ID B2UD15_RALPJ Unreviewed; 732 AA.
AC B2UD15;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 24-JAN-2024, entry version 102.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Rpic_0029 {ECO:0000313|EMBL:ACD25194.1};
OS Ralstonia pickettii (strain 12J).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=402626 {ECO:0000313|EMBL:ACD25194.1};
RN [1] {ECO:0000313|EMBL:ACD25194.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=12J {ECO:0000313|EMBL:ACD25194.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT "Complete sequence of chromosome1 of Ralstonia pickettii 12J.";
RL Submitted (MAY-2008) 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; CP001068; ACD25194.1; -; Genomic_DNA.
DR AlphaFoldDB; B2UD15; -.
DR STRING; 402626.Rpic_0029; -.
DR KEGG; rpi:Rpic_0029; -.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_114_51_4; -.
DR OMA; HIDEQAC; -.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00156; REC; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
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; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43065:SF46; C4-DICARBOXYLATE TRANSPORT SENSOR PROTEIN DCTB; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
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; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ACD25194.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:ACD25194.1}.
FT DOMAIN 114..167
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 212..435
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 458..574
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 604..716
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 158..203
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 508
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 653
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 732 AA; 78888 MW; 2A0E462916EA279A CRC64;
MPFLAHHHDC LGWNGEMAQR VLAFDWASTE LGPIQDWSPS LRAAVHMVLA CPVPLVMLWG
RHGYMVYNDA YAVFAGGRHP YLLGCPVELG WPEVADFNRH VMDVCLGGGT LSYRDKELVL
LRNGRPEDVW MDLYYSPLPD DTGRPAGVLA IVVETTERVQ TERERQAAEQ ALRQLTETLE
QRVADALSAR AEVEAQLRQA QKMEAIGNLT GGVAHDFNNV LQVIAGNLQM LSVEAPNNTR
VQHRIAAATR AVQRGATLAA QLLAFARRQQ LSPAVVNPTR LVQGMSEMLH RALGEAIKVE
THLAADLWNV QADRNQLENA LLNLAINARD AMRGGGMLTI AANNVTLDNT QADVRDQLTP
GDYLVFSVTD TGVGMPPEVV EHAFEPFFTT KPDGHGTGLG LSMVFGFVKQ SGGHIAIDST
VGQGTTVQLY FPRCTEAAPD DAVELRDTIV TPMGGRETIL VVEDDTDVRL TAVDMLTQLG
YRVLTAANGQ AALDLMNSGT SIDLLFTDVI MPGPIKGSEL SIRAAQRVPP LPVLLVSGYP
RDEVQHDGRL PPGVTLLGKP YRRDDLARMV RNVLTASRTA QAQAQSASPS AGPAVATDAS
QPPAVLLVED DTASREAMQE VLTTFGLQCV AAVNAEDALA LARTRSVQVL LTDLTLPGQS
GANLARTLLR MQPQLQVLLM SGYGTEAEIG EPIAGARLLG KPIDLMTLQQ ALAPWLGATV
RAADTQNVTN AA
//