TYRR_ENTAG
ID TYRR_ENTAG Reviewed; 521 AA.
AC Q9ZIB7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=HTH-type transcriptional regulatory protein TyrR {ECO:0000305};
GN Name=tyrR {ECO:0000303|PubMed:11055921};
OS Enterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea; Pantoea agglomerans group.
OX NCBI_TaxID=549;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF VAL-67; TYR-72;
RP ASP-97; GLU-201; ILE-402 AND VAL-499.
RC STRAIN=ATCC 21434 / AJ 2985;
RX PubMed=11055921; DOI=10.1128/aem.66.11.4764-4771.2000;
RA Katayama T., Suzuki H., Koyanagi T., Kumagai H.;
RT "Cloning and random mutagenesis of the Erwinia herbicola tyrR gene for
RT high-level expression of tyrosine phenol-lyase.";
RL Appl. Environ. Microbiol. 66:4764-4771(2000).
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; AF035010; AAD02000.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9ZIB7; -.
DR SMR; Q9ZIB7; -.
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 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 1: Evidence at protein level;
KW Activator; Aromatic hydrocarbons catabolism; ATP-binding; Cytoplasm;
KW DNA-binding; Nucleotide-binding; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..521
FT /note="HTH-type transcriptional regulatory protein TyrR"
FT /id="PRO_0000081340"
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 207..436
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT DNA_BIND 489..509
FT /note="H-T-H motif"
FT /evidence="ECO:0000250|UniProtKB:P07604"
FT BINDING 235..242
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT BINDING 298..307
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT MUTAGEN 67
FT /note="V->A: Decrease in ability to repress DNA
FT transcription. Loss of activity; when associated with C-72
FT and G-201."
FT /evidence="ECO:0000269|PubMed:11055921"
FT MUTAGEN 72
FT /note="Y->C: Decrease in ability to repress DNA
FT transcription. Loss of activity; when associated with A-67
FT and G-201."
FT /evidence="ECO:0000269|PubMed:11055921"
FT MUTAGEN 97
FT /note="D->G: Decrease in ability to repress DNA
FT transcription; when associated with V-402."
FT /evidence="ECO:0000269|PubMed:11055921"
FT MUTAGEN 201
FT /note="E->G: No effect. Loss of activity; when associated
FT with A-67 and C-72."
FT /evidence="ECO:0000269|PubMed:11055921"
FT MUTAGEN 402
FT /note="I->V: Decrease in ability to repress DNA
FT transcription; when associated with G-97."
FT /evidence="ECO:0000269|PubMed:11055921"
FT MUTAGEN 499
FT /note="V->I: No effect."
FT /evidence="ECO:0000269|PubMed:11055921"
SQ SEQUENCE 521 AA; 59023 MW; 05896D0CFF5314BE CRC64;
MRLEVFCQDR IGLARELLDL LVARSIDLRG IEVAASGRIY LNFSTLEFEQ FSNLMAEIRR
TPGVTDVRTV PYMPSEREHR VLSALLVAMP EPVFSVDLRT KVELANPAAQ NLFNLDENKI
RNFTADHLIN GFNFARWLES ERVQAQAQHV VIEGRDFLME AHPIYLSEDN DQADQLVGAM
VMLKSTARMG RQLQNLVVTD ETEFDHIVAV TPRMRQVVEQ ARKLAMHDAP LLIIGDTGTG
KDMLARACHL RSARGKMPFL ALNCASLPDD VAESELFGHA AGAYPNALEG KKGFFEQANG
GSVLLDEIGE MSPTMQTKLL RFLNDGTFRR VGEEHEVHVN VRVICATQKN LFELVQRGEF
REDLFYRLNV LTLNLPPLRE RVQDIMPLTE IFVARFADEQ GIPRPRLSSQ LNAFLMRYNW
PGNVRQLKNA LYRALTQLEG HELRPQDIVL PEQALDVSLG EEAMEGTLDQ ITSRFERSIL
TRLYLSYPST RKLAKRLGVS HTAIANKLRE YGLGQKRGDN E
