CHEY_BACSU
ID CHEY_BACSU Reviewed; 120 AA.
AC P24072; P37583;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Chemotaxis protein CheY;
GN Name=cheY; Synonyms=cheB; OrderedLocusNames=BSU16330;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / OI1085;
RX PubMed=1905718; DOI=10.1016/s0021-9258(18)98896-4;
RA Bischoff D.S., Ordal G.W.;
RT "Sequence and characterization of Bacillus subtilis CheB, a homolog of
RT Escherichia coli CheY, and its role in a different mechanism of
RT chemotaxis.";
RL J. Biol. Chem. 266:12301-12305(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
RC STRAIN=168 / OI1085;
RX PubMed=1447979; DOI=10.1111/j.1365-2958.1992.tb01448.x;
RA Bischoff D.S., Ordal G.W.;
RT "Identification and characterization of FliY, a novel component of the
RT Bacillus subtilis flagellar switch complex.";
RL Mol. Microbiol. 6:2715-2723(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 96-120.
RC STRAIN=168 / OI1085;
RX PubMed=1597417; DOI=10.1128/jb.174.12.4017-4025.1992;
RA Bischoff D.S., Weinreich M.D., Ordal G.W.;
RT "Nucleotide sequences of Bacillus subtilis flagellar biosynthetic genes
RT fliP and fliQ and identification of a novel flagellar gene, fliZ.";
RL J. Bacteriol. 174:4017-4025(1992).
RN [5]
RP PROTEIN SEQUENCE OF 2-13.
RC STRAIN=168 / JH642;
RX PubMed=8755892; DOI=10.1128/jb.178.15.4611-4619.1996;
RA Graumann P., Schroeder K., Schmid R., Marahiel M.A.;
RT "Cold shock stress-induced proteins in Bacillus subtilis.";
RL J. Bacteriol. 178:4611-4619(1996).
RN [6]
RP FUNCTION, PHOSPHORYLATION BY CHEA, AND MUTAGENESIS OF ASP-10 AND ASP-54.
RC STRAIN=168 / OI1085;
RX PubMed=8369293; DOI=10.1021/bi00086a035;
RA Bischoff D.S., Bourret R.B., Kirsch M.L., Ordal G.W.;
RT "Purification and characterization of Bacillus subtilis CheY.";
RL Biochemistry 32:9256-9261(1993).
RN [7]
RP FUNCTION, PHOSPHORYLATION AT ASP-54, DEPHOSPHORYLATION BY FLIY, INTERACTION
RP WITH FLIM AND FLIY, AND MUTAGENESIS OF ASP-54.
RC STRAIN=168 / OI1085;
RX PubMed=12920116; DOI=10.1074/jbc.m306180200;
RA Szurmant H., Bunn M.W., Cannistraro V.J., Ordal G.W.;
RT "Bacillus subtilis hydrolyzes CheY-P at the location of its action, the
RT flagellar switch.";
RL J. Biol. Chem. 278:48611-48616(2003).
RN [8]
RP DEPHOSPHORYLATION BY FLIY AND CHEC.
RC STRAIN=168 / OI1085;
RX PubMed=14749334; DOI=10.1074/jbc.m311497200;
RA Szurmant H., Muff T.J., Ordal G.W.;
RT "Bacillus subtilis CheC and FliY are members of a novel class of CheY-P-
RT hydrolyzing proteins in the chemotactic signal transduction cascade.";
RL J. Biol. Chem. 279:21787-21792(2004).
CC -!- FUNCTION: Involved in the transmission of sensory signals from the
CC chemoreceptors to the flagellar motors. Phosphorylated CheY interacts
CC with the flagella switch components FliM and FliY, which causes
CC counterclockwise rotation of the flagella, resulting in smooth
CC swimming. {ECO:0000269|PubMed:12920116, ECO:0000269|PubMed:8369293}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Phosphorylated CheY binds to FliM and FliY.
CC {ECO:0000269|PubMed:12920116}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- PTM: Phosphorylated by CheA. Dephosphorylated (inactivated) by FliY and
CC CheC. {ECO:0000269|PubMed:12920116, ECO:0000269|PubMed:8369293}.
CC -!- MISCELLANEOUS: The signaling mechanism of chemotaxis in B.subtilis
CC appears to be inverted in comparison to E.coli.
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DR EMBL; M59781; AAA22311.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13506.1; -; Genomic_DNA.
DR EMBL; M86738; AAA22450.1; -; Genomic_DNA.
DR EMBL; M87005; AAA22451.1; -; Genomic_DNA.
DR PIR; A40874; A40874.
DR RefSeq; NP_389515.1; NC_000964.3.
DR RefSeq; WP_003244957.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P24072; -.
DR SMR; P24072; -.
DR STRING; 224308.BSU16330; -.
DR jPOST; P24072; -.
DR PaxDb; P24072; -.
DR PRIDE; P24072; -.
DR EnsemblBacteria; CAB13506; CAB13506; BSU_16330.
DR GeneID; 940120; -.
DR KEGG; bsu:BSU16330; -.
DR PATRIC; fig|224308.179.peg.1774; -.
DR eggNOG; COG2201; Bacteria.
DR InParanoid; P24072; -.
DR OMA; AAGAHEY; -.
DR PhylomeDB; P24072; -.
DR BioCyc; BSUB:BSU16330-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071978; P:bacterial-type flagellum-dependent swarming motility; IMP:CACAO.
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 Chemotaxis; Cytoplasm; Direct protein sequencing; Magnesium; Metal-binding;
KW Phosphoprotein; Reference proteome; Two-component regulatory system.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8755892"
FT CHAIN 2..120
FT /note="Chemotaxis protein CheY"
FT /id="PRO_0000081057"
FT DOMAIN 4..119
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 54
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 54
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MUTAGEN 10
FT /note="D->K,R: No chemotaxis, tumbly swimming behavior and
FT shows exclusively clockwise rotation."
FT /evidence="ECO:0000269|PubMed:8369293"
FT MUTAGEN 54
FT /note="D->A: Lack of phosphorylation. No chemotaxis, tumbly
FT swimming behavior and shows exclusively clockwise
FT rotation."
FT /evidence="ECO:0000269|PubMed:12920116,
FT ECO:0000269|PubMed:8369293"
FT MUTAGEN 54
FT /note="D->S,T: No chemotaxis, tumbly swimming behavior and
FT shows exclusively clockwise rotation."
FT /evidence="ECO:0000269|PubMed:12920116,
FT ECO:0000269|PubMed:8369293"
SQ SEQUENCE 120 AA; 13310 MW; C3F1A0F02CE67505 CRC64;
MAHRILIVDD AAFMRMMIKD ILVKNGFEVV AEAENGAQAV EKYKEHSPDL VTMDITMPEM
DGITALKEIK QIDAQARIIM CSAMGQQSMV IDAIQAGAKD FIVKPFQADR VLEAINKTLN
