ID   FLGS_HELPY              Reviewed;         381 AA.
AC   O25026;
DT   11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Sensor histidine kinase FlgS;
DE            EC=2.7.13.3 {ECO:0000269|PubMed:10735847, ECO:0000269|PubMed:16035242};
GN   Name=flgS; OrderedLocusNames=HP_0244;
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, CATALYTIC ACTIVITY, AND AUTOPHOSPHORYLATION.
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, CATALYTIC ACTIVITY, AND AUTOPHOSPHORYLATION.
RC   STRAIN=G27;
RX   PubMed=16035242; DOI=10.1016/j.micres.2005.02.003;
RA   Jimenez-Pearson M.A., Dietz P., Beier D.;
RT   "Protein-protein interaction of HP137 with histidine kinase HP244 does not
RT   contribute to flagellar regulation in Helicobacter pylori.";
RL   Microbiol. Res. 160:299-305(2005).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=18978046; DOI=10.1128/jb.01219-08;
RA   Wen Y., Feng J., Scott D.R., Marcus E.A., Sachs G.;
RT   "The pH-responsive regulon of HP0244 (FlgS), the cytoplasmic histidine
RT   kinase of Helicobacter pylori.";
RL   J. Bacteriol. 191:449-460(2009).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH FLHA.
RC   STRAIN=ATCC 43504;
RX   PubMed=25802298; DOI=10.1128/jb.02610-14;
RA   Tsang J., Hirano T., Hoover T.R., McMurry J.L.;
RT   "Helicobacter pylori FlhA Binds the Sensor Kinase and Flagellar Gene
RT   Regulatory Protein FlgS with High Affinity.";
RL   J. Bacteriol. 197:1886-1892(2015).
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:9882675). Also plays an essential role
CC       in bacterial survival at pH 2.5 independently of FlgR
CC       (PubMed:18978046). Functions as a sensor protein kinase which is
CC       autophosphorylated at a histidine residue and transfers its phosphate
CC       group to the conserved aspartic acid residue in the regulatory domain
CC       of FlgR (PubMed:10735847, PubMed:16035242). In turn, FlgR functions as
CC       a transcriptional regulator initiating transcription from RpoN-
CC       dependent promoters (PubMed:10735847, PubMed:16035242).
CC       {ECO:0000269|PubMed:10735847, ECO:0000269|PubMed:16035242,
CC       ECO:0000269|PubMed:18978046, ECO:0000269|PubMed:9882675}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000269|PubMed:10735847,
CC         ECO:0000269|PubMed:16035242};
CC   -!- SUBUNIT: Interacts (via its C-terminal kinase domain) with FlhA (via N-
CC       terminus). {ECO:0000269|PubMed:25802298}.
CC   -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:10735847,
CC       ECO:0000269|PubMed:16035242}.
CC   -!- DISRUPTION PHENOTYPE: Shows a pronounced survival defect at pH 2.5 not
CC       due to the nonmotile phenotype. {ECO:0000269|PubMed:18978046}.
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DR   EMBL; AE000511; AAD07313.1; -; Genomic_DNA.
DR   PIR; D64550; D64550.
DR   RefSeq; NP_207042.1; NC_000915.1.
DR   RefSeq; WP_000748581.1; NC_018939.1.
DR   AlphaFoldDB; O25026; -.
DR   SMR; O25026; -.
DR   DIP; DIP-3202N; -.
DR   IntAct; O25026; 5.
DR   MINT; O25026; -.
DR   STRING; 85962.C694_01235; -.
DR   PaxDb; O25026; -.
DR   EnsemblBacteria; AAD07313; AAD07313; HP_0244.
DR   KEGG; hpy:HP_0244; -.
DR   PATRIC; fig|85962.47.peg.264; -.
DR   eggNOG; COG0642; Bacteria.
DR   OMA; AIWVMNE; -.
DR   PhylomeDB; O25026; -.
DR   BRENDA; 2.7.13.3; 2604.
DR   Proteomes; UP000000429; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Transferase; Two-component regulatory system.
FT   CHAIN           1..381
FT                   /note="Sensor histidine kinase FlgS"
FT                   /id="PRO_0000448703"
FT   DOMAIN          177..381
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         180
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   381 AA;  43656 MW;  E5C3609D515007C2 CRC64;
     MKKSKHLKRP YLKRSHLKHS DKASSFKGLL KKEDNVISLE NFKPKESEDL LENFSNKKDM
     QELLGLLNQF ILQSYKVEKE FKDYKALYEW VIEILPQAIW VVNENGSFFY KNSLANQSHE
     VFNKAKLENF NTEIEHENKS YLVQQNSIQG KQIITATDIS AQKRQERLAS MGKISAHLAH
     EIRNPVGSIS LLASVLLKHA NEKTKPIVVE LQKALWRVER IIKATLLFSK GIQANRTKQS
     LKTLESDLKE ALNCYTYSKD IDFLFNFSDE EGFFDFDLMG IVLQNFLYNA IDAIEALEES
     EQGQVKIEAF IQNEFIVFTI IDNGKEVENK SALFEPFETT KLKGNGLGLA LSLQVVKAHE
     GSIALLENQE KTFEIKILNA S