ID CHEA_BORBU Reviewed; 864 AA. AC Q44737; P70857; Q44877; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 16-JUN-2009, entry version 69. DE RecName: Full=Chemotaxis protein cheA; DE EC=2.7.13.3; GN Name=cheA; OrderedLocusNames=BB_0669; OS Borrelia burgdorferi (Lyme disease spirochete). OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia; OC Borrelia burgdorferi group. OX NCBI_TaxID=139; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=212; RX MEDLINE=98438936; PubMed=9765799; DOI=10.1016/S0923-2508(97)85239-4; RA Trueba G.A., Old I.G., Saint-Girons I., Johnson R.C.; RT "A cheA cheW operon in Borrelia burgdorferi, the agent of Lyme RT disease."; RL Res. Microbiol. 148:191-200(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35210 / B31 / CIP 102532 / DSM 4680; RX MEDLINE=98065943; PubMed=9403685; DOI=10.1038/37551; RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., RA Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D., RA Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J., RA Salzberg S.L., Hanson M., van Vugt R., Palmer N., Adams M.D., RA Gocayne J.D., Weidman J.F., Utterback T.R., Watthey L., McDonald L.A., RA Artiach P., Bowman C., Garland S.A., Fujii C., Cotton M.D., Horst K., RA Roberts K.M., Hatch B., Smith H.O., Venter J.C.; RT "Genomic sequence of a Lyme disease spirochaete, Borrelia RT burgdorferi."; RL Nature 390:580-586(1997). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30. RC STRAIN=212; RX MEDLINE=97144545; PubMed=8990312; RA Ge Y., Charon N.W.; RT "An unexpected flaA homolog is present and expressed in Borrelia RT burgdorferi."; RL J. Bacteriol. 179:552-556(1997). CC -!- FUNCTION: Involved in the transmission of sensory signals from the CC chemoreceptors to the flagellar motors. CheA is CC autophosphorylated; it can transfer its phosphate group to either CC cheB or cheY (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + protein L-histidine = ADP + protein N- CC phospho-L-histidine. CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential). CC -!- SIMILARITY: Contains 1 cheW-like domain. CC -!- SIMILARITY: Contains 1 histidine kinase domain. CC -!- SIMILARITY: Contains 1 HPt domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U28962; AAB96835.1; -; Genomic_DNA. DR EMBL; AE000783; AAC67024.1; -; Genomic_DNA. DR EMBL; U62900; AAC44771.1; -; Genomic_DNA. DR EMBL; X91907; CAA63002.1; -; Genomic_DNA. DR PIR; D70183; D70183. DR RefSeq; NP_212803.1; -. DR HSSP; Q56310; 1I59. DR GeneID; 1195521; -. DR GenomeReviews; AE000783_GR; BB_0669. DR KEGG; bbu:BB0669; -. DR NMPDR; fig|224326.1.peg.1053; -. DR TIGR; BB_0669; -. DR HOGENOM; Q44737; -. DR OMA; Q44737; SHEVHIT. DR BioCyc; BBUR224326:BB_0669-MON; -. DR BRENDA; 2.7.13.3; 142596. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0000155; F:two-component sensor activity; IEA:InterPro. DR GO; GO:0006928; P:cell motion; IEA:InterPro. DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW. DR GO; GO:0018106; P:peptidyl-histidine phosphorylation; IEA:InterPro. DR GO; GO:0000160; P:two-component signal transduction system (p...; IEA:UniProtKB-KW. DR InterPro; IPR003594; ATP_bd_ATPase. DR InterPro; IPR002545; CheW. DR InterPro; IPR004358; Sig_transdc_His_kin-like_C. DR InterPro; IPR008207; Sig_transdc_His_kin_P-trf. DR InterPro; IPR004105; Sig_transdc_His_kin_subgr_dim. DR InterPro; IPR005467; Sig_transdc_His_kinase_core. DR InterPro; IPR010808; Sig_transdc_His_kinase_P2-bd. DR Gene3D; G3DSA:3.30.565.10; ATP_bd_ATPase; 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 ProDom; PD003142; Hpt_N; 1. DR SMART; SM00260; CheW; 1. DR SMART; SM00387; HATPase_c; 1. DR SMART; SM00073; HPT; 1. DR PROSITE; PS50851; CHEW; 1. DR PROSITE; PS50109; HIS_KIN; 1. DR PROSITE; PS50894; HPT; 1. PE 3: Inferred from homology; KW ATP-binding; Chemotaxis; Complete proteome; Cytoplasm; Kinase; KW Nucleotide-binding; Phosphoprotein; Transferase; KW Two-component regulatory system. FT CHAIN 1 864 Chemotaxis protein cheA. FT /FTId=PRO_0000074712. FT DOMAIN 1 108 HPt. FT DOMAIN 480 725 Histidine kinase. FT DOMAIN 727 864 CheW-like. FT MOD_RES 51 51 Phosphohistidine; by autocatalysis (By FT similarity). FT CONFLICT 11 11 L -> I (in Ref. 1; AAB96835). FT CONFLICT 182 182 S -> H (in Ref. 1; AAB96835). FT CONFLICT 187 187 S -> G (in Ref. 1; AAB96835). FT CONFLICT 239 239 L -> S (in Ref. 1; AAB96835). FT CONFLICT 362 362 A -> S (in Ref. 1; AAB96835). FT CONFLICT 559 559 S -> P (in Ref. 1; AAB96835). SQ SEQUENCE 864 AA; 98353 MW; C1111DE0877BE624 CRC64; MEILDLENEE LLGVFFEEAQ NLVDILEENI MSLEDDPNNS DTIDEIFRAA HTLKGSSASL DMMELSDFTH IVEDVFDAIR DGKVNINNDL VDLLLSSLDV IKEMLALRID GKVYLNDISD LKSKLKQFLV IDDQTFIKRF DGNSIKNNFC LSESDLEEIR EGLGIGQKVL RISVVFNSNS NSEVENSGLK IFNILKNLGS VLHTIPKYEQ IIEDKFLKRV DYYLIYSDIE GVKKSLDSLN LIESYLVDEF NVKEELKKLA DEEIKDVDLD SNFVLNDNFD FTEDEISDLL LEVENQKLFK VRLDFVKDNP MATISGLQML QALKSLGKIF KSIPDSSELL ADKFFDFVIY YLISNTSEES IAKKINLPDV VSHFEIKNVN LESLKSVRLK EDDEAPFKEN KNIKKNSPIS VNLIRIDSKK IDYILNLVSE AVISKSSYNQ INSEMITLFY NFNYFYDYQE SFQRNFLIDL KIVFKDAGLT LEDEIESHIN SLMSFKMEKA LKDISELRNS FFRLLQNFKM TSGRLSRIIT DLHESVLKTR MLPISNIFSR FTRVVRDLSK KLNKIVNLKM EGEETELDKS VIDDLVDPLM HCVRNSMDHG LETVEERVKR GKSKAGTIIL RAKNEGNVIS IEIEDDGIGI DPKVIRRKLI EKGTIKEDAI YSDFELINLI FAPGFSTAVQ VTDLSGRGVG LDVVKKSIEK LNGTILVESE IGLGTIFKIK LPLTLVIIQG LLVKSGSETY VIPLNNVLET HRITEHDIKL LENYHEVYNL RDEVISVLRL DKLFNITRDD SLIEKFLIVV NTSNMKIAIV VDSILGEEDF VVKPIKDKFS SSAGIVGATT LGNGKVVLII DVFKLFDLQK DTKE //