GBDR_PSEAE
ID GBDR_PSEAE Reviewed; 367 AA.
AC Q9HTI4;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
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=PA5380 {ECO:0000312|EMBL:AAG08765.1};
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, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
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, DNA BINDING, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
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=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
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).
RN [5]
RP INDUCTION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=28791946; DOI=10.1099/mic.0.000502;
RA Sanchez D.G., Primo E.D., Damiani M.T., Lisa A.T.;
RT "Pseudomonas aeruginosa gbdR gene is transcribed from a sigma54-dependent
RT promoter under the control of NtrC/CbrB, IHF and BetI.";
RL Microbiology 163:1343-1354(2017).
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:19103776, PubMed:24097953). May play an important role during
CC P.aeruginosa interactions with eukaryotes (PubMed:17951379). Is
CC critical for induction of plcH and pchP in response to bovine
CC surfactant and mouse bronchoalveolar lavage fluid (BALF)
CC (PubMed:19103776). {ECO:0000269|PubMed:17951379,
CC ECO:0000269|PubMed:19103776, ECO:0000269|PubMed:24097953}.
CC -!- INDUCTION: The highest level of transcriptional activity is reached in
CC the presence of choline. Regulated at the transcriptional level by a
CC sigma-54-dependent promoter. Transcription can be activated by NtrC in
CC the absence of a preferential nitrogen source, by CbrB in the absence
CC of a preferential carbon source, and by the integration host factor
CC (IHF), by favouring DNA bending. Negatively regulated by BetI in the
CC absence of choline. {ECO:0000269|PubMed:28791946}.
CC -!- DISRUPTION PHENOTYPE: Mutant is unable to grow on choline, GB and DMG
CC as sole carbon or nitrogen sources (PubMed:17951379). Mutants that lack
CC this gene are unable to induce plcH and pchP in media containing GB or
CC choline and in phosphatidylcholine-rich environments, such as lung
CC surfactant or mouse lung lavage fluid (PubMed:19103776).
CC {ECO:0000269|PubMed:17951379, ECO:0000269|PubMed:19103776}.
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DR EMBL; AE004091; AAG08765.1; -; Genomic_DNA.
DR PIR; E82974; E82974.
DR RefSeq; NP_254067.1; NC_002516.2.
DR RefSeq; WP_003096699.1; NZ_QZGE01000031.1.
DR AlphaFoldDB; Q9HTI4; -.
DR SMR; Q9HTI4; -.
DR STRING; 287.DR97_2756; -.
DR PaxDb; Q9HTI4; -.
DR DNASU; 881137; -.
DR EnsemblBacteria; AAG08765; AAG08765; PA5380.
DR GeneID; 881137; -.
DR KEGG; pae:PA5380; -.
DR PATRIC; fig|208964.12.peg.5639; -.
DR PseudoCAP; PA5380; -.
DR HOGENOM; CLU_000445_59_0_6; -.
DR InParanoid; Q9HTI4; -.
DR OMA; CAGWHVR; -.
DR PhylomeDB; Q9HTI4; -.
DR BioCyc; PAER208964:G1FZ6-5507-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0032993; C:protein-DNA complex; IMP:CollecTF.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IMP:CollecTF.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IMP:CollecTF.
DR GO; GO:0031457; P:glycine betaine catabolic process; IMP:PseudoCAP.
DR GO; GO:0009896; P:positive regulation of catabolic process; IMP:PseudoCAP.
DR GO; GO:0045764; P:positive regulation of cellular amino acid metabolic process; IMP:PseudoCAP.
DR GO; GO:0010922; P:positive regulation of phosphatase activity; IMP:PseudoCAP.
DR GO; GO:0010518; P:positive regulation of phospholipase activity; IMP:PseudoCAP.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEP:CollecTF.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:PseudoCAP.
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; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..367
FT /note="HTH-type transcriptional regulator GbdR"
FT /id="PRO_0000453827"
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
