TYRR_ECOLI
ID TYRR_ECOLI Reviewed; 513 AA.
AC P07604;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=HTH-type transcriptional regulatory protein TyrR {ECO:0000305};
GN Name=tyrR {ECO:0000303|PubMed:4887504}; OrderedLocusNames=b1323, JW1316;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3001057; DOI=10.1016/s0021-9258(17)42487-2;
RA Cornish E.C., Argyropoulos V.P., Pittard J., Davidson B.E.;
RT "Structure of the Escherichia coli K12 regulatory gene tyrR. Nucleotide
RT sequence and sites of initiation of transcription and translation.";
RL J. Biol. Chem. 261:403-410(1986).
RN [2]
RP SEQUENCE REVISION.
RA Ganesan S.;
RL Thesis (1989), University of Melbourne, Australia.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP PROTEIN SEQUENCE OF 1-16, FUNCTION, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=8106498; DOI=10.1016/s0021-9258(17)37671-8;
RA Argaet V.P., Wilson T.J., Davidson B.E.;
RT "Purification of the Escherichia coli regulatory protein TyrR and analysis
RT of its interactions with ATP, tyrosine, phenylalanine, and tryptophan.";
RL J. Biol. Chem. 269:5171-5178(1994).
RN [7]
RP FUNCTION IN REGULATION OF TYROSINE BIOSYNTHESIS.
RC STRAIN=K12;
RX PubMed=4887504; DOI=10.1128/jb.97.3.1234-1241.1969;
RA Wallace B.J., Pittard J.;
RT "Regulator gene controlling enzymes concerned in tyrosine biosynthesis in
RT Escherichia coli.";
RL J. Bacteriol. 97:1234-1241(1969).
RN [8]
RP FUNCTION IN REGULATION OF AROMATIC AMINO ACID BIOSYNTHESIS.
RX PubMed=4399341; DOI=10.1128/jb.108.1.386-399.1971;
RA Brown K.D., Somerville R.L.;
RT "Repression of aromatic amino acid biosynthesis in Escherichia coli K-12.";
RL J. Bacteriol. 108:386-399(1971).
RN [9]
RP FUNCTION IN REGULATION OF AROMATIC AMINO ACID TRANSPORT.
RC STRAIN=K12;
RX PubMed=334742; DOI=10.1128/jb.132.2.453-461.1977;
RA Whipp M.J., Pittard A.J.;
RT "Regulation of aromatic amino acid transport systems in Escherichia coli K-
RT 12.";
RL J. Bacteriol. 132:453-461(1977).
RN [10]
RP INDUCTION.
RC STRAIN=K12;
RX PubMed=6120934; DOI=10.1128/jb.150.1.70-75.1982;
RA Camakaris H., Pittard J.;
RT "Autoregulation of the tyrR gene.";
RL J. Bacteriol. 150:70-75(1982).
RN [11]
RP FUNCTION IN TYRP REGULATION, AND DNA-BINDING.
RC STRAIN=K12;
RX PubMed=1860819; DOI=10.1128/jb.173.16.5068-5078.1991;
RA Andrews A.E., Lawley B., Pittard A.J.;
RT "Mutational analysis of repression and activation of the tyrP gene in
RT Escherichia coli.";
RL J. Bacteriol. 173:5068-5078(1991).
RN [12]
RP FUNCTION IN MTR ACTIVATION.
RX PubMed=2061290; DOI=10.1128/jb.173.13.4133-4143.1991;
RA Sarsero J.P., Wookey P.J., Pittard A.J.;
RT "Regulation of expression of the Escherichia coli K-12 mtr gene by TyrR
RT protein and Trp repressor.";
RL J. Bacteriol. 173:4133-4143(1991).
RN [13]
RP FUNCTION, DNA-BINDING, AND DOMAIN.
RX PubMed=8449883; DOI=10.1128/jb.175.6.1767-1776.1993;
RA Yang J., Ganesan S., Sarsero J., Pittard A.J.;
RT "A genetic analysis of various functions of the TyrR protein of Escherichia
RT coli.";
RL J. Bacteriol. 175:1767-1776(1993).
RN [14]
RP FUNCTION AS AN ACTIVATOR, DOMAIN, AND MUTAGENESIS OF ARG-2; VAL-5; CYS-7;
RP ASP-9; ARG-10 AND GLU-16.
