ID D8P5A0_RALSL Unreviewed; 675 AA.
AC D8P5A0;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=RCFBP_mp20660 {ECO:0000313|EMBL:CBJ54086.1};
OS Ralstonia solanacearum CFBP2957.
OG Plasmid RCFBPv3_mp {ECO:0000313|EMBL:CBJ54086.1}.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=859656 {ECO:0000313|EMBL:CBJ54086.1};
RN [1] {ECO:0000313|EMBL:CBJ54086.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFBP2957 {ECO:0000313|EMBL:CBJ54086.1};
RC PLASMID=RCFBPv3_mp {ECO:0000313|EMBL:CBJ54086.1};
RX PubMed=20550686; DOI=10.1186/1471-2164-11-379;
RA Remenant B., Coupat-Goutaland B., Guidot A., Cellier G., Wicker E.,
RA Allen C., Fegan M., Pruvost O., Elbaz M., Calteau A., Salvignol G.,
RA Mornico D., Mangenot S., Barbe V., Medigue C., Prior P.;
RT "Genomes of three tomato pathogens within the Ralstonia solanacearum
RT species complex reveal significant evolutionary divergence.";
RL BMC Genomics 11:379-379(2010).
RN [2] {ECO:0000313|EMBL:CBJ54086.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CFBP2957 {ECO:0000313|EMBL:CBJ54086.1};
RC PLASMID=RCFBPv3_mp {ECO:0000313|EMBL:CBJ54086.1};
RA Genoscope - CEA;
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
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; FP885907; CBJ54086.1; -; Genomic_DNA.
DR RefSeq; WP_013208577.1; NZ_CP115953.1.
DR AlphaFoldDB; D8P5A0; -.
DR GeneID; 69783805; -.
DR PATRIC; fig|859656.5.peg.4471; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.20.120.620; Backbone structure of the membrane domain of e. Coli histidine kinase receptor kdpd; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
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; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR038318; KdpD_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:CBJ54086.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Plasmid {ECO:0000313|EMBL:CBJ54086.1};
KW Transferase {ECO:0000313|EMBL:CBJ54086.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 66..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 90..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 120..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 227..279
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 304..521
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 547..666
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 270..300
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 600
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 675 AA; 72810 MW; 9A0500C497D0A66C CRC64;
MRPIVKSLLR PSSRACAAHR AQDTELFGNR PPGEAPPIRP SAWLVAVGAS VVGTFARLML
ESAAGIRLPF YLAFPVVTVA AWYGGFWPGV LAIVCYAALF AGLVALQISS LAQPLLPTQL
TVFALGTLLI CVLCEQLRRA RAGAERRARA ETQQRVSQQR LLAALQASPI SLYDVDNTMH
FTWVHNPVFG LQPHELLGRT VREVFGRRAA SRLTEAGQRV IATGSPTRVE FAFRRRHTQR
VVYDVVVMPL RDDTGEIIGL TNAVIDITEH RQAEARRTQL LEAESRAREE AERASRLKDD
FLATVSHELR TPLNAVLGWA QLLAMRPYDE AMFRRGLAAI ERSARTQVHL IDDLLDMSAI
LSGKVPLEIG PVDLADVLER ARETIEPMAR EKQITIDTEY PPVPLLQGDA GRLKQVFWNL
LANAVKFTPE GGHIRVSVHA SPEGLVATVR DTGIGIEPTF LPHVFDRFQQ ADLSSTRRHG
GLGLGLAIAK QLVELHHGRI TATSNGTNLG TTMTVTLPLN APPSNEQAGR APSLVTGTAA
PALDGLRVLA VDDNAESLGV IALMLERYGA EVVTVSSGAA ALDALARAAG SAPFDALVSD
LAMPGMDGMQ LLRAIRARGL TELPAIAVTA FADPIRLKAA KEAGYQSVIT KPIFPGELGN
VLAASVRRAT GPQDA
//
