ID A4JQQ2_BURVG Unreviewed; 989 AA.
AC A4JQQ2;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Bcep1808_5667 {ECO:0000313|EMBL:ABO58605.1};
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:ABO58605.1, 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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000616; ABO58605.1; -; Genomic_DNA.
DR AlphaFoldDB; A4JQQ2; -.
DR KEGG; bvi:Bcep1808_5667; -.
DR eggNOG; COG3707; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_114_51_4; -.
DR Proteomes; UP000002287; Chromosome 3.
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; 3.
DR CDD; cd17534; REC_DC-like; 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; 3.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 3.
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; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 2.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 2.
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); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ABO58605.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000002287};
KW Transferase {ECO:0000313|EMBL:ABO58605.1}.
FT DOMAIN 5..124
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 136..209
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 214..266
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 349..401
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 402..472
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 476..528
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 546..763
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 786..902
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 59
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 835
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 989 AA; 108608 MW; 8DA2F694209FD36B CRC64;
MTSAQILIVE DDRIVARDIA QQMSRAGYVV VGSTGSGEDA LALVETLAAD SKPDLVLMDV
RLEGELDGID TARRIREARD IPVVFLTAYA DEETIRRATA AEPYGYVLKP FDDMQLRTVV
EMALYKHGAE RRLRESEQRY AITLSSIGDG VLSTDVDGFV TFVNLAGEAL TGWSRSEATG
RRLSEVFSLH DENTHAPIED PMAAVLQTGS DGGLPARTIL RARGGSDLPV ECTGTPMTDE
RGVRQGIVIV FRDVTQKRRA QEAEILRETN ARLEMAMYGS NVGVWEIDMP EGDHKRGFAR
YSNIYEWLGF DTPQARLDYE AYMSVLHPDH RDSTDRAVAS FLESGDGLFE LENRLRHRDG
SDRWVLVRGT ARRDATGKPV RFVGSLVDIT ELKMTEQALR ASEERFRGTF ENAAVGVAHC
DLDGRFLRVN QRSGEIVGWP RDALQQRRLH ELIHADFSVA STERFRLLTE GRLKHYSEEV
PLVRFDGERV WVTLSVALQH DASGQTAHVI VIIQDISERK ALEETVRVAK DAAEAASRAK
DQFLANISHE LRTPLNGILG YAQILQRDAR LDTRQLASVG VIEQSGQHLL TLINDILDFA
RLGAGKLELQ VGEVSLRGFL ETIAEIVAVR AQQKRLVLNY VAAPDLPAVV RVDERRLRQV
LLNLLANAVQ FTDHGEVTLS VSRGAAGRLR FEVRDTGIGV SADRLEAIFQ PFEQAGDHTR
RGGGAGLGLA ISRQLVRMMG GEIEVTSSAG EGSVFGFELD APASAAGPCE RIPRLQADRL
DGARRVILVV DDVPANRALL AEVLGQAGFR VIESSDGRDA LDKAAACAPD LIVLDTVMPL
MGGIETLHHL RRSHTLGATP VIVVSADASE QNARANIDAG ANVFLEKPLN LDRLLGSIAM
LLGLATQQGA GPACEADRPM IIPPREDMAA LHRYALLGSM RDISRHADRL ASSHEKYEPF
AARLRHLAMT YESQALLSLI EHHLNSEGS
//