RX PubMed=8407813; DOI=10.1128/jb.175.19.6372-6375.1993;
RA Yang J., Camakaris H., Pittard A.J.;
RT "Mutations in the tyrR gene of Escherichia coli which affect TyrR-mediated
RT activation but not TyrR-mediated repression.";
RL J. Bacteriol. 175:6372-6375(1993).
RN [15]
RP DOMAINS, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8444880; DOI=10.1016/s0021-9258(18)53499-2;
RA Cui J., Somerville R.L.;
RT "The TyrR protein of Escherichia coli, analysis by limited proteolysis of
RT domain structure and ligand-mediated conformational changes.";
RL J. Biol. Chem. 268:5040-5047(1993).
RN [16]
RP FUNCTION, AND DNA-BINDING.
RC STRAIN=K12;
RX PubMed=7961453; DOI=10.1128/jb.176.22.6921-6930.1994;
RA Lawley B., Pittard A.J.;
RT "Regulation of aroL expression by TyrR protein and Trp repressor in
RT Escherichia coli K-12.";
RL J. Bacteriol. 176:6921-6930(1994).
RN [17]
RP SUBUNIT.
RX PubMed=8176727; DOI=10.1006/jmbi.1994.1294;
RA Wilson T.J., Maroudas P., Howlett G.J., Davidson B.E.;
RT "Ligand-induced self-association of the Escherichia coli regulatory protein
RT TyrR.";
RL J. Mol. Biol. 238:309-318(1994).
RN [18]
RP FUNCTION IN TYRP REGULATION.
RX PubMed=7798138; DOI=10.1128/jb.177.1.238-241.1995;
RA Lawley B., Fujita N., Ishihama A., Pittard A.J.;
RT "The TyrR protein of Escherichia coli is a class I transcription
RT activator.";
RL J. Bacteriol. 177:238-241(1995).
RN [19]
RP FUNCTION, AND SUBUNIT.
RX PubMed=8947567; DOI=10.1006/jmbi.1996.0607;
RA Bailey M.F., Davidson B.E., Minton A.P., Sawyer W.H., Howlett G.J.;
RT "The effect of self-association on the interaction of the Escherichia coli
RT regulatory protein TyrR with DNA.";
RL J. Mol. Biol. 263:671-684(1996).
RN [20]
RP FUNCTION, DOMAIN, AND MUTAGENESIS OF HIS-494 AND THR-495.
RX PubMed=10197993; DOI=10.1128/jb.181.8.2338-2345.1999;
RA Hwang J.S., Yang J., Pittard A.J.;
RT "Specific contacts between residues in the DNA-binding domain of the TyrR
RT protein and bases in the operator of the tyrP gene of Escherichia coli.";
RL J. Bacteriol. 181:2338-2345(1999).
RN [21]
RP SUBUNIT, AND DOMAIN.
RX PubMed=11923293; DOI=10.1074/jbc.m112184200;
RA Dixon M.P., Pau R.N., Howlett G.J., Dunstan D.E., Sawyer W.H.,
RA Davidson B.E.;
RT "The central domain of Escherichia coli TyrR is responsible for
RT hexamerization associated with tyrosine-mediated repression of gene
RT expression.";
RL J. Biol. Chem. 277:23186-23192(2002).
RN [22]
RP FUNCTION IN AROP REGULATION.
RX PubMed=14614536;
RA Wang J.G., Fan C.S., Wu Y.Q., Jin R.L., Liu D.X., Shang L., Jiang P.H.;
RT "Regulation of aroP expression by tyrR gene in Escherichia coli.";
RL Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 35:993-997(2003).
RN [23]
RP FUNCTION IN TYRP REGULATION, AND DNA-BINDING.
RX PubMed=15049824; DOI=10.1111/j.1365-2958.2003.03965.x;
RA Yang J., Hwang J.S., Camakaris H., Irawaty W., Ishihama A., Pittard J.;
RT "Mode of action of the TyrR protein: repression and activation of the tyrP
RT promoter of Escherichia coli.";
RL Mol. Microbiol. 52:243-256(2004).
RN [24]
RP DOMAIN, AND MUTAGENESIS OF GLU-160; HIS-173; THR-176 AND SER-184.
RX PubMed=30680497; DOI=10.1007/s10529-019-02645-x;
RA Bai D., Ding D., Li J., Cong L., Zhang D.;
RT "Pinpointing the L-phenylalanine binding sites of TyrR using biosensors and
RT computer-aided simulation.";
RL Biotechnol. Lett. 41:401-408(2019).
RN [25]
RP REVIEW.
