ID A4JRB5_BURVG Unreviewed; 745 AA.
AC A4JRB5;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Bcep1808_5890 {ECO:0000313|EMBL:ABO58818.1};
OS Burkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia cepacia
OS (strain R1808)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=269482 {ECO:0000313|EMBL:ABO58818.1, ECO:0000313|Proteomes:UP000002287};
RN [1] {ECO:0000313|Proteomes:UP000002287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G4 / LMG 22486 {ECO:0000313|Proteomes:UP000002287};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 3 of Burkholderia vietnamiensis G4.";
RL Submitted (MAR-2007) 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; CP000616; ABO58818.1; -; Genomic_DNA.
DR AlphaFoldDB; A4JRB5; -.
DR KEGG; bvi:Bcep1808_5890; -.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_114_15_4; -.
DR Proteomes; UP000002287; Chromosome 3.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 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; IPR025847; MEDS_domain.
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 PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF14417; MEDS; 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; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ABO58818.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000002287};
KW Transferase {ECO:0000313|EMBL:ABO58818.1}.
FT DOMAIN 373..589
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 614..730
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 663
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 745 AA; 80806 MW; 86263CDA6B0B12AC CRC64;
MKSASTLLKS APMRTDHFVQ FYDSDEQLVS EVASFSADAL RDGGSAIVIA RPERLAAVYA
RLGTLERANG SAARDRVFMS SAQALLDSCM DGGLPDPARF RRSIGTIVEA AVRAGRPVHA
FGEMVALLCA QHRYAGALRL EALWNELIER YRFSLYCGYP HDAFPSAEQS EMFRHVCALH
RRILPSASLR SDENQLHLTL ALSQQRARAL TDEIRRREDA EQQRNGVLMH APLPIALLSG
AAHRIVLANH RFSALCGRTD IVGRPLTSVL PGGDTAAIAR ALEAARVQGR STTIGEHHDR
PDTDDTDADG ARVYRLHFNP QPLADGLGVI VSAVEVTEHV AAREKLVAAN AERDRLLGEL
RDANQAKDQF LAVLGHELRN PLTPISLALE LIRNRDGQAT PNEIAIIQRQ LDHMVRLIDD
LLDVSRITRG KITLKKEAVR LADIVDRAVE VASPLLEQRR HRLHVDTDPE ARCHGDPVRL
SQVVANLLTN AAKYTLPGGD IAVHAQRGAD GSTLIEVHDN GAGIPPDRLQ SIFEPFYRID
GDNKQAHGGL GIGLALVRSL VNLHGGTVRA DSAGPGRGST FTIVLPEFRP RVGAAAAPQA
EPGIRVAAPG SGRRVMLVDD NEDAASTLAQ WLRDAGHEVA VVHDPVTALA AYRAYRPDVA
ILDIGLPVMD GYELLLRLKA INEVPPCIFL ALTGYGRHSD RERCLATGFA EHFVKPVDPA
ALHLAMSRTG AQGGTPNHDG PQAGR
//
