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Database: UniProt
Entry: B2UD15_RALPJ
LinkDB: B2UD15_RALPJ
Original site: B2UD15_RALPJ 
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
//
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