription; Transcription regulation; Transferase.
FT   CHAIN           1..484
FT                   /note="HTH-type transcriptional regulator TauR"
FT                   /id="PRO_0000430551"
FT   DOMAIN          16..84
FT                   /note="HTH gntR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00307"
FT   DNA_BIND        44..63
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00307"
FT   MOD_RES         330
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   484 AA;  52842 MW;  8683C9F4982DEE18 CRC64;
     MAIPVESFFL APGGQGSLQH RLRQMVTEGI LSGRFRPGDR MPSTRALAAH LGVARITVTL
     AYADLVASDY LLARGRSGTF VSAAAPDARK ARPLPRDGAR TDWARLLHPR AQGLPRPDRP
     RDWSLYRYPF IYGQADPELF DHQNWRACAL QALGRREFHR LSADCYDEDD PLLVEYILRH
     ILPRRGIAAV PSEVLITMGA QNGLWLAAQV LLGPGERAAM ENPGYPGTRA VLGTTGAEVL
     SVDVDDRGLV PAQLPARLKL VVTTASHHCP TNATLPVERR LALLAAAEAG DFLILEDDYE
     FEMSFLQSAA PSLKSLDAGG RVVHVGSFSK SLFPGLRLGY LVAPAPFVAA VRALRATVLR
     HPPGQLQRTL ALFLSLGHYD ALVARMKAAY RLRREVMTKA IEDNGLQIAG QGGFGGSSFW
     MQAPGAVDTE DLALRLRAEG VLIEPGRVFF DPARERRNFY RLAYSSIGPA AIPEGIARIA
     RALR