ID A0A257KSQ6_9BRAD Unreviewed; 911 AA.
AC A0A257KSQ6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CFE29_10900 {ECO:0000313|EMBL:OYU89580.1};
OS Bradyrhizobiaceae bacterium PARB1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae.
OX NCBI_TaxID=2015576 {ECO:0000313|EMBL:OYU89580.1, ECO:0000313|Proteomes:UP000216768};
RN [1] {ECO:0000313|EMBL:OYU89580.1, ECO:0000313|Proteomes:UP000216768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PARB1 {ECO:0000313|EMBL:OYU89580.1};
RA Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT formosa and its bacterial cohort.";
RL Submitted (JUN-2017) 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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OYU89580.1}.
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DR EMBL; NKIY01000003; OYU89580.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257KSQ6; -.
DR Proteomes; UP000216768; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR CDD; cd00731; CheA_reg; 1.
DR CDD; cd16916; HATPase_CheA-like; 1.
DR CDD; cd00088; HPT; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 3.40.50.2300; -; 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; 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; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
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; IPR001789; Sig_transdc_resp-reg_receiver.
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; PF00072; Response_reg; 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 SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 2.
DR SUPFAM; SSF52172; CheY-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.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:OYU89580.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Transferase {ECO:0000313|EMBL:OYU89580.1}.
FT DOMAIN 1..100
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 243..482
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 484..622
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 788..905
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 193..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 44
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 838
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 911 AA; 98847 MW; 2C148E86DBECD77B CRC64;
MDDLLREFLT ETNESLDTVD NQLVRFEQDP NNAKILDNIF RLVHTIKGTC GFLGLPRLEA
LAHAAETLMG KFRDGMPVTG AAVTLILTTI DRIKDILGQL EATEAEPEGV DEDLIDELHH
MAEKGMEAMN SPAPPIVPEV APAPVVESPP LVVQTLEREL RPGEVSLDEL ERAFRETETE
VLPVVAAPAH AEANTTPAAA PVAETKPAAK PASKPAAKKT AVELEHAEAD KVANQSIRVN
VDTLEHLMTM VSELVLTRNQ LLEISRRHED TEFKVPLQRL STVTAELQDG VMKTRMQPIG
NAWQKLPRIV RDLAGELGKQ IELEMHGADT ELDRQVLDLI KDPLTHMVRN SADHGLETPA
ERAATGKPEQ GTIRLSAYHE GGHILICIAD NGRGLNTERI KAKAIQNGLA TEADIEKMSE
AQIHKFIFAP GFSTAAAVTS VSGRGVGMDV VRTNIDQIGG TIDIKSVAGE GSSVTIKIPL
TLAIVSALIV EAGGDRFAIP QLAVVELVRA RANSEHRIER IKETPVLRLR NKLLPLMHLK
KLLKIDDGSS ADPENGFIVV TQVGNQTFGI VVDGVFHTEE IVVKPMSTKL RHINMFSGNT
ILGDGAVIMI VDPNGIAQEL GAQASNMGEI ADEYAAARAL SAEQLTSLLV FRAGSAQPKA
VPLGLVTRLE EIGVDKIELS NGRYMVQYRD QLMPLVQMEN VTVRSAGTQP ILVFADDGRS
MGLVVDEIVD IVEERLHIEV ASSRDGILGS AVIKGLATEV IDVGHFLPQA FADWFSRKEM
RVSSTAQSVL LVDDSAFFRN MLSPVLKAAG YKVRTATNAH EGLTVLRSGQ EFDVILTDIE
MPDMNGFEFA ETIRADQKHG QTPIIALSAM ISPAAIERGR QAGFHDYVAK FDRPGLIAAL
KEQTADVPQA A
//