ID   FLIY_BACSU              Reviewed;         378 AA.
AC   P24073;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 2.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Flagellar motor switch phosphatase FliY;
DE            EC=3.-.-.-;
DE   AltName: Full=CheY-P phosphatase FliY;
DE   AltName: Full=Flagellar motor switch protein FliY;
GN   Name=fliY; Synonyms=cheD; OrderedLocusNames=BSU16320;
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=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   [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 1-60.
RX   PubMed=1898932; DOI=10.1128/jb.173.2.710-719.1991;
RA   Zuberi A.R., Bischoff D.S., Ordal G.W.;
RT   "Nucleotide sequence and characterization of a Bacillus subtilis gene
RT   encoding a flagellar switch protein.";
RL   J. Bacteriol. 173:710-719(1991).
RN   [4]
RP   FUNCTION.
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   [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).
CC   -!- FUNCTION: Component of the flagellar switch. Binds CheY-P and increases
CC       its hydrolysis rate in vitro. May function constitutively to remove
CC       CheY-P around the flagellar switch to maintain an optimal level of
CC       CheY-P whereas CheC may function after addition of an attractant to
CC       cope with increased levels of CheY-P. {ECO:0000269|PubMed:12920116,
CC       ECO:0000269|PubMed:14749334}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The switch
CC       is localized at the base of the flagellar motor, in or near the C-ring,
CC       attached to the MS-ring. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FliN/MopA/SpaO family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M86738; AAA22449.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13505.1; -; Genomic_DNA.
DR   EMBL; M37691; AAA22447.1; -; Genomic_DNA.
DR   PIR; S25279; S25279.
DR   RefSeq; NP_389514.1; NC_000964.3.
DR   RefSeq; WP_003231962.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; P24073; -.
DR   SMR; P24073; -.
DR   STRING; 224308.BSU16320; -.
DR   jPOST; P24073; -.
DR   PaxDb; P24073; -.
DR   PRIDE; P24073; -.
DR   EnsemblBacteria; CAB13505; CAB13505; BSU_16320.
DR   GeneID; 936421; -.
DR   KEGG; bsu:BSU16320; -.
DR   PATRIC; fig|224308.179.peg.1773; -.
DR   eggNOG; COG1776; Bacteria.
DR   eggNOG; COG1886; Bacteria.
DR   InParanoid; P24073; -.
DR   OMA; MMGGDGK; -.
DR   PhylomeDB; P24073; -.
DR   BioCyc; BSUB:BSU16320-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0009425; C:bacterial-type flagellum basal body; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:CACAO.
DR   GO; GO:0044780; P:bacterial-type flagellum assembly; IMP:CACAO.
DR   GO; GO:0071978; P:bacterial-type flagellum-dependent swarming motility; IMP:CACAO.
DR   GO; GO:0006935; P:chemotaxis; IMP:CACAO.
DR   GO; GO:0016311; P:dephosphorylation; IMP:CACAO.
DR   GO; GO:1902021; P:regulation of bacterial-type flagellum-dependent cell motility; IMP:CACAO.
DR   Gene3D; 2.30.330.10; -; 1.
DR   Gene3D; 3.40.1550.10; -; 1.
DR   InterPro; IPR007597; CheC.
DR   InterPro; IPR028976; CheC-like_sf.
DR   InterPro; IPR012826; FliN.
DR   InterPro; IPR001543; FliN-like_C.
DR   InterPro; IPR001172; FliN_T3SS_HrcQb.
DR   InterPro; IPR036429; SpoA-like_sf.
DR   Pfam; PF04509; CheC; 2.
DR   Pfam; PF01052; FliMN_C; 1.
DR   PRINTS; PR00956; FLGMOTORFLIN.
DR   SUPFAM; SSF101801; SSF101801; 1.
DR   SUPFAM; SSF103039; SSF103039; 1.
DR   TIGRFAMs; TIGR02480; fliN; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Chemotaxis; Flagellar rotation; Hydrolase; Membrane;
KW   Reference proteome.
FT   CHAIN           1..378
FT                   /note="Flagellar motor switch phosphatase FliY"
FT                   /id="PRO_0000184133"
FT   REGION          225..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   378 AA;  41052 MW;  24E84990108567FC CRC64;
     MENNRLSQDE IDALLNGTGS TLDEPEIPEV DDLSEMERDA IGEIGNISFG SSATALSTLL
     NQKVDITTPS VTVIPRSKIS DAFPEPYVAI EVNYTEGFSG SNLLVVEQSD AAIIADLMIG
     GDGKGADPSL GEIHLSAVQE AMNQMMGSAA TSMSTVFSKK IDISPPRVEL LDVTEEKGTD
     RIPDDEMLVK VSFNLKVGEL IDSSIMQLYP LTFAKDLISS LMNSESAEEE ETVQPEVTYE
     QPKEPVTPEP RIEPKQQQQP PKRQGTAKKA APVQVSPVEF SAFDPNEAVQ APIHNLDMLL
     DIPLSITVEL GRTKRSVKEI LELSAGSIIE LDKLAGEPVD ILVNQRIVAK GEVVVIEENF
     GVRVTDILSQ AERINNLK