ID   CHEV3_HELPY             Reviewed;         311 AA.
AC   O25154;
DT   11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 126.
DE   RecName: Full=Chemotaxis protein CheV3 {ECO:0000303|PubMed:11535789};
GN   Name=cheV3 {ECO:0000303|PubMed:11535789}; OrderedLocusNames=HP_0393;
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 DISRUPTION PHENOTYPE.
RX   PubMed=11535789; DOI=10.1099/00221287-147-9-2493;
RA   Pittman M.S., Goodwin M., Kelly D.J.;
RT   "Chemotaxis in the human gastric pathogen Helicobacter pylori: different
RT   roles for CheW and the three CheV paralogues, and evidence for CheV2
RT   phosphorylation.";
RL   Microbiology 147:2493-2504(2001).
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19332820; DOI=10.1099/mic.0.021857-0;
RA   Lowenthal A.C., Simon C., Fair A.S., Mehmood K., Terry K., Anastasia S.,
RA   Ottemann K.M.;
RT   "A fixed-time diffusion analysis method determines that the three cheV
RT   genes of Helicobacter pylori differentially affect motility.";
RL   Microbiology 155:1181-1191(2009).
CC   -!- FUNCTION: Plays a role in chemotaxis signal transduction system in
CC       order to colonize the host stomach. May act as a phosphate sink to
CC       control the flow of phosphate to CheAY. {ECO:0000269|PubMed:11535789,
CC       ECO:0000269|PubMed:19332820}.
CC   -!- DISRUPTION PHENOTYPE: Deletion mutant is fully chemotactic and forms
CC       swarms the same way as wild-type strain (PubMed:11535789). Mutant
CC       appears however to change direction frequently and shows defects in
CC       mouse colonization (PubMed:19332820). {ECO:0000269|PubMed:11535789,
CC       ECO:0000269|PubMed:19332820}.
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DR   EMBL; AE000511; AAD07458.1; -; Genomic_DNA.
DR   PIR; A64569; A64569.
DR   RefSeq; NP_207191.1; NC_000915.1.
DR   RefSeq; WP_000818647.1; NC_018939.1.
DR   AlphaFoldDB; O25154; -.
DR   SMR; O25154; -.
DR   IntAct; O25154; 5.
DR   STRING; 85962.C694_01995; -.
DR   PaxDb; O25154; -.
DR   EnsemblBacteria; AAD07458; AAD07458; HP_0393.
DR   KEGG; hpy:HP_0393; -.
DR   PATRIC; fig|85962.47.peg.417; -.
DR   eggNOG; COG0784; Bacteria.
DR   eggNOG; COG0835; Bacteria.
DR   OMA; RLEWNQV; -.
DR   PhylomeDB; O25154; -.
DR   Proteomes; UP000000429; Chromosome.
DR   GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR   InterPro; IPR024181; Chemotax_regulator_CheV.
DR   InterPro; IPR036061; CheW-like_dom_sf.
DR   InterPro; IPR002545; CheW-lke_dom.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   Pfam; PF01584; CheW; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PIRSF; PIRSF002867; CheV; 1.
DR   SMART; SM00260; CheW; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF50341; SSF50341; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   PROSITE; PS50851; CHEW; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   3: Inferred from homology;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..311
FT                   /note="Chemotaxis protein CheV3"
FT                   /id="PRO_0000448751"
FT   DOMAIN          13..164
FT                   /note="CheW-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00052"
FT   DOMAIN          182..308
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   MOD_RES         241
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   311 AA;  35630 MW;  223A196E088FD718 CRC64;
     MAEKTANDLK LSEIELVDFR IYGMQEGVPY EGIYGINVAK VQEIIPMPTL FEYPTNLDYI
     IGVFDLRSII IPLIDLAKWI GIIPDKSKEN EKIVIITEFN NVKMGFLVHS ARRIRRISWK
     DVEPASFSAS NSINKENITG TTRIENDKTL LILDLESILD DLKLNEDAKN AKDTHKERFE
     GEVLFLDDSK TARKTLKNHL SKLGFSITEA VDGEDGLNKL EMLFKKYGDD LRKHLKFIIS
     DVEMPKMDGY HFLFKLQKDP RFAYIPVIFN SSICDNYSAE RAKEMGAVAY LVKFDAEKFT
     EEISKILDKN A