ID   TYRR_CITBR              Reviewed;         514 AA.
AC   O54426;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=HTH-type transcriptional regulatory protein TyrR {ECO:0000250|UniProtKB:P07604};
GN   Name=tyrR {ECO:0000303|Ref.1};
OS   Citrobacter braakii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter; Citrobacter freundii complex.
OX   NCBI_TaxID=57706;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29063;
RA   Bai Q., Somerville R.L.;
RT   "Cloning and characterization of the tyrR genes of Citrobacter braakii and
RT   Salmonella typhimurium.";
RL   Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Dual transcriptional regulator of the TyrR regulon, which
CC       includes a number of genes coding for proteins involved in the
CC       biosynthesis or transport of the three aromatic amino acids,
CC       phenylalanine, tyrosine and tryptophan. These three aromatic amino
CC       acids act as effectors which bind to the TyrR protein to form an active
CC       regulatory protein. Acts by binding specifically to TyrR boxes in the
CC       promoter region of the target genes. {ECO:0000250|UniProtKB:P07604}.
CC   -!- SUBUNIT: Homodimer. In presence of tyrosine (or high concentrations of
CC       phenylalanine or tryptophan) and ATP, it self-associates to form an
CC       hexamer. {ECO:0000250|UniProtKB:P07604}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P07604}.
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DR   EMBL; U90140; AAB93868.1; -; Genomic_DNA.
DR   AlphaFoldDB; O54426; -.
DR   SMR; O54426; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR030828; HTH_TypR.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR002078; Sigma_54_int.
DR   InterPro; IPR025943; Sigma_54_int_dom_ATP-bd_2.
DR   Pfam; PF18024; HTH_50; 1.
DR   Pfam; PF00158; Sigma54_activat; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF55021; SSF55021; 1.
DR   SUPFAM; SSF55785; SSF55785; 1.
DR   TIGRFAMs; TIGR04381; HTH_TypR; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS00676; SIGMA54_INTERACT_2; 1.
DR   PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE   3: Inferred from homology;
KW   Activator; Aromatic hydrocarbons catabolism; ATP-binding; Cytoplasm;
KW   DNA-binding; Nucleotide-binding; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..514
FT                   /note="HTH-type transcriptional regulatory protein TyrR"
FT                   /id="PRO_0000081338"
FT   DOMAIN          2..72
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   DOMAIN          78..120
FT                   /note="PAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          206..428
FT                   /note="Sigma-54 factor interaction"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   DNA_BIND        482..502
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000250|UniProtKB:P07604"
FT   BINDING         234..241
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   BINDING         290..299
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
SQ   SEQUENCE   514 AA;  57863 MW;  7BE29B6C3D41A06B CRC64;
     MRLEVFCEDR LGLTRELLDL LVLRSIDLRG IEIDPIGRIY LNFAELEFTN FSSLMAEIRR
     ISGVTDVRTV PWMPSEREHL ALSALLEALP EPVLSLDMKS KIEMANPASC QLFAHTQDRM
     RNHTAAQLIN GFNFQRWLES NPQDSHSEHV VINGQNFLME ITPVHLQGEN QEQMLTGAVV
     MLRSTIRMGR QLQNMTTQDL SAFSQIIAVS AKMKHVVEQA RKLATLSAPL LITGNTGTGK
     DLFAHACHLA SPRASKPYLA LNCASIPEDA VESELFGHAP EGKKGFFEQA NGGSVLLDEI
     GEMSPRMQTK LLRFLNDGTF RRVGEDHEVH VDVRVICATQ KNLVEMVQKG LFREDLYYRL
     NVLTLNLPPL RDLPADIMPL TELFVARFAD EQGVPRPKLS ADLSTVLTRY GWPGNVRHVK
     NAIYRALTQL EGYELRPQDI LLPDYDAATV AVGEEVMEGS LDEITSRFER SVLTQLYMNY
     PSTRKLAKRL GVSHTAIANK LREYGLSQQK KSEE