ID A0A257EUR6_9RHOB Unreviewed; 402 AA.
AC A0A257EUR6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CFE34_15205 {ECO:0000313|EMBL:OYU17534.1};
OS Rhodobacteraceae bacterium PARR1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=2015578 {ECO:0000313|EMBL:OYU17534.1, ECO:0000313|Proteomes:UP000216502};
RN [1] {ECO:0000313|EMBL:OYU17534.1, ECO:0000313|Proteomes:UP000216502}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PARR1 {ECO:0000313|EMBL:OYU17534.1};
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:OYU17534.1}.
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DR EMBL; NKIT01000112; OYU17534.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257EUR6; -.
DR Proteomes; UP000216502; 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 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; 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; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
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 PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00260; CheW; 1.
DR SMART; SM01231; H-kinase_dim; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000216502}.
FT DOMAIN 58..261
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 263..402
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
SQ SEQUENCE 402 AA; 43262 MW; A376C1B1E3A10337 CRC64;
MSAPSPETNA PDSGLMRVSS DKISRLMDLV GELSLSVSET VQSPDLSGLV LTNFDAAVHR
LNMIVREVQD AATELRLVPV DDVFRRLRRM VRELERQTGK SIDMLIVGGD TAIDKLVADK
LYDPLLHVVR NSADHGLETP EDREKAGKSS QGRITLSAAQ VGSEVQIVVA DDGRGLSRDR
ILQKAREKGF FGPDEEPEPS ALWRVIFEPG FSTAETVSNL SGRGVGMDVL NSTMTALRGR
IGVDSTAGQG TRVSLHIPVS LAFLDCIILR LGVQLFAVPI DVVSEIAKPA PGDLLDISAG
DGSEMFRLRG NYIPVCRLDR FYGDMTSAMQ STNPDSVLVV FNTSNGSIAV PVDEILDRQQ
VVMKPLIGRL AKVRASWGCA LLGTGEVALV LDCERLGAGV SA
//
