ID   CHEV1_HELPY             Reviewed;         321 AA.
AC   O24864;
DT   11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 131.
DE   RecName: Full=Chemotaxis protein CheV1 {ECO:0000303|PubMed:11535789};
GN   Name=cheV1 {ECO:0000303|PubMed:11535789}; OrderedLocusNames=HP_0019;
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 an essential role in chemotaxis signal transduction
CC       system in order to colonize the host stomach. May act as a phosphate
CC       sink to control the flow of phosphate to CheAY.
CC       {ECO:0000269|PubMed:11535789, ECO:0000269|PubMed:19332820}.
CC   -!- DISRUPTION PHENOTYPE: Deletion shows a severe inhibitory effect on
CC       chemotaxis, although swarming is not completely abolished
CC       (PubMed:11535789). Mutant shows also defects in mouse colonization
CC       (PubMed:19332820). {ECO:0000269|PubMed:11535789,
CC       ECO:0000269|PubMed:19332820}.
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DR   EMBL; AE000511; AAD07087.1; -; Genomic_DNA.
DR   PIR; C64522; C64522.
DR   RefSeq; NP_206821.1; NC_000915.1.
DR   RefSeq; WP_000785454.1; NC_018939.1.
DR   AlphaFoldDB; O24864; -.
DR   DIP; DIP-3650N; -.
DR   IntAct; O24864; 3.
DR   MINT; O24864; -.
DR   STRING; 85962.C694_00090; -.
DR   PaxDb; O24864; -.
DR   EnsemblBacteria; AAD07087; AAD07087; HP_0019.
DR   KEGG; hpy:HP_0019; -.
DR   PATRIC; fig|85962.47.peg.18; -.
DR   eggNOG; COG0784; Bacteria.
DR   eggNOG; COG0835; Bacteria.
DR   OMA; IMICEFS; -.
DR   PhylomeDB; O24864; -.
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..321
FT                   /note="Chemotaxis protein CheV1"
FT                   /id="PRO_0000448749"
FT   DOMAIN          19..177
FT                   /note="CheW-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00052"
FT   DOMAIN          198..319
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   MOD_RES         252
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   321 AA;  36587 MW;  A0070CE9DF623953 CRC64;
     MADSLAGIDQ VTSLHKNNEL QLLCFRLGKN KDLYAVNVFK IREVVKYHGN LTIISHENNS
     LVEGLIIIRE LTIPLIDMKK WFYYDSQNKN KDLRPYRIEK EKGEDDIVMI CEFSRWTIGV
     RIYEADRILS KKWTEMEQSA GLGGSAGNNK LVSRTRYFDG RLVQVVDIEK MLIDVFPWIE
     DEKHNDLETL SKIHSNQCVL LADDSPSVLK TMQMILDKLG VKHIDFINGK TLLEHLFNPT
     TDVSNIGLII TDLEMPEASG FEVIKQVKNN PLTSKIPIVV NSSMSGSSNE DMARSLKADD
     FISKSNPKDI QRVVKQFLEL A