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Database: UniProt
Entry: A0A5C1QBF5_9SPIO
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ID   A0A5C1QBF5_9SPIO        Unreviewed;       687 AA.
AC   A0A5C1QBF5;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   08-OCT-2025, entry version 20.
DE   RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=EW093_04525 {ECO:0000313|EMBL:QEN03994.1};
OS   Thiospirochaeta perfilievii.
OC   Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia; Spirochaetales;
OC   Spirochaetaceae; Thiospirochaeta.
OX   NCBI_TaxID=252967 {ECO:0000313|EMBL:QEN03994.1, ECO:0000313|Proteomes:UP000323824};
RN   [1] {ECO:0000313|EMBL:QEN03994.1, ECO:0000313|Proteomes:UP000323824}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P {ECO:0000313|EMBL:QEN03994.1,
RC   ECO:0000313|Proteomes:UP000323824};
RA   Fomenkov A., Dubinina G., Grabovich M., Vincze T., Roberts R.J.;
RL   Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QEN03994.1, ECO:0000313|Proteomes:UP000323824}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P {ECO:0000313|EMBL:QEN03994.1,
RC   ECO:0000313|Proteomes:UP000323824};
RA   Leshcheva N., Mikheeva N.;
RT   "Complete Genome Sequence and Methylome Analysis of free living
RT   Spirochaetas.";
RL   Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
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.
CC       {ECO:0000256|ARBA:ARBA00035100}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
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DR   EMBL; CP035807; QEN03994.1; -; Genomic_DNA.
DR   RefSeq; WP_149567251.1; NZ_CP035807.1.
DR   AlphaFoldDB; A0A5C1QBF5; -.
DR   KEGG; sper:EW093_04525; -.
DR   OrthoDB; 9803176at2; -.
DR   Proteomes; UP000323824; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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; cd00731; CheA_reg; 1.
DR   CDD; cd16916; HATPase_CheA-like; 1.
DR   CDD; cd00088; HPT; 1.
DR   FunFam; 2.30.30.40:FF:000048; Chemotaxis protein CheA, putative; 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; 3.30.565.10; 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; IPR036061; CheW-like_dom_sf.
DR   InterPro; IPR002545; CheW-lke_dom.
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   InterPro; IPR037257; T2SS_E_N_sf.
DR   PANTHER; PTHR43395:SF10; 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   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; SSF160246; EspE N-terminal domain-like; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00110}; Reference proteome {ECO:0000313|Proteomes:UP000323824};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          1..103
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   DOMAIN          269..545
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          547..679
FT                   /note="CheW-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50851"
FT   MOD_RES         46
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   687 AA;  76897 MW;  656A4286EA5368CE CRC64;
     MEDDNFIKIF KEEALELLGH LEDSLLELES SPDDEDLISA VFRVMHTVKG SAGMVGLDLI
     SKFTHEVESI LESVRSGDIK VSKGFIDYTL RSRDIILSMI NDPEYRIDDQ EAFFVDFKNA
     LNENYISPDD NKESITYRVI FKPEPKMFFT GTNPLMMVHE VLELGDGLVI PYYEKIPKLS
     NLNTEECYVY WEIYITTQKS VNKIHDIFIF VDAPSEVTIE EWELNSEEPI PEKLGDLLVK
     RGSLKKEELD KALKEQHKLG EILVKESMLS EHEIKNALKA QTYINKTKTK KIEAAAPAND
     SIRINSNKLD SLIDLVGEIV TIYAQMLQLS HDTNDSKLIS IIERFGLLTE ELRDNSMSMR
     MLPIGSTFSR FRRLVRDLSS ELGKKIELVT EGAETELDKN VIEQLHDPLV HIIRNCIDHG
     IESPTVRKAN GKDETGTIKL SAIHAGASVQ IVIQDDGGGL NREKIRSKGI ARGLIRDGEE
     ILDDDLFNLI FAPGFSTAAS ITNVSGRGVG LDVVKKQIEE LKGSVAITSE EGKYTRITLT
     LPITLAIIEG LLVNIGGDSY VIPLSTVEAC VELKEENKDH KSGKNVITFR EKLVPYIDLR
     TFFEVEGRRR DIEQIVIVNS NSSQIGLLVD NVIGGNQTVI KSLGSMYRHI KEISGAAILG
     DGSVALVFDI EQLVRVVQDF EEISVGN
//
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