PTXS_PSEPK
ID PTXS_PSEPK Reviewed; 339 AA.
AC Q88HH7;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=HTH-type transcriptional regulator PtxS {ECO:0000305};
GN Name=ptxS {ECO:0000303|PubMed:20581202};
GN OrderedLocusNames=PP_3380 {ECO:0000312|EMBL:AAN68984.1};
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
RN [2]
RP FUNCTION, DNA-BINDING, ACTIVITY REGULATION, SUBUNIT, TRANSCRIPTIONAL
RP REGULATION, AND DOMAIN.
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=20581202; DOI=10.1128/jb.00520-10;
RA Daddaoua A., Krell T., Alfonso C., Morel B., Ramos J.L.;
RT "Compartmentalized glucose metabolism in Pseudomonas putida is controlled
RT by the PtxS repressor.";
RL J. Bacteriol. 192:4357-4366(2010).
RN [3]
RP CRYSTALLIZATION.
RX PubMed=23143237; DOI=10.1107/s1744309112028540;
RA Pineda-Molina E., Daddaoua A., Krell T., Ramos J.L., Garcia-Ruiz J.M.,
RA Gavira J.A.;
RT "In situ X-ray data collection from highly sensitive crystals of
RT Pseudomonas putida PtxS in complex with DNA.";
RL Acta Crystallogr. F 68:1307-1310(2012).
CC -!- FUNCTION: Negatively regulates glucose metabolism by binding directly
CC to the promoter region of the kgu and gad operons (PubMed:20581202). It
CC also negatively regulates its own synthesis (PubMed:20581202).
CC {ECO:0000269|PubMed:20581202}.
CC -!- ACTIVITY REGULATION: 2-ketogluconate acts as a molecular effector and
CC causes dissociation of PtxS from its target promoter.
CC {ECO:0000269|PubMed:20581202}.
CC -!- SUBUNIT: Homodimer in solution. {ECO:0000269|PubMed:20581202}.
CC -!- INTERACTION:
CC Q88HH7; Q88HH7: ptxS; NbExp=2; IntAct=EBI-6411771, EBI-6411771;
CC -!- INDUCTION: Negatively autoregulates its own synthesis by binding to a
CC specific operator site within the ptxS upstream region.
CC {ECO:0000269|PubMed:20581202}.
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:20581202}.
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DR EMBL; AE015451; AAN68984.1; -; Genomic_DNA.
DR RefSeq; NP_745520.1; NC_002947.4.
DR RefSeq; WP_010954253.1; NC_002947.4.
DR STRING; 160488.PP_3380; -.
DR EnsemblBacteria; AAN68984; AAN68984; PP_3380.
DR KEGG; ppu:PP_3380; -.
DR PATRIC; fig|160488.4.peg.3593; -.
DR eggNOG; COG1609; Bacteria.
DR HOGENOM; CLU_037628_6_0_6; -.
DR OMA; MHGVETA; -.
DR PhylomeDB; Q88HH7; -.
DR BioCyc; PPUT160488:G1G01-3611-MON; -.
DR Proteomes; UP000000556; Chromosome.
DR CollecTF; EXPREG_000011c0; -.
DR GO; GO:0032993; C:protein-DNA complex; IPI:CollecTF.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IPI:CollecTF.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:CollecTF.
DR CDD; cd01392; HTH_LacI; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR InterPro; IPR000843; HTH_LacI.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR001761; Peripla_BP/Lac1_sug-bd_dom.
DR InterPro; IPR028082; Peripla_BP_I.
DR Pfam; PF00356; LacI; 1.
DR Pfam; PF00532; Peripla_BP_1; 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..339
FT /note="HTH-type transcriptional regulator PtxS"
FT /id="PRO_0000456056"
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 339 AA; 36789 MW; 32AD9BA84D584F5F CRC64;
MTDAPAHTRE RVTISEVARV AGVSKATVSR YIGGDRQLLA EATAKRLEEV IERLGYRPNQ
MARGLKRGQT RLIGMLVADI LNPYSVAVMH GVETACRQHG YSLVVCNTNR DDEQERHHLV
ALQSYNVEGL IVNTLGHHPG ELLNLQRDIP MVLVDRQLPE LNVDLVGLDN ADAVEQALDH
LQAQGYRDIL AVSEPLDGTS SRLERVQAFG ASISRRPGMR QQVLEIGAGL QGQLASFLAH
SGHGPQAIFT FNGVATLAVT RALLEAGRNL VADVGLIALD DLDWYPLVGK GITALAQPTE
RIGVAAFESL LGRLRGDSGA ARRIDFKANL IIRGSTQPQ
