FLGR_HELPY
ID FLGR_HELPY Reviewed; 381 AA.
AC O25408;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Transcriptional regulatory protein FlgR;
GN Name=flgR; OrderedLocusNames=HP_0703;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2]
RP FUNCTION.
RX PubMed=9882675; DOI=10.1128/jb.181.2.593-599.1999;
RA Spohn G., Scarlato V.;
RT "Motility of Helicobacter pylori is coordinately regulated by the
RT transcriptional activator FlgR, an NtrC homolog.";
RL J. Bacteriol. 181:593-599(1999).
RN [3]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=10735847; DOI=10.1128/jb.182.8.2068-2076.2000;
RA Beier D., Frank R.;
RT "Molecular characterization of two-component systems of Helicobacter
RT pylori.";
RL J. Bacteriol. 182:2068-2076(2000).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15231786; DOI=10.1128/jb.186.14.4535-4542.2004;
RA Brahmachary P., Dashti M.G., Olson J.W., Hoover T.R.;
RT "Helicobacter pylori FlgR is an enhancer-independent activator of sigma54-
RT RNA polymerase holoenzyme.";
RL J. Bacteriol. 186:4535-4542(2004).
CC -!- FUNCTION: Member of the two-component regulatory system FlgR/FlgS that
CC induces the transcriptional induction of the genes needed in motility
CC and flagellar biogenesis (PubMed:15231786, PubMed:9882675). Upon
CC phosphorylation by FlgS, functions as a transcriptional regulator and
CC activates transcription of RpoN-dependent flagellar genes
CC (PubMed:10735847, PubMed:15231786). {ECO:0000269|PubMed:10735847,
CC ECO:0000269|PubMed:15231786, ECO:0000269|PubMed:9882675}.
CC -!- PTM: Phosphorylated by FlgS. {ECO:0000269|PubMed:10735847}.
CC -!- DISRUPTION PHENOTYPE: Disruption leads to loss of motility due to the
CC failure of the mutant strain to express the RpoN-dependent flagellar
CC genes. {ECO:0000269|PubMed:15231786}.
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DR EMBL; AE000511; AAD07754.1; -; Genomic_DNA.
DR PIR; G64607; G64607.
DR RefSeq; NP_207497.1; NC_000915.1.
DR RefSeq; WP_000684509.1; NC_018939.1.
DR AlphaFoldDB; O25408; -.
DR SMR; O25408; -.
DR DIP; DIP-3569N; -.
DR IntAct; O25408; 2.
DR MINT; O25408; -.
DR STRING; 85962.C694_03625; -.
DR PaxDb; O25408; -.
DR EnsemblBacteria; AAD07754; AAD07754; HP_0703.
DR KEGG; hpy:HP_0703; -.
DR PATRIC; fig|85962.47.peg.752; -.
DR eggNOG; COG2204; Bacteria.
DR OMA; MPISMQV; -.
DR PhylomeDB; O25408; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR002078; Sigma_54_int.
DR InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR InterPro; IPR025943; Sigma_54_int_dom_ATP-bd_2.
DR InterPro; IPR029995; TR_FlbD/FleR/FlgR.
DR PANTHER; PTHR32071:SF21; PTHR32071:SF21; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00158; Sigma54_activat; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
DR PROSITE; PS00675; SIGMA54_INTERACT_1; 1.
DR PROSITE; PS00676; SIGMA54_INTERACT_2; 1.
DR PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE 1: Evidence at protein level;
KW ATP-binding; DNA-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Two-component regulatory system.
FT CHAIN 1..381
FT /note="Transcriptional regulatory protein FlgR"
FT /id="PRO_0000448706"
FT DOMAIN 2..113
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 136..365
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT BINDING 164..171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT BINDING 227..236
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT MOD_RES 51
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 381 AA; 43414 MW; 293D713778E538D8 CRC64;
MKIAIVEDDI NMRKSLELFF ELQDDLEIVS FKNPKDALAK LDESFDLVIT DINMPHMDGL
EFLRLLEGKY ESIVITGNAT LNKAIDSIRL GVKDFFQKPF KPELLLESIY RTKKVLEFQK
KHPLEKPLKK PHKHSFLAAS KALEESKRQA LKVASTDANV MLLGESGVGK EVFAHFIHQH
SQRSKHPFIA INMSAIPEHL LESELFGYQK GAFTDATAPK MGLFESANKG TIFLDEIAEM
PLQLQSKLLR VVQEKEITRL GDNKSVKIDV RFISATNANM KEKIAAKEFR EDLFFRLQIV
PITIAPLRER VEEILPIAEI KLKEVCDAYH LGPKSFSKNA AKCLLEYSWH GNVRELLGVV
ERAAILSEET EIQEKDLFLE R
