TYRR_SALTY
ID TYRR_SALTY Reviewed; 513 AA.
AC P0A2D7; O54427;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=HTH-type transcriptional regulatory protein TyrR {ECO:0000250|UniProtKB:P07604};
GN Name=tyrR {ECO:0000303|Ref.1}; OrderedLocusNames=STM1683;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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; U90141; AAB93869.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20600.1; -; Genomic_DNA.
DR RefSeq; NP_460641.1; NC_003197.2.
DR RefSeq; WP_001235493.1; NC_003197.2.
DR AlphaFoldDB; P0A2D7; -.
DR SMR; P0A2D7; -.
DR STRING; 99287.STM1683; -.
DR PaxDb; P0A2D7; -.
DR EnsemblBacteria; AAL20600; AAL20600; STM1683.
DR GeneID; 1253201; -.
DR KEGG; stm:STM1683; -.
DR PATRIC; fig|99287.12.peg.1777; -.
DR HOGENOM; CLU_000445_8_2_6; -.
DR OMA; CQNRIGI; -.
DR PhylomeDB; P0A2D7; -.
DR BioCyc; SENT99287:STM1683-MON; -.
DR Proteomes; UP000001014; Chromosome.
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; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR InterPro; IPR025943; Sigma_54_int_dom_ATP-bd_2.
DR InterPro; IPR025944; Sigma_54_int_dom_CS.
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; PS00675; SIGMA54_INTERACT_1; 1.
DR PROSITE; PS00676; SIGMA54_INTERACT_2; 1.
DR PROSITE; PS00688; SIGMA54_INTERACT_3; 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; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..513
FT /note="HTH-type transcriptional regulatory protein TyrR"
FT /id="PRO_0000081342"
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"
FT CONFLICT 111
FT /note="Q -> H (in Ref. 1; AAB93869)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="H -> N (in Ref. 1; AAB93869)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="N -> S (in Ref. 1; AAB93869)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="S -> G (in Ref. 1; AAB93869)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="M -> I (in Ref. 1; AAB93869)"
FT /evidence="ECO:0000305"
FT CONFLICT 427
FT /note="L -> V (in Ref. 1; AAB93869)"
FT /evidence="ECO:0000305"
FT CONFLICT 480
FT /note="Y -> N (in Ref. 1; AAB93869)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 513 AA; 57680 MW; 244357570666A59B CRC64;
MRLEVFCEDR LGLTRELLDL LVLRSIDLRG IEIDPIGRIY LNFAELEFTD FSSLMAEIRR
ISGVTDVRTV PWMPSEREHL ALSALLEALP EPVLSLDMKS KVEMANPASC QLFAQSQERM
RHHTAAQLIN GFNFQRWLDG NPQSSHNEHV VINGQNFLME ITPVHLQNEN DEYVLTGAVV
MLRSTIRMGQ QLQNLSTQDL SAFSQIIAVS AKMKHVVEQA RKLAMLSAPL LITGDTGTGK
DLFAYACHQA SPRSAKPYLA LNCASIPEDA VESELFGHAP EGKKGFFEQA NGGSVLLDEI
GEMSPRMQAK LLRFLNDGTF RRVGEDHEIH VDVRVICATQ KNLVELVQKG LFREDLYYRL
NVLTLNLPPL RDCPQDIMPL TELFVARFAD EQGVPRPKLS ADLSTVLTRY GWPGNVRQLK
NAIYRALTQL EGYELRPQDI LLPDYDAATV AVGEDAMEGS LDDITSRFER SVLTQLYRSY
PSTRKLAKRL GVSHTAIANK LREYGLSQKK GEE
