CHEV_BACSU
ID CHEV_BACSU Reviewed; 303 AA.
AC P37599;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Chemotaxis protein CheV;
GN Name=cheV; OrderedLocusNames=BSU14010;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DOMAIN.
RC STRAIN=168;
RX PubMed=8169223; DOI=10.1128/jb.176.9.2727-2735.1994;
RA Fredrick K.L., Helmann J.D.;
RT "Dual chemotaxis signaling pathways in Bacillus subtilis: a sigma D-
RT dependent gene encodes a novel protein with both CheW and CheY homologous
RT domains.";
RL J. Bacteriol. 176:2727-2735(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Scanlan E., Devine K.M.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / OI1085;
RX PubMed=8169224; DOI=10.1128/jb.176.9.2736-2739.1994;
RA Rosario M.M.L., Fredrick K.L., Ordal G.W., Helmann J.D.;
RT "Chemotaxis in Bacillus subtilis requires either of two functionally
RT redundant CheW homologs.";
RL J. Bacteriol. 176:2736-2739(1994).
RN [5]
RP FUNCTION IN ADAPTATION, PHOSPHORYLATION AT ASP-235 BY CHEA, AND MUTAGENESIS
RP OF ASP-235.
RC STRAIN=168 / OI1085;
RX PubMed=11553614; DOI=10.1074/jbc.m104955200;
RA Karatan E., Saulmon M.M., Bunn M.W., Ordal G.W.;
RT "Phosphorylation of the response regulator CheV is required for adaptation
RT to attractants during Bacillus subtilis chemotaxis.";
RL J. Biol. Chem. 276:43618-43626(2001).
CC -!- FUNCTION: Involved in the transmission of sensory signals from the
CC chemoreceptors to the flagellar motors. Chemotaxis involves both a
CC phosphorylation-dependent excitation and a methylation-dependent
CC adaptation. CheV and CheW are involved in the coupling of the methyl-
CC accepting chemoreceptors to the central two-component kinase CheA; they
CC are both necessary for efficient chemotaxis. Moreover, CheA-dependent
CC phosphorylation of CheV is required for adaptation to attractants
CC during B.subtilis chemotaxis. {ECO:0000269|PubMed:11553614,
CC ECO:0000269|PubMed:8169224}.
CC -!- DEVELOPMENTAL STAGE: Peak expression is seen in early stationary phase.
CC -!- DOMAIN: Consists of two domains: an N-terminal CheW-like coupling
CC domain and a C-terminal two-component receiver domain.
CC {ECO:0000269|PubMed:8169223}.
CC -!- PTM: Phosphorylated by CheA. {ECO:0000269|PubMed:11553614}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking CheV are somewhat reduced in
CC chemotactic proficiency, but a double mutant lacking both CheV and CheW
CC has a strong tumble bias, does not respond to addition of attractant,
CC shows essentially no accumulation in capillary assays, and has greatly
CC reduced methyl turnover on the methyl-accepting chemotaxis proteins
CC (MCPs). {ECO:0000269|PubMed:8169224}.
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DR EMBL; Z29584; CAA82701.1; -; Genomic_DNA.
DR EMBL; U05345; AAA16526.1; -; Unassigned_DNA.
DR EMBL; AJ222587; CAA10864.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13274.1; -; Genomic_DNA.
DR PIR; A55592; A55592.
DR RefSeq; NP_389284.1; NC_000964.3.
DR RefSeq; WP_009967126.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P37599; -.
DR SMR; P37599; -.
DR IntAct; P37599; 1.
DR MINT; P37599; -.
DR STRING; 224308.BSU14010; -.
DR jPOST; P37599; -.
DR PaxDb; P37599; -.
DR PRIDE; P37599; -.
DR DNASU; 939239; -.
DR EnsemblBacteria; CAB13274; CAB13274; BSU_14010.
DR GeneID; 939239; -.
DR KEGG; bsu:BSU14010; -.
DR PATRIC; fig|224308.179.peg.1528; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG0835; Bacteria.
DR InParanoid; P37599; -.
DR OMA; RLEWNQV; -.
DR PhylomeDB; P37599; -.
DR BioCyc; BSUB:BSU14010-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0006935; P:chemotaxis; IGI:CACAO.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR InterPro; IPR024181; Chemotax_regulator_CheV.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR Pfam; PF01584; CheW; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PIRSF; PIRSF002867; CheV; 1.
DR SMART; SM00260; CheW; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF50341; SSF50341; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW Chemotaxis; Phosphoprotein; Reference proteome.
FT CHAIN 1..303
FT /note="Chemotaxis protein CheV"
FT /id="PRO_0000198353"
FT DOMAIN 16..154
FT /note="CheW-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00052"
FT DOMAIN 176..302
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MOD_RES 235
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169,
FT ECO:0000269|PubMed:11553614"
FT MUTAGEN 235
FT /note="D->A: Is severely impaired in adaptation to the
FT addition of asparagine. Shows near normal counterclockwise
FT bias in the absence of attractant. Is not phosphorylated in
FT the presence of CheA-P."
FT /evidence="ECO:0000269|PubMed:11553614"
SQ SEQUENCE 303 AA; 34634 MW; E6B0BA91461C4D18 CRC64;
MSLQQYEILL DSGTNELEIV KFGVGENAFG INVMKVREII QPVEVTSVPH SHQHVEGMIK
LRGEILPVIS LFSFFGVEPE GSKDEKYIVT EFNKRKIVFH VGSVSQIHRV SWEAIEKPTS
LNQGMERHLT GIIKLEDLMI FLPDYEKIIY DIESDSGVDT YNMHTEGFDE RRTDKKLIIV
EDSPLLMRLL QDELKEAGYN NIASFENGKE AYEYIMNLAE NETDLSKQID MIITDIEMPK
MDGHRLTKLL KENPKSSDVP VMIFSSLITD DLRHRGEVVG ADEQISKPEI SDLIKKVDTY
VIE
