ID   CHEV2_HELPY             Reviewed;         313 AA.
AC   O25337;
DT   11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 127.
DE   RecName: Full=Chemotaxis protein CheV2 {ECO:0000303|PubMed:11535789};
GN   Name=cheV2 {ECO:0000303|PubMed:11535789}; OrderedLocusNames=HP_0616;
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, DISRUPTION PHENOTYPE, AND PHOSPHORYLATION.
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   -!- PTM: Phosphorylated; probably by transfer of CheAY phosphate group.
CC       {ECO:0000269|PubMed:11535789}.
CC   -!- DISRUPTION PHENOTYPE: Deletion mutant is fully chemotactic and forms
CC       swarms the same way as wild-type strain (PubMed:11535789). Mutant shows
CC       however defects in mouse colonization (PubMed:19332820).
CC       {ECO:0000269|PubMed:11535789, ECO:0000269|PubMed:19332820}.
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DR   EMBL; AE000511; AAD07681.1; -; Genomic_DNA.
DR   PIR; H64596; H64596.
DR   RefSeq; NP_207411.1; NC_000915.1.
DR   RefSeq; WP_000251148.1; NC_018939.1.
DR   AlphaFoldDB; O25337; -.
DR   SMR; O25337; -.
DR   IntAct; O25337; 1.
DR   STRING; 85962.C694_03185; -.
DR   PaxDb; O25337; -.
DR   DNASU; 898950; -.
DR   EnsemblBacteria; AAD07681; AAD07681; HP_0616.
DR   KEGG; hpy:HP_0616; -.
DR   PATRIC; fig|85962.47.peg.664; -.
DR   eggNOG; COG0784; Bacteria.
DR   eggNOG; COG0835; Bacteria.
DR   OMA; YLAFPNG; -.
DR   PhylomeDB; O25337; -.
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   1: Evidence at protein level;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..313
FT                   /note="Chemotaxis protein CheV2"
FT                   /id="PRO_0000448750"
FT   DOMAIN          16..172
FT                   /note="CheW-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00052"
FT   DOMAIN          193..313
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   MOD_RES         246
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   313 AA;  35661 MW;  59007E3967980E16 CRC64;
     MVRDIDKTTS LHLNNEAQFL CFRLDAEKDA QLYGMNIFKI REIIHYDGEV TEILGGSDGV
     MLGFLSVRGE SIPLVDVKRW LHYNANDPSR DLKECSVKDD HNLVIVCHFS NHSIALKVLK
     IERIIHKNWT EISAGDKQGI NEEGKLSAIT RFDEERVVQI LDVEKMISDV FPSLKDLDDL
     TLRCIEAIQS QKLILIAEDS LSALKTLEKI VQTLELRYLA FPNGRELLDY LYEKEHYQQV
     GVVITDLEMP NISGFEVLKT IKADHRTEHL PVIINSSMSS DSNRQLAQSL EADGFVVKSN
     ILEIHEMLKK TLS