ID Q1LG89_CUPMC Unreviewed; 768 AA.
AC Q1LG89;
DT 30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 30-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Rmet_3969 {ECO:0000313|EMBL:ABF10837.1};
OS Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS CH34) (Ralstonia metallidurans).
OG Plasmid megaplasmid CH34 {ECO:0000313|Proteomes:UP000002429}.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=266264 {ECO:0000313|EMBL:ABF10837.1, ECO:0000313|Proteomes:UP000002429};
RN [1] {ECO:0000313|Proteomes:UP000002429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34
RC {ECO:0000313|Proteomes:UP000002429};
RC PLASMID=Plasmid megaplasmid CH34 {ECO:0000313|Proteomes:UP000002429};
RX PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT master survivalist in harsh and anthropogenic environments.";
RL PLoS ONE 5:E10433-E10433(2010).
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; CP000353; ABF10837.1; -; Genomic_DNA.
DR RefSeq; WP_011518476.1; NC_007974.2.
DR AlphaFoldDB; Q1LG89; -.
DR KEGG; rme:Rmet_3969; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR HOGENOM; CLU_000650_2_1_4; -.
DR Proteomes; UP000002429; Plasmid megaplasmid CH34.
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; cd00088; HPT; 1.
DR Gene3D; 3.40.50.2300; -; 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; IPR011006; CheY-like_superfamily.
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 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; 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; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 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:ABF10837.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Plasmid {ECO:0000313|EMBL:ABF10837.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002429};
KW Transferase {ECO:0000313|EMBL:ABF10837.1}.
FT DOMAIN 4..108
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 237..486
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 488..622
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 646..762
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 51
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 695
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 768 AA; 83962 MW; F74825812C2DFE1B CRC64;
MNPEQLRDAS LLDLFALEAD AQADVLNAGL LALERDPTAA VQLEACMRAA HSLKGAARIV
GLEGGVRVAH VMEDCLVAAQ RGGLLLSASH IDALLQGTDL LQRIGHPPDG NANWPELGGK
AEIDAFVARL EALLDGGADV AALAAPTVLP PAAEPAPPEP PLPTVNHPST STVVPAQPQE
YTGSNQERIL RVNAERLDRL LAMAGESMVE THWLRPFGVA IQQARRQQMR VMQALDGVQA
LLDSPDSTVP RLRAALMETR QLLEDSHGQL TQRVEEFDQY DHRQSGLSRR LYDTALSCRM
RPLADGITGY SRMVRDLGRS LGKRVRLELS GEQTQVDRDI LEHLDAPLAH LLRNAVDHGI
EAPDTRRAAG KPEEGRVSLH AWHNAGRLVI EIFDDGAGVD LEALRAAIVR RGLAQADTVA
RLSQAELLEF LLLPGFSMRE TVSEVSGRGV GLDAVQDMVR AVRGSLRLSQ QPGSGLHFHL
ELPLTLSIVR ALLVEISGEA YAFPLGHVLR AVAVRREDIE QTEQHQHFRH DGKPVGLISA
AQVLQRPERG QDGDTVPVVV IGEQDRVYGI AVDRLIGERL LVVQPLAQAL GKIKDIAAGS
LTDDGMPVLI FDVEDMLRSV EKLVSDGRIE RVRHGGEEAT QTRRKRVLVV DDSLTVRELE
RKLLSGRGYD VAVAVDGMDG WNVLRAESFD LVITDVDMPR MDGIELVSRI RGDTRLTHLP
VMIVSYKDRE QDRERGLQAG ADYYLAKGSF HDTALLDAVR DLIGEARS
//