RX PubMed=1943694; DOI=10.1111/j.1365-2958.1991.tb01904.x;
RA Pittard A.J., Davidson B.E.;
RT "TyrR protein of Escherichia coli and its role as repressor and
RT activator.";
RL Mol. Microbiol. 5:1585-1592(1991).
RN [26]
RP REVIEW.
RX PubMed=15612913; DOI=10.1111/j.1365-2958.2004.04385.x;
RA Pittard J., Camakaris H., Yang J.;
RT "The TyrR regulon.";
RL Mol. Microbiol. 55:16-26(2005).
RN [27] {ECO:0007744|PDB:2JHE}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-190, AND DOMAIN.
RX PubMed=17222426; DOI=10.1016/j.jmb.2006.12.018;
RA Verger D., Carr P.D., Kwok T., Ollis D.L.;
RT "Crystal structure of the N-terminal domain of the TyrR transcription
RT factor responsible for gene regulation of aromatic amino acid biosynthesis
RT and transport in Escherichia coli K12.";
RL J. Mol. Biol. 367:102-112(2007).
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 (PubMed:4887504, PubMed:4399341,
CC PubMed:334742, PubMed:1860819, PubMed:8449883, PubMed:7961453,
CC PubMed:7798138, PubMed:14614536, PubMed:15049824). These three aromatic
CC amino acids act as effectors which bind to the TyrR protein to form an
CC active regulatory protein (PubMed:4399341, PubMed:334742,
CC PubMed:1860819, PubMed:8106498, PubMed:7961453). Modulates the
CC expression of at least eight unlinked transcription units, including
CC aroF, aroG, aroLM, aroP, mtr, tyrA, tyrB and tyrP (PubMed:4887504,
CC PubMed:4399341, PubMed:334742, PubMed:1860819, PubMed:8449883,
CC PubMed:7961453, PubMed:7798138, PubMed:14614536, PubMed:15049824). In
CC most cases TyrR acts as a repressor, but positive effects have been
CC observed on the tyrP gene, which is repressed in the presence of
CC tyrosine and activated at high phenylalanine concentrations
CC (PubMed:334742, PubMed:1860819, PubMed:8449883, PubMed:7798138,
CC PubMed:15049824, PubMed:8407813). Is also involved in activation, but
CC not repression, of mtr expression in association with phenylalanine or
CC tyrosine (PubMed:2061290, PubMed:8449883, PubMed:8407813). Acts by
CC binding specifically to TyrR boxes in the promoter region of the target
CC genes (PubMed:1860819, PubMed:8449883, PubMed:7961453, PubMed:8947567,
CC PubMed:10197993). {ECO:0000269|PubMed:10197993,
CC ECO:0000269|PubMed:14614536, ECO:0000269|PubMed:15049824,
CC ECO:0000269|PubMed:1860819, ECO:0000269|PubMed:2061290,
CC ECO:0000269|PubMed:334742, ECO:0000269|PubMed:4399341,
CC ECO:0000269|PubMed:4887504, ECO:0000269|PubMed:7798138,
CC ECO:0000269|PubMed:7961453, ECO:0000269|PubMed:8106498,
CC ECO:0000269|PubMed:8407813, ECO:0000269|PubMed:8449883,
CC ECO:0000269|PubMed:8947567}.
CC -!- ACTIVITY REGULATION: Binding of ATP strongly enhances the affinity of
CC TyrR for tyrosine. {ECO:0000269|PubMed:8106498}.
CC -!- SUBUNIT: Homodimer (PubMed:8106498, PubMed:8176727, PubMed:8947567,
CC PubMed:11923293). In presence of tyrosine (or high concentrations of
CC phenylalanine or tryptophan) and ATP, it self-associates to form an
CC hexamer (PubMed:8176727, PubMed:8947567, PubMed:11923293). At low
CC tyrosine concentrations, homodimers can bind to certain recognition
CC sequences referred to as 'strong TyrR boxes' (PubMed:8176727).
CC Homohexamers are the active repressing species, interacting with two or
CC three tyrR boxes in the targeted regulatory DNA, including 'strong TyrR
CC boxes' and lower-affinity sites called 'weak TyrR boxes'
CC (PubMed:8176727). {ECO:0000269|PubMed:11923293,
CC ECO:0000269|PubMed:8106498, ECO:0000269|PubMed:8176727,
CC ECO:0000269|PubMed:8947567}.
CC -!- INTERACTION:
CC P07604; P06959: aceF; NbExp=2; IntAct=EBI-559274, EBI-542707;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Interacts with its own promoter-operator region.
