ID   GNTR_PSEAE              Reviewed;         343 AA.
AC   Q9I1F6;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=HTH-type transcriptional regulator GntR {ECO:0000305};
GN   Name=gntR {ECO:0000303|PubMed:28752954};
GN   OrderedLocusNames=PA2320 {ECO:0000312|EMBL:AAG05708.1};
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 [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   [2]
RP   FUNCTION, DNA-BINDING, ACTIVITY REGULATION, AND INDUCTION.
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=28752954; DOI=10.1111/1462-2920.13871;
RA   Daddaoua A., Corral-Lugo A., Ramos J.L., Krell T.;
RT   "Identification of GntR as regulator of the glucose metabolism in
RT   Pseudomonas aeruginosa.";
RL   Environ. Microbiol. 19:3721-3733(2017).
CC   -!- FUNCTION: Involved in the regulation of glucose metabolism. Represses
CC       its own expression as well as that of the gluconate permease GntP
CC       (PubMed:28752954). It employs an effector mediated de-repression
CC       mechanism: in the absence of ligand, GntR binds to the gntR and gntP
CC       promoters and represses their expression. The release of promoter bound
CC       GntR is induced by gluconate and 6-phosphogluconate that bind with
CC       similar apparent affinities to the GntR/DNA complex. The release of
CC       GntR leads to transcription of the genes (PubMed:28752954).
CC       {ECO:0000269|PubMed:28752954}.
CC   -!- ACTIVITY REGULATION: Free GntR fails to recognize gluconate and 6-
CC       phosphogluconate, whereas the GntR/DNA complexes recognize both
CC       ligands. It is therefore likely that GntR DNA binding induces
CC       structural changes that permit GntR to recognize effectors.
CC       {ECO:0000269|PubMed:28752954}.
CC   -!- INDUCTION: Negatively autoregulated. {ECO:0000269|PubMed:28752954}.
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DR   EMBL; AE004091; AAG05708.1; -; Genomic_DNA.
DR   PIR; C83355; C83355.
DR   RefSeq; NP_251010.1; NC_002516.2.
DR   RefSeq; WP_003107131.1; NZ_QZGE01000021.1.
DR   AlphaFoldDB; Q9I1F6; -.
DR   SMR; Q9I1F6; -.
DR   STRING; 287.DR97_6113; -.
DR   PaxDb; Q9I1F6; -.
DR   PRIDE; Q9I1F6; -.
DR   EnsemblBacteria; AAG05708; AAG05708; PA2320.
DR   GeneID; 883124; -.
DR   KEGG; pae:PA2320; -.
DR   PATRIC; fig|208964.12.peg.2425; -.
DR   PseudoCAP; PA2320; -.
DR   HOGENOM; CLU_037628_6_3_6; -.
DR   InParanoid; Q9I1F6; -.
DR   OMA; MVFVDRW; -.
DR   PhylomeDB; Q9I1F6; -.
DR   BioCyc; PAER208964:G1FZ6-2359-MON; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:PseudoCAP.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR   GO; GO:0010906; P:regulation of glucose metabolic process; IMP:PseudoCAP.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   CDD; cd01392; HTH_LacI; 1.
DR   Gene3D; 1.10.260.40; -; 1.
DR   InterPro; IPR000843; HTH_LacI.
DR   InterPro; IPR046335; LacI/GalR-like_sensor.
DR   InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR   InterPro; IPR028082; Peripla_BP_I.
DR   Pfam; PF00356; LacI; 1.
DR   Pfam; PF13377; Peripla_BP_3; 1.
DR   SMART; SM00354; HTH_LACI; 1.
DR   SUPFAM; SSF47413; SSF47413; 1.
DR   SUPFAM; SSF53822; SSF53822; 1.
DR   PROSITE; PS00356; HTH_LACI_1; 1.
DR   PROSITE; PS50932; HTH_LACI_2; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..343
FT                   /note="HTH-type transcriptional regulator GntR"
FT                   /id="PRO_0000454758"
FT   DOMAIN          16..70
FT                   /note="HTH lacI-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00111"
FT   DNA_BIND        18..37
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00111"
SQ   SEQUENCE   343 AA;  37148 MW;  21CF556274330FBE CRC64;
     MSITKNDKNT RTTGRPTLNE VARRAGVSPI TASRALRGVA SVAEELAQKV RDAARELGYV
     ANPAARALAS AQSHSVAVLV PSLANLLFIE TLEAIHAVLR PQGLEVLIGN FHYSRNEEED
     LIRNYLAYQP RGLLLTGFER TESARRMIEA SGIPCVYMMD LDSGSGLNCV GFSQLRAGEA
     AAEHLLARGR RRLAYIGAQL DQRTLLRGEG FRRALQKAGC YDPGLEILTP RPSSVALGGE
     LFVQLLASQP QVDGVFFCND DLAQGALLEA LRRGVKVPEQ IAVLGFNDLP GSDCTVPRLS
     SIRTPREAIG RRAAEQLLAL IAGKEVRDSA LDMGFELMAR EST