ARSS_HELPY
ID ARSS_HELPY Reviewed; 427 AA.
AC O24972; O24971;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 11-DEC-2019, sequence version 2.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Sensor histidine kinase ArsS {ECO:0000303|PubMed:16672598};
DE EC=2.7.13.3 {ECO:0000269|PubMed:10735847};
GN Name=arsS {ECO:0000303|PubMed:16672598}; OrderedLocusNames=HP_0164/HP_0165;
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, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, AND SEQUENCE REVISION.
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 [3]
RP FUNCTION.
RC STRAIN=G27;
RX PubMed=15109719; DOI=10.1111/j.1574-6968.2004.tb09512.x;
RA Pflock M., Dietz P., Schaer J., Beier D.;
RT "Genetic evidence for histidine kinase HP165 being an acid sensor of
RT Helicobacter pylori.";
RL FEMS Microbiol. Lett. 234:51-61(2004).
RN [4]
RP FUNCTION.
RX PubMed=16672598; DOI=10.1128/jb.188.10.3449-3462.2006;
RA Pflock M., Finsterer N., Joseph B., Mollenkopf H., Meyer T.F., Beier D.;
RT "Characterization of the ArsRS regulon of Helicobacter pylori, involved in
RT acid adaptation.";
RL J. Bacteriol. 188:3449-3462(2006).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22865848; DOI=10.1128/jb.01263-12;
RA Marcus E.A., Sachs G., Wen Y., Feng J., Scott D.R.;
RT "Role of the Helicobacter pylori sensor kinase ArsS in protein trafficking
RT and acid acclimation.";
RL J. Bacteriol. 194:5545-5551(2012).
RN [6]
RP FUNCTION.
RX PubMed=25997502; DOI=10.1111/hel.12235;
RA Marcus E.A., Sachs G., Wen Y., Scott D.R.;
RT "Phosphorylation-dependent and Phosphorylation-independent Regulation of
RT Helicobacter pylori Acid Acclimation by the ArsRS Two-component System.";
RL Helicobacter 21:69-81(2016).
RN [7]
RP FUNCTION IN BIOFILM FORMATION, AND DISRUPTION PHENOTYPE.
RX PubMed=27432830; DOI=10.1128/jb.00324-16;
RA Servetas S.L., Carpenter B.M., Haley K.P., Gilbreath J.J., Gaddy J.A.,
RA Merrell D.S.;
RT "Characterization of Key Helicobacter pylori Regulators Identifies a Role
RT for ArsRS in Biofilm Formation.";
RL J. Bacteriol. 198:2536-2548(2016).
CC -!- FUNCTION: Member of the two-component regulatory system ArsS/ArsR that
CC regulates genes involved in biofilm formation and acid adaptation by
CC acting on major ammonia-producing pathways (PubMed:16672598,
CC PubMed:22865848, PubMed:27432830). Functions as a sensor protein kinase
CC which is autophosphorylated at a histidine residue and transfers its
CC phosphate group to the conserved aspartic acid residue in the
CC regulatory domain of ArsR (PubMed:10735847). In turn, ArsR binds to the
CC upstream promoter regions of target genes including ureA, amiE and amiF
CC to positively regulate their expression in response to acidic pH
CC (PubMed:15109719, PubMed:16672598). Participates also in acidic
CC acclimatation in a phosphorylation-independent pathway by regulating
CC acid-induced trafficking of urease and its accessory proteins to the
CC inner membrane (PubMed:25997502). {ECO:0000269|PubMed:10735847,
CC ECO:0000269|PubMed:15109719, ECO:0000269|PubMed:16672598,
CC ECO:0000269|PubMed:22865848, ECO:0000269|PubMed:25997502,
CC ECO:0000269|PubMed:27432830}.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:10735847}.
CC -!- DISRUPTION PHENOTYPE: Deletion leads to a decreased urease activity to
CC one-third of the level of the wild type (PubMed:22865848). Displays
CC also an exacerbated stress response that results in enhanced and
CC accelerated biofilm formation (PubMed:27432830).
CC {ECO:0000269|PubMed:22865848, ECO:0000269|PubMed:27432830}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD07233.1; Type=Frameshift; Note=The gene was originally annotated as two separate ORFs HP_0165 (AC O24972) and HP_0164 (AC O24971) probably due to a sequencing error.; Evidence={ECO:0000305|PubMed:10735847};
CC Sequence=AAD07239.1; Type=Frameshift; Evidence={ECO:0000305|PubMed:10735847};
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DR EMBL; AE000511; AAD07239.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AE000511; AAD07233.1; ALT_FRAME; Genomic_DNA.
DR PIR; D64540; D64540.
DR PIR; E64540; E64540.
DR AlphaFoldDB; O24972; -.
DR SMR; O24972; -.
DR IntAct; O24972; 5.
DR STRING; 85962.C694_00815; -.
DR PaxDb; O24972; -.
DR EnsemblBacteria; AAD07233; AAD07233; HP_0164.
DR EnsemblBacteria; AAD07239; AAD07239; HP_0165.
DR KEGG; hpy:HP_0164; -.
DR KEGG; hpy:HP_0165; -.
DR PATRIC; fig|85962.47.peg.177; -.
DR eggNOG; COG0642; Bacteria.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; 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; IPR003660; HAMP_dom.
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 SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 1: Evidence at protein level;
KW Kinase; Membrane; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..427
FT /note="Sensor histidine kinase ArsS"
FT /id="PRO_0000448746"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 151..203
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 211..398
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 214
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 427 AA; 49917 MW; 05DF300AFCE8C699 CRC64;
MRFSIFFKVV ALFMITLFSF GAFAYYFVSS QISHENYQNE MRHYQFVTTI NEILNNYSDY
RAIEDYLYKI GFRETTIENL EKVLAKRRHQ LHHRNIGYAE VFKFSDMVFI LLKKDEHFVL
YKDLHSVSYR NYFLAITVGL LLILFLFLFV LQSLLPLREL RSQVKPFAQG DKSVSCKSKQ
KDEIGDLANE FDNCILKINA MNESRVLFLR SIMHELRTPI TKGKILSSML KEELSCKRFS
SIFDHLNMLI EQFARIEQLA SKNYGSNKEK FLMSDLIDKI EKMLLIDEDK ESPIHVSSSN
YIIEADFELF SIALKNMVDN AIKYSDDKQV FLDFIGNNLV VSNKSKPLKE DFEKYLQPYF
KSSNPSQAHG FGLGMYIIKN ALEAMGLNLS YHYSNGRICF TIHDCVFNSF YDLEEDNEEL
PPPPPKI
