CHEY1_HELPY
ID CHEY1_HELPY Reviewed; 124 AA.
AC P71403; O07677;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Chemotaxis protein CheY1 {ECO:0000303|PubMed:10722597};
GN Name=cheY1 {ECO:0000303|PubMed:10722597}; OrderedLocusNames=HP_1067;
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 [GENOMIC DNA].
RC STRAIN=ATCC 43504 / NCTC 11637 / JCM 7653 / RPH 13487;
RA Wren B.W.;
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 4867 / CCUG 17874 / NCTC 11638;
RX PubMed=9244252; DOI=10.1128/jb.179.15.4676-4683.1997;
RA Beier D., Spohn G., Rappuoli R., Scarlato V.;
RT "Identification and characterization of an operon of Helicobacter pylori
RT that is involved in motility and stress adaptation.";
RL J. Bacteriol. 179:4676-4683(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43504 / NCTC 11637 / JCM 7653 / RPH 13487;
RA Jackson C.J., Pittman M.S., Clayton C.L., McColm A.A., Bagshaw J.A.,
RA Kelly D.J.;
RT "Chemotaxis is essential for virulence in Helicobacter pylori:
RT identification of a novel signal transduction protein (CheF) with both CheA
RT and CheY domains.";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=10722597; DOI=10.1128/iai.68.4.2016-2023.2000;
RA Foynes S., Dorrell N., Ward S.J., Stabler R.A., McColm A.A., Rycroft A.N.,
RA Wren B.W.;
RT "Helicobacter pylori possesses two CheY response regulators and a histidine
RT kinase sensor, CheA, which are essential for chemotaxis and colonization of
RT the gastric mucosa.";
RL Infect. Immun. 68:2016-2023(2000).
RN [6]
RP PHOSPHORYLATION AT ASP-53, AND DEPHOSPHORYLATION BY CHEZ.
RX PubMed=16207913; DOI=10.1099/mic.0.28217-0;
RA Jimenez-Pearson M.A., Delany I., Scarlato V., Beier D.;
RT "Phosphate flow in the chemotactic response system of Helicobacter
RT pylori.";
RL Microbiology 151:3299-3311(2005).
RN [7]
RP DEPHOSPHORYLATION BY CHEZ.
RX PubMed=20497335; DOI=10.1111/j.1365-2958.2010.07200.x;
RA Lertsethtakarn P., Ottemann K.M.;
RT "A remote CheZ orthologue retains phosphatase function.";
RL Mol. Microbiol. 77:225-235(2010).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, FUNCTION,
RP AND INTERACTION WITH FLIM.
RX PubMed=20207758; DOI=10.1128/jb.00603-09;
RA Lam K.H., Ling T.K., Au S.W.;
RT "Crystal structure of activated CheY1 from Helicobacter pylori.";
RL J. Bacteriol. 192:2324-2334(2010).
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
CC (PubMed:10722597). Upon phosphorylation by CheA, interacts with the
CC flagellar motor protein FliM to cause clockwise flagellar rotation and
CC bacterial reversals, as opposed to straight swimming when CheY1 is not
CC phosphorylated (PubMed:20207758). {ECO:0000269|PubMed:10722597,
CC ECO:0000269|PubMed:20207758}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:20207758};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Interacts (when phosphorylated) with FliM.
CC {ECO:0000269|PubMed:20207758}.
CC -!- INTERACTION:
CC P71403; O25153: cheAY; NbExp=3; IntAct=EBI-6409045, EBI-6410665;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- PTM: Phosphorylated by CheAY (PubMed:16207913). Dephosphorylated
CC (inactivated) by CheZ (PubMed:16207913, PubMed:20497335).
CC {ECO:0000269|PubMed:16207913, ECO:0000269|PubMed:20497335}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA57487.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X81897; CAA57487.1; ALT_INIT; Genomic_DNA.
DR EMBL; U97567; AAB66375.1; -; Genomic_DNA.
DR EMBL; AE000511; AAD08113.1; -; Genomic_DNA.
DR EMBL; AF021090; AAD01682.1; -; Genomic_DNA.
DR PIR; C64653; C64653.
DR RefSeq; NP_207858.1; NC_000915.1.
DR RefSeq; WP_000772151.1; NC_018939.1.
DR PDB; 3GWG; X-ray; 1.80 A; A=1-124.
DR PDB; 3H1E; X-ray; 2.40 A; A=1-124.
DR PDB; 3H1F; X-ray; 2.20 A; A=1-124.
DR PDB; 3H1G; X-ray; 1.70 A; A=1-124.
DR PDBsum; 3GWG; -.
DR PDBsum; 3H1E; -.
DR PDBsum; 3H1F; -.
DR PDBsum; 3H1G; -.
DR AlphaFoldDB; P71403; -.
DR SMR; P71403; -.
DR DIP; DIP-3256N; -.
DR IntAct; P71403; 4.
DR MINT; P71403; -.
DR STRING; 85962.C694_05515; -.
DR PaxDb; P71403; -.
DR EnsemblBacteria; AAD08113; AAD08113; HP_1067.
DR KEGG; hpy:HP_1067; -.
DR PATRIC; fig|85962.47.peg.1146; -.
DR eggNOG; COG0745; Bacteria.
DR OMA; AAGAHEY; -.
DR PhylomeDB; P71403; -.
DR EvolutionaryTrace; P71403; -.
DR Proteomes; UP000000429; 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 1: Evidence at protein level;
KW 3D-structure; Chemotaxis; Cytoplasm; Flagellar rotation; Magnesium;
KW Metal-binding; Phosphoprotein; Reference proteome;
KW Two-component regulatory system.
FT CHAIN 1..124
FT /note="Chemotaxis protein CheY1"
FT /id="PRO_0000081050"
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:0007744|PDB:3GWG, ECO:0007744|PDB:3H1E,
FT ECO:0007744|PDB:3H1G"
FT BINDING 53
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0007744|PDB:3GWG, ECO:0007744|PDB:3H1E,
FT ECO:0007744|PDB:3H1G"
FT BINDING 55
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0007744|PDB:3GWG, ECO:0007744|PDB:3H1E,
FT ECO:0007744|PDB:3H1G"
FT MOD_RES 53
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169,
FT ECO:0000269|PubMed:16207913"
FT VARIANT 122
FT /note="T -> A (in strain: NCTC 11637 and NCTC 11638)"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:3H1G"
FT HELIX 10..22
FT /evidence="ECO:0007829|PDB:3H1G"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:3H1G"
FT HELIX 34..43
FT /evidence="ECO:0007829|PDB:3H1G"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:3H1G"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:3H1G"
FT HELIX 61..69
FT /evidence="ECO:0007829|PDB:3H1G"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:3H1E"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:3H1G"
FT HELIX 88..97
FT /evidence="ECO:0007829|PDB:3H1G"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:3H1G"
FT HELIX 109..120
FT /evidence="ECO:0007829|PDB:3H1G"
SQ SEQUENCE 124 AA; 13915 MW; F2B40BC0C04FCBFA CRC64;
MKLLVVDDSS TMRRIIKNTL SRLGYEDVLE AEHGVEAWEK LDANADTKVL ITDWNMPEMN
GLDLVKKVRS DSRFKEIPII MITTEGGKAE VITALKAGVN NYIVKPFTPQ VLKEKLEVVL
GTND
