ARSR_HELPY
ID ARSR_HELPY Reviewed; 225 AA.
AC O24973;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 142.
DE RecName: Full=Transcriptional regulatory protein ArsR {ECO:0000303|PubMed:22865848};
GN Name=arsR {ECO:0000303|PubMed:22865848}; OrderedLocusNames=HP_0166;
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, AND PHOSPHORYLATION.
RX PubMed=11751811; DOI=10.1128/jb.184.2.350-362.2002;
RA Dietz P., Gerlach G., Beier D.;
RT "Identification of target genes regulated by the two-component system
RT HP166-HP165 of Helicobacter pylori.";
RL J. Bacteriol. 184:350-362(2002).
RN [3]
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 [4]
RP FUNCTION.
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 [5]
RP FUNCTION, MUTAGENESIS OF ASP-52, AND PHOSPHORYLATION AT ASP-52.
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 [6]
RP FUNCTION IN BIOFILM FORMATION, AND MUTAGENESIS OF ASP-52.
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:22865848,
CC PubMed:25997502, PubMed:27432830). Upon phosphorylation by ArsS,
CC functions as a transcription regulator by direct binding to promoter
CC regions of target genes including ureA, amiE and amiF to positively
CC regulate their expression in response to acidic pH (PubMed:11751811,
CC PubMed:16672598). Negatively autoregulates its expression
CC (PubMed:11751811). {ECO:0000269|PubMed:11751811,
CC ECO:0000269|PubMed:16672598, ECO:0000269|PubMed:22865848,
CC ECO:0000269|PubMed:25997502, ECO:0000269|PubMed:27432830}.
CC -!- PTM: Phosphorylated on Asp-52 by ArsS. {ECO:0000269|PubMed:25997502}.
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DR EMBL; AE000511; AAD07234.1; -; Genomic_DNA.
DR PIR; F64540; F64540.
DR RefSeq; NP_206965.1; NC_000915.1.
DR RefSeq; WP_000573710.1; NC_018939.1.
DR AlphaFoldDB; O24973; -.
DR SMR; O24973; -.
DR IntAct; O24973; 3.
DR STRING; 85962.C694_00820; -.
DR PaxDb; O24973; -.
DR EnsemblBacteria; AAD07234; AAD07234; HP_0166.
DR GeneID; 66521416; -.
DR KEGG; hpy:HP_0166; -.
DR PATRIC; fig|85962.47.peg.179; -.
DR eggNOG; COG0745; Bacteria.
DR OMA; NYEFFGD; -.
DR PhylomeDB; O24973; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0032993; C:protein-DNA complex; IPI:CollecTF.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IPI:CollecTF.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IPI:CollecTF.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:CollecTF.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEP:CollecTF.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEP:CollecTF.
DR CDD; cd00383; trans_reg_C; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR001867; OmpR/PhoB-type_DNA-bd.
DR InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR039420; WalR-like.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR48111; PTHR48111; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00486; Trans_reg_C; 1.
DR SMART; SM00448; REC; 1.
DR SMART; SM00862; Trans_reg_C; 1.
DR SUPFAM; SSF46894; SSF46894; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR PROSITE; PS51755; OMPR_PHOB; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Two-component regulatory system.
FT CHAIN 1..225
FT /note="Transcriptional regulatory protein ArsR"
FT /id="PRO_0000448745"
FT DOMAIN 3..116
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DNA_BIND 123..225
FT /note="OmpR/PhoB-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01091"
FT MOD_RES 52
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169,
FT ECO:0000269|PubMed:25997502"
FT MUTAGEN 52
FT /note="D->N: Significant decrease in levels of UreA, UreI
FT and UreE expression in a pH independent manner. Significant
FT increase in biofilm formation."
FT /evidence="ECO:0000269|PubMed:25997502,
FT ECO:0000269|PubMed:27432830"
SQ SEQUENCE 225 AA; 25856 MW; B4845F9A662CB682 CRC64;
MIEVLMIEDD IELAEFLSEF LLQHGIHVTN YDEPYTGISA ANTQNYDLLL LDLTLPNLDG
LEVCRRISKQ KHIPIIISSA RSDVEDKIKA LDYGADDYLP KPYDPKELLA RIQSLLRRSH
KKEEVSEPGD ANIFRVDKDS REVYMHEKKL DLTRAEYEIL SLLISKKGYV FSRESIAIES
ESINPESSNK SIDVIIGRLR SKIEKNPKQP QYIISVRGIG YKLEY
