ID   CHEA_BACSU              Reviewed;         672 AA.
AC   P29072;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   02-SEP-2026, entry version 165.
DE   RecName: Full=Chemotaxis protein CheA;
DE            EC=2.7.13.3;
GN   Name=cheA; Synonyms=cheN; OrderedLocusNames=BSU16430;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1938941; DOI=10.1128/jb.173.23.7443-7448.1991;
RA   Fuhrer D.K., Ordal G.W.;
RT   "Bacillus subtilis CheN, a homolog of CheA, the central regulator of
RT   chemotaxis in Escherichia coli.";
RL   J. Bacteriol. 173:7443-7448(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   SEQUENCE REVISION TO 271-272; 462 AND 466.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PHOSPHORYLATION OF CHEV.
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. CheA is autophosphorylated; it
CC       can transfer its phosphate group to CheB, CheY or CheV.
CC       {ECO:0000269|PubMed:11553614}.
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:11553614};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}. Note=It is not known
CC       whether CheA is actually membrane bound although CheA has two regions
CC       at the C-terminal end with the potential to be transmembrane regions.
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DR   EMBL; M57894; AAA22313.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13516.2; -; Genomic_DNA.
DR   PIR; A41653; QRBSCN.
DR   RefSeq; NP_389525.2; NC_000964.3.
DR   RefSeq; WP_003245734.1; NC_000964.3.
DR   AlphaFoldDB; P29072; -.
DR   SMR; P29072; -.
DR   FunCoup; P29072; 310.
DR   IntAct; P29072; 7.
DR   STRING; 224308.BSU16430; -.
DR   jPOST; P29072; -.
DR   PaxDb; 224308-BSU16430; -.
DR   EnsemblBacteria; CAB13516; CAB13516; BSU_16430.
DR   GeneID; 939600; -.
DR   KEGG; bsu:BSU16430; -.
DR   PATRIC; fig|224308.179.peg.1784; -.
DR   eggNOG; COG0643; Bacteria.
DR   eggNOG; COG2198; Bacteria.
DR   InParanoid; P29072; -.
DR   OrthoDB; 9803176at2; -.
DR   PhylomeDB; P29072; -.
DR   BioCyc; BSUB:BSU16430-MONOMER; -.
DR   BRENDA; 2.7.13.3; 658.
DR   Proteomes; UP000001570; Chromosome.
DR   AbasyAtlas; P29072; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IBA:GO_Central.
DR   GO; GO:0071978; P:bacterial-type flagellum-dependent swarming motility; IMP:CACAO.
DR   GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IBA:GO_Central.
DR   GO; GO:0050920; P:regulation of chemotaxis; IBA:GO_Central.
DR   CDD; cd00731; CheA_reg; 1.
DR   CDD; cd16916; HATPase_CheA-like; 1.
DR   CDD; cd00088; HPT; 1.
DR   FunFam; 3.30.565.10:FF:000016; Chemotaxis protein CheA, putative; 1.
DR   Gene3D; 1.10.287.560; Histidine kinase CheA-like, homodimeric domain; 1.
DR   Gene3D; 3.30.70.1110; Histidine kinase CheA-like, P2 response regulator-binding domain; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 1.20.120.160; HPT domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR051315; Bact_Chemotaxis_CheA.
DR   InterPro; IPR004105; CheA-like_dim.
DR   InterPro; IPR037006; CheA-like_homodim_sf.
DR   InterPro; IPR037052; CheA-like_P2_sf.
DR   InterPro; IPR010808; CheA_P2-bd.
DR   InterPro; IPR036061; CheW-like_dom_sf.
DR   InterPro; IPR002545; CheW-lke_dom.
DR   InterPro; IPR035891; CheY-binding_CheA.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR003594; HATPase_dom.
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   PANTHER; PTHR43395:SF1; CHEMOTAXIS PROTEIN CHEA; 1.
DR   PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
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; PF07194; P2; 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   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF50341; CheW-like; 1.
DR   SUPFAM; SSF55052; CheY-binding domain of CheA; 1.
DR   SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50851; CHEW; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50894; HPT; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Chemotaxis; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Transferase;
KW   Two-component regulatory system.
FT   CHAIN           1..672
FT                   /note="Chemotaxis protein CheA"
FT                   /id="PRO_0000074711"
FT   DOMAIN          1..103
FT                   /note="HPt"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00110"
FT   DOMAIN          290..540
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   DOMAIN          542..672
FT                   /note="CheW-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00052"
FT   REGION          250..292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        253..262
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        271..286
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         46
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   CONFLICT        271..272
FT                   /note="KQ -> NE (in Ref. 1; AAA22313)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        462
FT                   /note="A -> P (in Ref. 1; AAA22313)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        466
FT                   /note="Missing (in Ref. 1; AAA22313)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   672 AA;  74812 MW;  7BC3456AC34CB999 CRC64;
     MDMNQYLDVF IDESKEHLQT CNEKLLLLEK DPTDLQLVHD IFRAAHTLKG MSATMGYTDL
     AHLTHLLENV LDAIRNGDME VTSDWLDILF EALDHLETMV QSIIDGGDGK RDISEVSAKL
     DVNGAHAESA ASAEPAEAQS SASDWEYDEF ERTVIQEAEE QGFKRYEIKI SLNENCMLKA
     VRVYMVFEKL NEVGEVAKTI PSAEVLETED FGTDFQVCFL THQSAEDIEQ LINGVSEIEH
     VEVIQGAPLT SAEKPEESKQ EDSPAAAVPA KQEKQKQPAK NDEQAKHSAG GSKTIRVNID
     RLDSLMNLFE ELVIDRGRLE QIAKELEHNE LTETVERMTR ISGDLQSIIL NMRMVPVETV
     FNRFPRMIRQ LQKELNKKIE LSIIGAETEL DRTVIDEIGD PLVHLIRNSI DHGIEAPETR
     LQKGKPESGK VVLKAYHSGN HVFIEVEDDG AGLNRKKILE KALERGVITE KEAETLEDNQ
     IYELIFAPGF STADQISDIS GRGVGLDVVK NKLESLGGSV SVKSAEGQGS LFSIQLPLTL
     SIISVLLIKL EEETFAIPIS SIIETAVIDR KDILQTHDRE VIDFRGHIVP VVYLKEEFKI
     EDTRKDAEQL HIIVVKKGDK PTAFVVDSFI GQQEVVLKSL GDYLTNVFAI SGATILGDGE
     VALIIDCNAL II
//