ID   PTXS_PSEDL              Reviewed;         340 AA.
AC   A0A167V873;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   03-AUG-2022, sequence version 2.
DT   03-AUG-2022, entry version 22.
DE   RecName: Full=HTH-type transcriptional regulator PtxS {ECO:0000305};
GN   Name=ptxS {ECO:0000312|EMBL:ANB66399.1};
OS   Pseudomonas plecoglossicida.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=70775;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=JUIM01;
RA   Sun W., Zhang X., Wang D., Cui F.;
RT   "Cloning and bioinformatics analysis of 2-ketogluconate metabolic
RT   regulatory protein PtxS gene from Pseudomonas plecoglossicida JUIM01.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, ACTIVITY REGULATION, SUBUNIT, DOMAIN, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=JUIM01;
RX   PubMed=33529626; DOI=10.1016/j.ijbiomac.2021.01.198;
RA   Sun L., Wang D., Sun W., Zhang X., Cui F., Su C., Zhang X., Xu G., Shi J.,
RA   Xu Z.;
RT   "Characterization of a transcriptional regulator PtxS from Pseudomonas
RT   plecoglossicida for regulating 2-ketogluconic acid metabolism.";
RL   Int. J. Biol. Macromol. 174:330-338(2021).
CC   -!- FUNCTION: Involved in the regulation of 2-ketogluconic acid metabolism
CC       via the control of the expression of the kgu operon (PubMed:33529626).
CC       Binds directly to a 14-bp palindrome sequence via its conserved HTH
CC       motif (PubMed:33529626). {ECO:0000269|PubMed:33529626}.
CC   -!- ACTIVITY REGULATION: 2-ketogluconate acts as a molecular effector and
CC       causes dissociation of PtxS from its target promoter (PubMed:33529626).
CC       Glucose negatively affects the molecular binding of PtxS and 2KGA, and
CC       gluconic acid inhibits the PtxS-2KGA binding reaction
CC       (PubMed:33529626). {ECO:0000269|PubMed:33529626}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:33529626}.
CC   -!- DOMAIN: Contains an N-terminal helix-turn-helix DNA-binding domain and
CC       a C-terminal domain that binds the effector.
CC       {ECO:0000269|PubMed:33529626}.
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DR   EMBL; KU168041; ANB66399.1; -; Genomic_DNA.
DR   SMR; A0A167V873; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd01392; HTH_LacI; 1.
DR   Gene3D; 1.10.260.40; -; 1.
DR   InterPro; IPR000843; HTH_LacI.
DR   InterPro; IPR001647; HTH_TetR.
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; Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..340
FT                   /note="HTH-type transcriptional regulator PtxS"
FT                   /id="PRO_0000456055"
FT   DOMAIN          12..67
FT                   /note="HTH lacI-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00111"
FT   DNA_BIND        14..33
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00111"
SQ   SEQUENCE   340 AA;  36684 MW;  F2F713215FDF5A5F CRC64;
     MDKTLSQART RVTISEVAQA AGVSKATVSR YIGGDRQLLA DATAQRIEAV IEQLGYRPNR
     MASALKRGRT RLIGMLLADI RNPYSVAVMH GVETACREHG YSLVVCNTDC DDARERQHLQ
     ALQAYNVDGL IVNTLGHHAG ELASLAQELP MVLVDRQLAE LQTDLVGLDN ADAVEQALDH
     LHACGYRDIL AVSEPLDGTS SRQERVAAFQ ASIARRSGLR GQVLEVSANL PGQLAAFLAS
     AGHGPQALFS CNGVATLEVM RHLHGRGEQL FQQLGLVALD DLDWYPLVGG GITALAQPTE
     RIAAAAVQCL LERLQGSQLP ARRLDLRAQL IVRGSTPIRN