TRPI_PSEAE
ID TRPI_PSEAE Reviewed; 295 AA.
AC P11720; Q9I795;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 04-MAY-2001, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=HTH-type transcriptional regulator TrpI {ECO:0000305};
DE AltName: Full=TrpBA operon transcriptional activator {ECO:0000305};
GN Name=trpI {ECO:0000303|PubMed:2492495};
GN OrderedLocusNames=PA0037 {ECO:0000312|EMBL:AAG03427.1};
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PAC174;
RX PubMed=2492495; DOI=10.1128/jb.171.1.172-183.1989;
RA Chang M., Hadero A., Crawford I.P.;
RT "Sequence of the Pseudomonas aeruginosa trpI activator gene and relatedness
RT of trpI to other procaryotic regulatory genes.";
RL J. Bacteriol. 171:172-183(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DNA-BINDING.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=2107533; DOI=10.1093/nar/18.4.979;
RA Chang M., Crawford I.P.;
RT "The roles of indoleglycerol phosphate and the TrpI protein in the
RT expression of trpBA from Pseudomonas aeruginosa.";
RL Nucleic Acids Res. 18:979-988(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [4]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=1756720; DOI=10.1002/j.1460-2075.1991.tb04991.x;
RA Gao J., Gussin G.N.;
RT "Mutations in TrpI binding site II that differentially affect activation of
RT the trpBA promoter of Pseudomonas aeruginosa.";
RL EMBO J. 10:4137-4144(1991).
RN [5]
RP FUNCTION, DNA-BINDING, AND SUBUNIT.
RX PubMed=1900276; DOI=10.1128/jb.173.5.1590-1597.1991;
RA Chang M., Crawford I.P.;
RT "In vitro determination of the effect of indoleglycerol phosphate on the
RT interaction of purified TrpI protein with its DNA-binding sites.";
RL J. Bacteriol. 173:1590-1597(1991).
RN [6]
RP FUNCTION, DNA-BINDING, AND INDUCTION.
RX PubMed=1904858; DOI=10.1128/jb.173.12.3763-3769.1991;
RA Gao J.G., Gussin G.N.;
RT "Activation of the trpBA promoter of Pseudomonas aeruginosa by TrpI protein
RT in vitro.";
RL J. Bacteriol. 173:3763-3769(1991).
RN [7]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=9858743; DOI=10.1016/s0378-1119(98)00243-1;
RA Olekhnovich I., Gussin G.N.;
RT "Recognition of binding sites I and II by the TrpI activator protein of
RT pseudomonas aeruginosa: efficient binding to both sites requires InGP even
RT when site II is replaced by site I.";
RL Gene 223:247-255(1998).
CC -!- FUNCTION: Activates the expression of the trpBA genes, which encode the
CC two tryptophan synthase subunits, and represses initiation at its own
CC promoter. Acts by binding to two adjacent sites in the intergenic
CC region. In the absence of the inducer indoleglycerol phosphate (InGP),
CC TrpI binds to site I. In the presence of InGP, TrpI binds to site I and
CC site II. Binding to site II is site I dependent. InGP strongly
CC stimulates binding to site II and is required for maximal activation of
CC trpBA. {ECO:0000269|PubMed:1756720, ECO:0000269|PubMed:1900276,
CC ECO:0000269|PubMed:1904858, ECO:0000269|PubMed:2107533,
CC ECO:0000269|PubMed:9858743}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:1900276}.
CC -!- INDUCTION: Negatively autoregulated. {ECO:0000269|PubMed:1904858}.
CC -!- MISCELLANEOUS: The trpAB promoter and the trpI promoter overlap, so
CC that RNA polymerase cannot form open complexes with both promoters
CC simultaneously. {ECO:0000269|PubMed:1904858}.
CC -!- SIMILARITY: Belongs to the LysR transcriptional regulatory family.
CC {ECO:0000305}.
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DR EMBL; M21093; AAD15136.1; -; Genomic_DNA.
DR EMBL; X51868; CAA36157.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG03427.1; -; Genomic_DNA.
DR PIR; A32234; A30769.
DR PIR; A83641; A83641.
DR PIR; S12643; S12643.
DR RefSeq; NP_248727.1; NC_002516.2.
DR RefSeq; WP_003114633.1; NZ_QZGE01000012.1.
DR AlphaFoldDB; P11720; -.
DR SMR; P11720; -.
DR STRING; 287.DR97_2991; -.
DR PaxDb; P11720; -.
DR EnsemblBacteria; AAG03427; AAG03427; PA0037.
DR GeneID; 883090; -.
DR KEGG; pae:PA0037; -.
DR PATRIC; fig|208964.12.peg.37; -.
DR PseudoCAP; PA0037; -.
DR HOGENOM; CLU_039613_37_2_6; -.
DR InParanoid; P11720; -.
DR OMA; EPPWPAD; -.
DR PhylomeDB; P11720; -.
DR BioCyc; PAER208964:G1FZ6-38-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR CollecTF; EXPREG_00000910; -.
DR GO; GO:0032993; C:protein-DNA complex; IPI:CollecTF.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IPI:CollecTF.
DR GO; GO:2000284; P:positive regulation of cellular amino acid biosynthetic process; IMP:PseudoCAP.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:PseudoCAP.
DR GO; GO:0006351; P:transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd08482; PBP2_TrpI; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR005119; LysR_subst-bd.
DR InterPro; IPR037418; TrpI_PBP2.
DR InterPro; IPR000847; Tscrpt_reg_HTH_LysR.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00126; HTH_1; 1.
DR Pfam; PF03466; LysR_substrate; 1.
DR PRINTS; PR00039; HTHLYSR.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50931; HTH_LYSR; 1.
PE 1: Evidence at protein level;
KW Activator; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW DNA-binding; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Tryptophan biosynthesis.
FT CHAIN 1..295
FT /note="HTH-type transcriptional regulator TrpI"
FT /id="PRO_0000105763"
FT DOMAIN 6..63
FT /note="HTH lysR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
FT DNA_BIND 23..42
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
FT VARIANT 46
FT /note="D -> E (in strain: PAC174)"
FT VARIANT 55
FT /note="K -> R (in strain: PAC174)"
FT VARIANT 115
FT /note="Q -> R (in strain: PAC174)"
FT VARIANT 163
FT /note="P -> S (in strain: PAC174)"
FT VARIANT 170
FT /note="V -> L (in strain: PAC174)"
FT VARIANT 181
FT /note="A -> S (in strain: PAC174)"
FT VARIANT 206..207
FT /note="WA -> S (in strain: PAC174)"
FT CONFLICT 209
FT /note="S -> G (in Ref. 2; CAA36157)"
FT /evidence="ECO:0000305"
FT CONFLICT 254..258
FT /note="GRLAA -> APGG (in Ref. 1; AAD15136 and 2; CAA36157)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 295 AA; 32253 MW; E726ABA618C4069E CRC64;
MSRDLPSLNA LRAFEAAARL HSISLAAEEL HVTHGAVSRQ VRLLEDDLGV ALFGKDGRGV
KLTDSGVRLR DACGDAFERL RGVCAELRRQ TAEAPFVLGV PGSLLARWFI PRLDQLNRAL
PDLRLQLSTS EGEFDPRRPG LDAMLWFAEP PWPADMQVFE LAPERMGPVV SPRLAQETGL
AQAPAARLLQ EPLLHTASRP QAWPAWAASQ GLAAEALRYG QGFEHLYYLL EAAVAGLGVA
IAPEPLVRDD LAAGRLAAPW GFIETDARLA LWVPARLHDP RAGRLAQWLR EQLAG