CC Autogenously regulated by a mechanism that gives similar rates of
CC expression of tyrR irrespective of concentration of the aromatic amino
CC acids. {ECO:0000269|PubMed:6120934}.
CC -!- DOMAIN: Contains an N-terminal domain (1-190), a central domain (206-
CC 433) and a C-terminal region (444-513) (PubMed:8449883, PubMed:8444880,
CC PubMed:17222426). The N-terminal domain is required for transcription
CC activation functions, dimerization and ATP-independent aromatic amino
CC acid binding (PubMed:8449883, PubMed:8407813, PubMed:8444880,
CC PubMed:17222426, PubMed:30680497). The central domain is involved in
CC ATP binding and hydrolysis, and is responsible for ATP-dependent
CC tyrosine binding and hexamerization associated with tyrosine-mediated
CC repression functions (PubMed:8449883, PubMed:8444880, PubMed:11923293).
CC The C-terminal region contains a classical helix-turn-helix motif
CC responsible for binding to DNA targets known as TyrR boxes
CC (PubMed:8449883, PubMed:10197993). {ECO:0000269|PubMed:10197993,
CC ECO:0000269|PubMed:11923293, ECO:0000269|PubMed:17222426,
CC ECO:0000269|PubMed:30680497, ECO:0000269|PubMed:8407813,
CC ECO:0000269|PubMed:8444880, ECO:0000269|PubMed:8449883}.
CC -!- MISCELLANEOUS: Regulation of individual transcription units within the
CC regulon reflects their physiological function and is determined by the
CC position and nature of the recognition sites (TyrR boxes) associated
CC with each of the promoters. {ECO:0000305|PubMed:15612913}.
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DR EMBL; M12114; AAA24706.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74405.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA14905.1; -; Genomic_DNA.
DR PIR; A47086; RGECAY.
DR RefSeq; NP_415839.1; NC_000913.3.
DR RefSeq; WP_001300658.1; NZ_STEB01000005.1.
DR PDB; 2JHE; X-ray; 2.30 A; A/B/C/D=1-190.
DR PDBsum; 2JHE; -.
DR AlphaFoldDB; P07604; -.
DR BMRB; P07604; -.
DR SMR; P07604; -.
DR BioGRID; 4260150; 11.
DR DIP; DIP-11062N; -.
DR IntAct; P07604; 4.
DR STRING; 511145.b1323; -.
DR jPOST; P07604; -.
DR PaxDb; P07604; -.
DR PRIDE; P07604; -.
DR EnsemblBacteria; AAC74405; AAC74405; b1323.
DR EnsemblBacteria; BAA14905; BAA14905; BAA14905.
DR GeneID; 945879; -.
DR KEGG; ecj:JW1316; -.
DR KEGG; eco:b1323; -.
DR PATRIC; fig|1411691.4.peg.955; -.
DR EchoBASE; EB1035; -.
DR eggNOG; COG3283; Bacteria.
DR HOGENOM; CLU_000445_8_2_6; -.
DR InParanoid; P07604; -.
DR OMA; CQNRIGI; -.
DR PhylomeDB; P07604; -.
DR BioCyc; EcoCyc:PD00413; -.
DR EvolutionaryTrace; P07604; -.
DR PRO; PR:P07604; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IDA:EcoCyc.
DR GO; GO:0003677; F:DNA binding; IDA:EcoCyc.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:EcoCyc.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:EcoCyc.
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; PF13188; PAS_8; 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; PS50112; PAS; 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 3D-structure; Activator; Aromatic hydrocarbons catabolism; ATP-binding;
KW Cytoplasm; Direct protein sequencing; DNA-binding; Nucleotide-binding;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..513
FT /note="HTH-type transcriptional regulatory protein TyrR"
FT /id="PRO_0000081339"
FT DOMAIN 2..72
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT DOMAIN 78..114
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:0000305|PubMed:8449883"
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 MUTAGEN 2
FT /note="R->A,S: Shows a decrease in activation of expression
FT of either mtr or tyrP. Does not affect repression of aroF."
FT /evidence="ECO:0000269|PubMed:8407813"
FT MUTAGEN 5
FT /note="V->P,F: Shows no activation of expression of either
FT mtr or tyrP. Does not affect repression of aroF."
FT /evidence="ECO:0000269|PubMed:8407813"
FT MUTAGEN 7
FT /note="C->R: Shows no activation of expression of either
FT mtr or tyrP. Does not affect repression of aroF."
