CHEA_BORBU
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 25-MAY-2022, entry version 140.
DE RecName: Full=Chemotaxis protein CheA;
DE EC=2.7.13.3;
GN Name=cheA; OrderedLocusNames=BB_0669;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=212;
RX 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 disease.";
RL Res. Microbiol. 148:191-200(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX 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., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30.
RC STRAIN=212;
RX PubMed=8990312; DOI=10.1128/jb.179.2.552-556.1997;
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 autophosphorylated; it
CC can transfer its phosphate group to either CheB or CheY (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {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; 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; NC_001318.1.
DR RefSeq; WP_010889794.1; NC_001318.1.
DR AlphaFoldDB; Q44737; -.
DR SMR; Q44737; -.
DR STRING; 224326.BB_0669; -.
DR PRIDE; Q44737; -.
DR EnsemblBacteria; AAC67024; AAC67024; BB_0669.
DR KEGG; bbu:BB_0669; -.
DR PATRIC; fig|224326.49.peg.1060; -.
DR HOGENOM; CLU_000650_3_2_12; -.
DR OMA; MMDMAKS; -.
DR BRENDA; 2.7.13.3; 902.
DR Proteomes; UP000001807; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 1.10.287.560; -; 1.
DR Gene3D; 1.20.120.160; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR Gene3D; 3.30.70.1110; -; 1.
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; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
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 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; 2.
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; SSF47226; SSF47226; 1.
DR SUPFAM; SSF50341; SSF50341; 1.
DR SUPFAM; SSF55052; SSF55052; 2.
DR SUPFAM; SSF55874; SSF55874; 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; Cytoplasm; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase;
KW Two-component regulatory system.
FT CHAIN 1..864
FT /note="Chemotaxis protein CheA"
FT /id="PRO_0000074712"
FT DOMAIN 1..108
FT /note="HPt"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00110"
FT DOMAIN 480..725
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 727..864
FT /note="CheW-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00052"
FT MOD_RES 51
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT CONFLICT 11
FT /note="L -> I (in Ref. 1; AAB96835)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="S -> H (in Ref. 1; AAB96835)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="S -> G (in Ref. 1; AAB96835)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="L -> S (in Ref. 1; AAB96835)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="A -> S (in Ref. 1; AAB96835)"
FT /evidence="ECO:0000305"
FT CONFLICT 559
FT /note="S -> P (in Ref. 1; AAB96835)"
FT /evidence="ECO:0000305"
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
