GBDR_PSEAB
ID GBDR_PSEAB Reviewed; 367 AA.
AC A0A0H2ZIC3;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=HTH-type transcriptional regulator GbdR {ECO:0000305};
DE AltName: Full=Glycine betaine/dimethylglycine responsive regulator {ECO:0000303|PubMed:17951379};
GN Name=gbdR {ECO:0000303|PubMed:17951379};
GN OrderedLocusNames=PA14_71070 {ECO:0000312|EMBL:ABJ14763.1};
OS Pseudomonas aeruginosa (strain UCBPP-PA14).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCBPP-PA14;
RX PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT combinatorial.";
RL Genome Biol. 7:R90.1-R90.14(2006).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=UCBPP-PA14;
RX PubMed=17951379; DOI=10.1128/jb.01393-07;
RA Wargo M.J., Szwergold B.S., Hogan D.A.;
RT "Identification of two gene clusters and a transcriptional regulator
RT required for Pseudomonas aeruginosa glycine betaine catabolism.";
RL J. Bacteriol. 190:2690-2699(2008).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=UCBPP-PA14;
RX PubMed=19103776; DOI=10.1128/iai.01008-08;
RA Wargo M.J., Ho T.C., Gross M.J., Whittaker L.A., Hogan D.A.;
RT "GbdR regulates Pseudomonas aeruginosa plcH and pchP transcription in
RT response to choline catabolites.";
RL Infect. Immun. 77:1103-1111(2009).
RN [4]
RP FUNCTION, AND DNA-BINDING.
RC STRAIN=UCBPP-PA14;
RX PubMed=24097953; DOI=10.1128/jb.01055-13;
RA Hampel K.J., LaBauve A.E., Meadows J.A., Fitzsimmons L.F., Nock A.M.,
RA Wargo M.J.;
RT "Characterization of the GbdR regulon in Pseudomonas aeruginosa.";
RL J. Bacteriol. 196:7-15(2014).
CC -!- FUNCTION: Specific regulator of choline metabolism, which activates
CC transcription of at least 25 genes from 11 promoters in response to
CC choline metabolites (PubMed:24097953). Required for the induction of
CC plcH, encoding the phospholipase C, and pchP, encoding the
CC phosphorylcholine phosphatase, in response to glycine betaine (GB) and
CC dimethylglycine (DMG) (PubMed:19103776). Also controls the expression
CC of gbcAB and dgcAB, which are required for GB and DMG degradation,
CC respectively, in response to both GB and DMG (PubMed:17951379). The
CC GbdR regulon also includes genes encoding sarcosine, glycine and serine
CC catabolic enzymes, the BetX and CbcXWV quaternary amine transport
CC proteins and the acetylcholine esterase gene, choE (PubMed:24097953).
CC Acts by binding directly to the promoter region of the genes
CC (PubMed:24097953). May play an important role during P.aeruginosa
CC interactions with eukaryotes (PubMed:17951379).
CC {ECO:0000269|PubMed:17951379, ECO:0000269|PubMed:19103776,
CC ECO:0000269|PubMed:24097953}.
CC -!- DISRUPTION PHENOTYPE: Mutant is unable to grow on choline, GB and DMG
CC as sole carbon or nitrogen sources (PubMed:17951379). Deletion mutant
CC cannot induce expression of plcH (PubMed:19103776).
CC {ECO:0000269|PubMed:17951379, ECO:0000269|PubMed:19103776}.
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DR EMBL; CP000438; ABJ14763.1; -; Genomic_DNA.
DR RefSeq; WP_003096699.1; NZ_CP034244.1.
DR SMR; A0A0H2ZIC3; -.
DR EnsemblBacteria; ABJ14763; ABJ14763; PA14_71070.
DR KEGG; pau:PA14_71070; -.
DR HOGENOM; CLU_000445_59_0_6; -.
DR OMA; CAGWHVR; -.
DR BioCyc; PAER208963:G1G74-5980-MON; -.
DR Proteomes; UP000000653; Chromosome.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0009893; P:positive regulation of metabolic process; IEA:UniProt.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR002818; DJ-1/PfpI.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR018060; HTH_AraC.
DR InterPro; IPR018062; HTH_AraC-typ_CS.
DR Pfam; PF01965; DJ-1_PfpI; 1.
DR Pfam; PF12833; HTH_18; 1.
DR SMART; SM00342; HTH_ARAC; 1.
DR SUPFAM; SSF46689; SSF46689; 2.
DR SUPFAM; SSF52317; SSF52317; 1.
DR PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1.
DR PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Transcription; Transcription regulation.
FT CHAIN 1..367
FT /note="HTH-type transcriptional regulator GbdR"
FT /id="PRO_0000453826"
FT DOMAIN 227..325
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00593"
FT DNA_BIND 244..265
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00593"
FT DNA_BIND 292..315
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00593"
SQ SEQUENCE 367 AA; 41000 MW; EA82FAAE34D45D4D CRC64;
MTTYAPGVPP QNRNPQSIGF LLLDNFTLIS LASAVEPLRM ANQLSGRELY RWHTLSLDGR
QVWASDGLQI TPDAGTDNAP AVDCVIVCGG VGIQRSVTRE HVTFLQAQAR QGRRLGAVCT
GSWALARAGL LDGYDCSVHW ECLAAMQEAF PRVAMSTRLF SIDRNRFTSS GGTAPMDMML
HLIGREHGRE LSAAISEMFI YERIRNEQDH QRVPLKHMLG TNQPKLQEIV ALMEANLEEP
IDLDELAVYV NVSRRQLERL FQKYLHCSPS RYYLKLRLIR ARQLLKQTSM SIIEVASVCG
FVSTPHFSKC YREYFGIPPR DERQGQPLGQ PVVLMPIPQD LALMPNSSAL SALSQAQGES
TFASVRI
