CHEAY_HELPY
ID CHEAY_HELPY Reviewed; 803 AA.
AC O25153;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 149.
DE RecName: Full=Sensor histidine kinase CheAY;
DE EC=2.7.13.3 {ECO:0000269|PubMed:16207913};
GN Name=cheAY; OrderedLocusNames=HP_0392;
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 DOMAIN.
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 [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND AUTOPHOSPHORYLATION.
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).
CC -!- FUNCTION: Member of the two-component regulatory system CheAY/CheY that
CC regulates chemotaxis and colonization of the gastric mucosa
CC (PubMed:10722597). Functions as a sensor protein kinase which is
CC autophosphorylated at a histidine residue and transfers its phosphate
CC group to the conserved aspartic acid residue in the regulatory domain
CC of CheY (PubMed:16207913). In turn, phosphorylated CheY (CheY-P)
CC interacts with the flagellar motor protein FliM to cause clockwise
CC flagellar rotation and bacterial reversals, as opposed to straight
CC swimming when CheY is not phosphorylated (By similarity).
CC {ECO:0000250|UniProtKB:P71403, ECO:0000269|PubMed:10722597,
CC ECO:0000269|PubMed:16207913}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000269|PubMed:16207913};
CC -!- INTERACTION:
CC O25153; O25152: cheW; NbExp=3; IntAct=EBI-6410665, EBI-7496390;
CC O25153; P71403: cheY1; NbExp=3; IntAct=EBI-6410665, EBI-6409045;
CC -!- DOMAIN: Contains a C-terminal CheY-like regulatory domain where the
CC phosphate can be transferred. {ECO:0000269|PubMed:10722597}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:16207913}.
CC -!- DISRUPTION PHENOTYPE: Mutants are unable to colonize mice.
CC {ECO:0000269|PubMed:16207913}.
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DR EMBL; AE000511; AAD07457.1; -; Genomic_DNA.
DR PIR; H64568; H64568.
DR RefSeq; NP_207190.1; NC_000915.1.
DR RefSeq; WP_000342347.1; NC_018939.1.
DR AlphaFoldDB; O25153; -.
DR SMR; O25153; -.
DR DIP; DIP-3162N; -.
DR IntAct; O25153; 5.
DR MINT; O25153; -.
DR STRING; 85962.C694_01990; -.
DR PaxDb; O25153; -.
DR EnsemblBacteria; AAD07457; AAD07457; HP_0392.
DR KEGG; hpy:HP_0392; -.
DR PATRIC; fig|85962.47.peg.416; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR OMA; MMDMAKS; -.
DR PhylomeDB; O25153; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 1.10.287.560; -; 1.
DR Gene3D; 1.20.120.160; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR004105; CheA-like_dim.
DR InterPro; IPR037006; CheA-like_homodim_sf.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR Pfam; PF01584; CheW; 1.
DR Pfam; PF02895; H-kinase_dim; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00260; CheW; 1.
DR SMART; SM01231; H-kinase_dim; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF47226; SSF47226; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF50341; SSF50341; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW Kinase; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..803
FT /note="Sensor histidine kinase CheAY"
FT /id="PRO_0000448747"
FT DOMAIN 270..517
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 519..653
FT /note="CheW-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00052"
FT DOMAIN 678..796
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT REGION 134..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Phosphohistidine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00110"
FT MOD_RES 273
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 729
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 803 AA; 89759 MW; B6D9B0FC82B54E27 CRC64;
MDDLQEIMED FLIEAFEMNE QLDQDLVELE HNPEDLDLLN RIFRVAHTIK GSSSFLNLNI
LTHLTHNMED VLNRARKGEI KITPDIMDVV LRSIDLMKTL LVTIRDTGSD TNNGKENEIE
EAVKQLQAIT SQNLESAKER TTEAPQKENK EETKEEAKEE NKENKAKAPT AENTSSDNPL
ADEPDLDYAN MSAEEVEAEI ERLLNKRQEA DKERRAQKKQ EAKPKQEVTP TKETPKAPKT
ETKAKAKADT EENKAPSIGV EQTVRVDVRR LDHLMNLIGE LVLGKNRLIR IYSDVEERYD
GEKFLEELNQ VVSSISAVTT DLQLAVMKTR MQPVGKVFNK FPRMVRDLSR ELGKSIELII
EGEETELDKS IVEEIGDPLI HIIRNSCDHG IEPLEERRKL NKPETGKVQL SAYNEGNHIV
IKISDDGKGL DPVMLKEKAI EKGVISERDA EGMSDREAFN LIFKPGFSTA KVVSNVSGRG
VGMDVVKTNI EKLNGIIEID SEVGVGTTQK LKIPLTLAII QALLVGVQEE YYAIPLSSVL
ETVRISQDEI YTVDGKSVLR LRDEVLSLVR LSDIFKVDAI LESNSDVYVV IIGLADQKIG
VIVDYLIGQE EVVIKSLGYY LKNTRGIAGA TVRGDGKITL IVDVGAMMDM AKSIKVNITT
LMNESENTKS KNSPSDYIVL AIDDSSTDRA IIRKCLKPLG ITLLEATNGL EGLEMLKNGD
KIPDAILVDI EMPKMDGYTF ASEVRKYNKF KNLPLIAVTS RVTKTDRMRG VESGMTEYIT
KPYSGEYLTT VVKRSIKLEG DQS
