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Database: UniProt
Entry: F0GA14_9BURK
LinkDB: F0GA14_9BURK
Original site: F0GA14_9BURK 
ID   F0GA14_9BURK            Unreviewed;       778 AA.
AC   F0GA14;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE   Flags: Fragment;
GN   ORFNames=B1M_25422 {ECO:0000313|EMBL:EGD01650.1};
OS   Burkholderia sp. TJI49.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=987057 {ECO:0000313|EMBL:EGD01650.1, ECO:0000313|Proteomes:UP000003049};
RN   [1] {ECO:0000313|EMBL:EGD01650.1, ECO:0000313|Proteomes:UP000003049}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TJI49 {ECO:0000313|EMBL:EGD01650.1,
RC   ECO:0000313|Proteomes:UP000003049};
RX   PubMed=23653265; DOI=10.1007/s11274-013-1366-5;
RA   Khan A., Asif H., Studholme D.J., Khan I.A., Azim M.K.;
RT   "Genome characterization of a novel Burkholderia cepacia complex genomovar
RT   isolated from dieback affected mango orchards.";
RL   World J. Microbiol. Biotechnol. 29:2033-2044(2013).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGD01650.1}.
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DR   EMBL; AEXE01001517; EGD01650.1; -; Genomic_DNA.
DR   AlphaFoldDB; F0GA14; -.
DR   PATRIC; fig|987057.7.peg.3998; -.
DR   Proteomes; UP000003049; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; cd17546; REC_hyHK_CKI1_RcsC-like; 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; 1.20.120.160; HPT 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; IPR036641; HPT_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
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; PF01627; Hpt; 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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50894; HPT; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:EGD01650.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:EGD01650.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          199..415
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          552..666
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          684..778
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   MOD_RES         601
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         723
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EGD01650.1"
SQ   SEQUENCE   778 AA;  85741 MW;  0D53758E1A59758B CRC64;
     GFGHMIYLLP LEVQLRALRY ELMLICGAAL VVIVLLCVAY RYWNYRFLSR IYAEASRALD
     TEMLNHLLVH ATPVGLCIVR RENLEIIVAN PIARTVMGLR ITENQLPGEL IGAFEKSLQG
     VQSDADGSRI FQFPFTLSRP KRPPLHIEIT YAPAKLNKQD VFFCAVIDMT SHHQAEILLR
     EAKLTSDAAA KAKVAFFASM SHEIRTPLSS LVGNIELVAR GPLAPEQQAR VQAMQTSARG
     LLQIVNDVLD FSKIDVGELS LMEEWCSVVE LLEKLAQSHA PLAVQQGLMF YTVFDRDIPS
     RLLFDPIRVS QIVNNLLSNA LKFTPSGKIV LRASWGGGVL VLSVTDSGIG IPEELKQRLF
     VPFSQGDSNR LAQARGTGLG LSICARLCEL MKGRIRLDSA VGVGTRITVE LPLKTSEAGQ
     ESERALPYRR PVILCRAQEN LEWLSSLFDP AVTVITAVAN PGEPIDASVH DVLLVTDEYT
     ESEVLEWWRR PGAILWLSRS GPIIPARRED GGVGVSIYSL AGMRSAAALL GTSPQQALES
     GTDRRTSEGK LSVLVVEDNV LNRHLLVDQL GTFGVLAIEA TNGEEALALL AKEPVKAVMT
     DIDMPVMDGF QLLSEMRRLG YRIPVYAVSA SARPEDIAQG LARGFTDYLA KPVPLDVLEK
     VVGDLSAPSR TEADQDRDET VPGVPSVPDK YVPGFLEQAR KDIDEFATLI RERDVSRLRR
     WLHGVAGGLS VLGPSELYEQ CQELRSYVRE SEGWDEEMEA QAQAIRDTLE GMVSALRH
//
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