ID   CHEY1_HELPJ             Reviewed;         124 AA.
AC   Q9ZM64;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Chemotaxis protein CheY1;
GN   Name=cheY1; OrderedLocusNames=jhp_0358;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
CC   -!- FUNCTION: Chemotactic response regulator protein that modulates the
CC       rotation direction of bacterial flagellar motors. Plays an important
CC       role in the colonization and infection of Helicobacter pylori. Upon
CC       phosphorylation by CheA, interacts with the flagellar motor protein
CC       FliM to cause clockwise flagellar rotation and bacterial reversals, as
CC       opposed to straight swimming when CheY1 is not phosphorylated.
CC       {ECO:0000250|UniProtKB:P71403}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P71403};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Interacts (when phosphorylated) with FliM.
CC       {ECO:0000250|UniProtKB:P71403}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- PTM: Phosphorylated by CheAY. Dephosphorylated (inactivated) by CheZ.
CC       {ECO:0000250|UniProtKB:P71403}.
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DR   EMBL; AE001439; AAD05946.1; -; Genomic_DNA.
DR   PIR; F71941; F71941.
DR   RefSeq; WP_000772146.1; NZ_CP011330.1.
DR   AlphaFoldDB; Q9ZM64; -.
DR   SMR; Q9ZM64; -.
DR   STRING; 85963.jhp_0358; -.
DR   EnsemblBacteria; AAD05946; AAD05946; jhp_0358.
DR   GeneID; 66521625; -.
DR   KEGG; hpj:jhp_0358; -.
DR   PATRIC; fig|85963.30.peg.653; -.
DR   eggNOG; COG0745; Bacteria.
DR   OMA; AAGAHEY; -.
DR   Proteomes; UP000000804; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0097588; P:archaeal or bacterial-type flagellum-dependent cell motility; IEA:UniProtKB-KW.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   Pfam; PF00072; Response_reg; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   3: Inferred from homology;
KW   Chemotaxis; Cytoplasm; Flagellar rotation; Magnesium; Metal-binding;
KW   Phosphoprotein; Two-component regulatory system.
FT   CHAIN           1..124
FT                   /note="Chemotaxis protein CheY1"
FT                   /id="PRO_0000081051"
FT   DOMAIN          2..120
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   BINDING         8
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P71403"
FT   BINDING         53
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P71403"
FT   BINDING         55
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P71403"
FT   MOD_RES         53
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   124 AA;  13926 MW;  DFA619C0D4C90F63 CRC64;
     MKLLVVDDSS TMRRIIKNTL SRLGYEDVLE AEHGVEAWEK LDANADTKVL ITDWNMPEMN
     GLDLVKKVRA DNRFKEIPII MITTEGGKAE VITALKAGVN NYIVKPFTPQ VLKEKLEVVL
     GTND