TYRR_HAEIN
ID TYRR_HAEIN Reviewed; 318 AA.
AC P44694;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=HTH-type transcriptional regulatory protein TyrR {ECO:0000305};
GN Name=tyrR {ECO:0000303|PubMed:9226720}; OrderedLocusNames=HI_0410;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP PROTEIN SEQUENCE OF 2-7, FUNCTION, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=9226720; DOI=10.1006/prep.1997.0757;
RA Zhu Q., Zhao S., Somerville R.L.;
RT "Expression, purification, and functional analysis of the TyrR protein of
RT Haemophilus influenzae.";
RL Protein Expr. Purif. 10:237-246(1997).
RN [3]
RP STRUCTURE BY NMR OF 258-318.
RX PubMed=11344327; DOI=10.1110/ps.45301;
RA Wang Y., Zhao S., Somerville R.L., Jardetzky O.;
RT "Solution structure of the DNA-binding domain of the TyrR protein of
RT Haemophilus influenzae.";
RL Protein Sci. 10:592-598(2001).
CC -!- FUNCTION: Transcriptional regulator of the TyrR regulon, which includes
CC a number of genes coding for proteins involved in the biosynthesis or
CC transport of the three aromatic amino acids, phenylalanine, tyrosine
CC and tryptophan. These three aromatic amino acids act as effectors which
CC bind to the TyrR protein to form an active regulatory protein (By
CC similarity). Acts by binding specifically to TyrR boxes in the promoter
CC region of the target genes (PubMed:9226720). Can efficiently repress
CC the transcription of the aroF promoter, but lacks the ability to
CC function as a transcriptional activator (PubMed:9226720).
CC {ECO:0000250|UniProtKB:P07604, ECO:0000269|PubMed:9226720}.
CC -!- ACTIVITY REGULATION: The DNA binding ability is drastically reduced in
CC the presence of ATP. Tyrosine further reduces the binding affinity of
CC TyrR in the presence of ATP. {ECO:0000269|PubMed:9226720}.
CC -!- SUBUNIT: Homodimer (PubMed:9226720). In presence of tyrosine (or high
CC concentrations of phenylalanine or tryptophan) and ATP, it self-
CC associates to form an hexamer (By similarity).
CC {ECO:0000250|UniProtKB:P07604, ECO:0000269|PubMed:9226720}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- CAUTION: Lacks a counterpart to the N-terminal domain of the TyrR
CC protein of E.coli. {ECO:0000305|PubMed:9226720}.
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DR EMBL; L42023; AAC22069.1; -; Genomic_DNA.
DR PIR; C64066; C64066.
DR RefSeq; NP_438572.1; NC_000907.1.
DR RefSeq; WP_005693758.1; NC_000907.1.
DR PDB; 1G2H; NMR; -; A=258-318.
DR PDBsum; 1G2H; -.
DR AlphaFoldDB; P44694; -.
DR BMRB; P44694; -.
DR SMR; P44694; -.
DR STRING; 71421.HI_0410; -.
DR PRIDE; P44694; -.
DR EnsemblBacteria; AAC22069; AAC22069; HI_0410.
DR KEGG; hin:HI_0410; -.
DR PATRIC; fig|71421.8.peg.429; -.
DR eggNOG; COG3283; Bacteria.
DR HOGENOM; CLU_000445_0_7_6; -.
DR OMA; FFEYADG; -.
DR PhylomeDB; P44694; -.
DR BioCyc; HINF71421:G1GJ1-425-MON; -.
DR EvolutionaryTrace; P44694; -.
DR Proteomes; UP000000579; 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 Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR030828; HTH_TypR.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002078; Sigma_54_int.
DR InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR Pfam; PF18024; HTH_50; 1.
DR Pfam; PF00158; Sigma54_activat; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR04381; HTH_TypR; 1.
DR PROSITE; PS00675; SIGMA54_INTERACT_1; 1.
DR PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; ATP-binding; Cytoplasm;
KW Direct protein sequencing; DNA-binding; Nucleotide-binding;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..318
FT /note="HTH-type transcriptional regulatory protein TyrR"
FT /id="PRO_0000081343"
FT DOMAIN 15..239
FT /note="Sigma-54 factor interaction; truncated"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT DNA_BIND 292..312
FT /note="H-T-H motif"
FT /evidence="ECO:0000250|UniProtKB:P07604"
FT BINDING 43..50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT BINDING 101..110
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:1G2H"
FT HELIX 277..289
FT /evidence="ECO:0007829|PDB:1G2H"
FT HELIX 293..299
FT /evidence="ECO:0007829|PDB:1G2H"
FT HELIX 305..312
FT /evidence="ECO:0007829|PDB:1G2H"
FT TURN 313..315
FT /evidence="ECO:0007829|PDB:1G2H"
SQ SEQUENCE 318 AA; 35954 MW; 5AB2AD8D994044F8 CRC64;
MTISKFNPQK PFECFIVQSE AMKSAVENAK RFAMFDAPLL IQGETGSGKD LLAKACHYQS
LRRDKKFIAV NCAGLPDEDA ESEMFGRKVG DSETIGFFEY ANKGTVLLDG IAELSLSLQA
KLLRFLTDGS FRRVGEEKEH YANVRVICTS QVPLHLLVEQ GKVRADLFHR LNVLTINVPA
LRDRMADIEP LAQGFLQEIS EELKIAKPTF DKDFLLYLQK YDWKGNVREL YNTLYRACSL
VQDNHLTIES LNLALPQSAV ISLDEFENKT LDEIIGFYEA QVLKLFYAEY PSTRKLAQRL
GVSHTAIANK LKQYGIGK
