ID   CHEC_BACSU              Reviewed;         209 AA.
AC   P40403;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=CheY-P phosphatase CheC;
DE            EC=3.-.-.-;
GN   Name=cheC; Synonyms=ylxJ; OrderedLocusNames=BSU16450;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2832368; DOI=10.1128/jb.170.4.1568-1574.1988;
RA   Helmann J.D., Marquez L.M., Chamberlin M.J.;
RT   "Cloning, sequencing, and disruption of the Bacillus subtilis sigma 28
RT   gene.";
RL   J. Bacteriol. 170:1568-1574(1988).
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   DISRUPTION PHENOTYPE.
RX   PubMed=7893679; DOI=10.1021/bi00011a040;
RA   Rosario M.M.L., Kirby J.R., Bochar D.A., Ordal G.W.;
RT   "Chemotactic methylation and behavior in Bacillus subtilis: role of two
RT   unique proteins, CheC and CheD.";
RL   Biochemistry 34:3823-3831(1995).
RN   [4]
RP   INTERACTION WITH CHED.
RX   PubMed=8866475; DOI=10.1111/j.1365-2958.1996.tb02560.x;
RA   Rosario M.M.L., Ordal G.W.;
RT   "CheC and CheD interact to regulate methylation of Bacillus subtilis
RT   methyl-accepting chemotaxis proteins.";
RL   Mol. Microbiol. 21:511-518(1996).
RN   [5]
RP   FUNCTION.
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).
RN   [6]
RP   MUTAGENESIS OF ASP-149.
RX   PubMed=16469702; DOI=10.1016/j.cell.2005.11.046;
RA   Chao X., Muff T.J., Park S.-Y., Zhang S., Pollard A.M., Ordal G.W.,
RA   Bilwes A.M., Crane B.R.;
RT   "A receptor-modifying deamidase in complex with a signaling phosphatase
RT   reveals reciprocal regulation.";
RL   Cell 124:561-571(2006).
CC   -!- FUNCTION: Involved in restoring normal CheY-P levels following the
CC       addition of attractant by increasing the rate of CheY-P hydrolysis. Is
CC       only 6% as active as FliY, which indicates that CheC may function after
CC       addition of an attractant to cope with increased levels of CheY-P
CC       whereas FliY may function constitutively to remove CheY-P around the
CC       flagellar switch to maintain an optimal level of CheY-P. In addition,
CC       it was shown to prevent methylation of the methyl-accepting chemotaxis
CC       proteins (MCPs). Inhibits CheD. {ECO:0000269|PubMed:14749334}.
CC   -!- SUBUNIT: Forms a complex with CheD.
CC   -!- DISRUPTION PHENOTYPE: Cells fail to synthesize flagellin protein and
CC       grow as long filaments. They do not respond to attractants. CheC
CC       mutants showed overmethylation of the MCPs compared with wild-type
CC       strain. {ECO:0000269|PubMed:7893679}.
CC   -!- SIMILARITY: Belongs to the CheC family. {ECO:0000305}.
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DR   EMBL; M20144; AAA61468.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13518.1; -; Genomic_DNA.
DR   PIR; A55216; A55216.
DR   RefSeq; NP_389527.1; NC_000964.3.
DR   RefSeq; WP_003231935.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; P40403; -.
DR   SMR; P40403; -.
DR   IntAct; P40403; 3.
DR   STRING; 224308.BSU16450; -.
DR   PaxDb; P40403; -.
DR   PRIDE; P40403; -.
DR   EnsemblBacteria; CAB13518; CAB13518; BSU_16450.
DR   GeneID; 939621; -.
DR   KEGG; bsu:BSU16450; -.
DR   PATRIC; fig|224308.179.peg.1786; -.
DR   eggNOG; COG1776; Bacteria.
DR   InParanoid; P40403; -.
DR   OMA; LYIETEI; -.
DR   PhylomeDB; P40403; -.
DR   BioCyc; BSUB:BSU16450-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0050918; P:positive chemotaxis; IMP:CACAO.
DR   Gene3D; 3.40.1550.10; -; 1.
DR   InterPro; IPR007597; CheC.
DR   InterPro; IPR028976; CheC-like_sf.
DR   Pfam; PF04509; CheC; 2.
DR   SUPFAM; SSF103039; SSF103039; 1.
PE   1: Evidence at protein level;
KW   Chemotaxis; Hydrolase; Reference proteome.
FT   CHAIN           1..209
FT                   /note="CheY-P phosphatase CheC"
FT                   /id="PRO_0000089638"
FT   MUTAGEN         149
FT                   /note="D->K: Impaired chemotaxis. No binding to CheD.
FT                   Almost no enhancement of CheC activity by CheD."
FT                   /evidence="ECO:0000269|PubMed:16469702"
SQ   SEQUENCE   209 AA;  23049 MW;  D4FBD9F5446E9DA7 CRC64;
     MSIFNGIKEE QMDILREVGN IGAGHSASAM AQLLNRKIDM EVPFAKLLSF DELVDFFGGA
     DVPVASIFLR MEGDLTGSMF FIMPFFQAEQ FIRELIGNPD FDIEDLGEDH MSSSALHELG
     NILAGSYLTA LADLTKLQLY PSVPEVSLDM FGAVISEGLM ELSQVGEHAI VVDTSIFDQS
     HQQELKAHMF MLPDYDSFEK LFVALGASL