FT /evidence="ECO:0000269|PubMed:8407813"
FT MUTAGEN 7
FT /note="C->S: Shows very little activation of expression of
FT either mtr or tyrP. Does not affect repression of aroF."
FT /evidence="ECO:0000269|PubMed:8407813"
FT MUTAGEN 9
FT /note="D->R: Shows very little activation of expression of
FT either mtr or tyrP. Does not affect repression of aroF."
FT /evidence="ECO:0000269|PubMed:8407813"
FT MUTAGEN 10
FT /note="R->I,S: Shows no activation of expression of either
FT mtr or tyrP. Does not affect repression of aroF."
FT /evidence="ECO:0000269|PubMed:8407813"
FT MUTAGEN 16
FT /note="E->R: Shows very little activation of expression of
FT either mtr or tyrP. Does not affect repression of aroF."
FT /evidence="ECO:0000269|PubMed:8407813"
FT MUTAGEN 160
FT /note="E->F,L: Reduces the activation function to 65% of
FT the wild-type value. Does not affect repression of aroF."
FT /evidence="ECO:0000269|PubMed:30680497"
FT MUTAGEN 173
FT /note="H->L,V: Reduces the activation function to 73% of
FT the wild-type value. Does not affect repression of aroF."
FT /evidence="ECO:0000269|PubMed:30680497"
FT MUTAGEN 176
FT /note="T->E: Loss of activation and repression functions.
FT May affect the overall conformation of the protein."
FT /evidence="ECO:0000269|PubMed:30680497"
FT MUTAGEN 184
FT /note="S->V,L: Reduces the activation function to 45% of
FT the wild-type value. Does not affect repression of aroF."
FT /evidence="ECO:0000269|PubMed:30680497"
FT MUTAGEN 494
FT /note="H->A: Loss of affinity for the tyrP promoter."
FT /evidence="ECO:0000269|PubMed:10197993"
FT MUTAGEN 495
FT /note="T->A: Decreases binding affinity for the tyrP
FT promoter."
FT /evidence="ECO:0000269|PubMed:10197993"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:2JHE"
FT HELIX 13..23
FT /evidence="ECO:0007829|PDB:2JHE"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:2JHE"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:2JHE"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:2JHE"
FT HELIX 48..60
FT /evidence="ECO:0007829|PDB:2JHE"
FT STRAND 64..71
FT /evidence="ECO:0007829|PDB:2JHE"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:2JHE"
FT HELIX 77..88
FT /evidence="ECO:0007829|PDB:2JHE"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:2JHE"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:2JHE"
FT HELIX 107..113
FT /evidence="ECO:0007829|PDB:2JHE"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:2JHE"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:2JHE"
FT HELIX 134..139
FT /evidence="ECO:0007829|PDB:2JHE"
FT STRAND 146..152
FT /evidence="ECO:0007829|PDB:2JHE"
FT STRAND 155..164
FT /evidence="ECO:0007829|PDB:2JHE"
FT TURN 165..168
FT /evidence="ECO:0007829|PDB:2JHE"
FT STRAND 169..176
FT /evidence="ECO:0007829|PDB:2JHE"
FT HELIX 178..185
FT /evidence="ECO:0007829|PDB:2JHE"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:2JHE"
SQ SEQUENCE 513 AA; 57656 MW; B580A401C3A27866 CRC64;
MRLEVFCEDR LGLTRELLDL LVLRGIDLRG IEIDPIGRIY LNFAELEFES FSSLMAEIRR
IAGVTDVRTV PWMPSEREHL ALSALLEALP EPVLSVDMKS KVDMANPASC QLFGQKLDRL
RNHTAAQLIN GFNFLRWLES EPQDSHNEHV VINGQNFLME ITPVYLQDEN DQHVLTGAVV
MLRSTIRMGR QLQNVAAQDV SAFSQIVAVS PKMKHVVEQA QKLAMLSAPL LITGDTGTGK
DLFAYACHQA SPRAGKPYLA LNCASIPEDA VESELFGHAP EGKKGFFEQA NGGSVLLDEI
GEMSPRMQAK LLRFLNDGTF RRVGEDHEVH VDVRVICATQ KNLVELVQKG MFREDLYYRL
NVLTLNLPPL RDCPQDIMPL TELFVARFAD EQGVPRPKLA ADLNTVLTRY AWPGNVRQLK
NAIYRALTQL DGYELRPQDI LLPDYDAATV AVGEDAMEGS LDEITSRFER SVLTQLYRNY
PSTRKLAKRL GVSHTAIANK LREYGLSQKK NEE
