ID A0A257FU46_9BURK Unreviewed; 772 AA.
AC A0A257FU46;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CFE41_00535 {ECO:0000313|EMBL:OYU29584.1};
OS Burkholderiales bacterium PBB2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales.
OX NCBI_TaxID=2015564 {ECO:0000313|EMBL:OYU29584.1, ECO:0000313|Proteomes:UP000215624};
RN [1] {ECO:0000313|EMBL:OYU29584.1, ECO:0000313|Proteomes:UP000215624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBB2 {ECO:0000313|EMBL:OYU29584.1};
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:OYU29584.1}.
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DR EMBL; NKIM01000001; OYU29584.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257FU46; -.
DR Proteomes; UP000215624; 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; cd16916; HATPase_CheA-like; 1.
DR CDD; cd00088; HPT; 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; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
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 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; 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 Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000215624}.
FT DOMAIN 5..109
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 391..600
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 602..750
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 300..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 52
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 772 AA; 83014 MW; C06F64791A4D1DB2 CRC64;
MSDDDAEILA VARAGFLDEA LDMLRQFEQS LLVLESDPGD HESLNSAFRA AHTIKGTAGM
FGCEAVVVFT HEAETLLEAL RAGKRALDEP VVAALLESRD QIEALLDEVR SGAQDPEVQA
RGTALAARLR ALLGQPVASS PAAAPIAQAD APASAPSQEA ATGSPSPCWH LSLRFKQDAL
RNGLDPLSFL RYLATLGQVR AIRSLVDEIP ALDALDAEAC HLGFELSFDS EASRKEIEDV
FEFAVDDSDV QILAPGAAAA EFEDLASHRC GDDAQARAAL FEVWRDLGLR FALRLEPPAL
EPAPDAETTP AAAPVPHIER RATEGASDTR GRDRRSGIGE RREGGRDRRA GDDTRFVRVR
ADKLDRLIDL IGELVIAGSG AQMIAHLEGN EALVEANSRV MDLVQETRDG TLALRMVPIG
ETFARFQRVV RDISKQLGKE VELVVTGGDA ELDKSMVDAI ADPLMHLVRN SMDHGLEAPA
EREAAGKGAT GRLSLNAFHE AGSIVIEVSD DGRGLARERI LNKAIERELI QEGQVLSDHE
VWQLIFLPGF STAEAVTDLS GRGVGMDVVK RSIESLRGNI TLSSQVGRGT LTQIRLPLTL
AMIDGFLTLV GGVNYVLPLA AVAECIDVPA ECEREAERGE HRVSGTFNLR GEVLPWLDLA
RFYGMTPQTH GAEPSAASSA RQRRSVVVVR DGQTRLGLIV DRLMGEHQTV IKPLSGIFQH
LKALAGSTIL GSGEVALLLD VPGLTAAAIR GGQRDLQLRR PSHPEQKAAT HS
//
