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Database: UniProt
Entry: B1T0X6_9BURK
LinkDB: B1T0X6_9BURK
Original site: B1T0X6_9BURK 
ID   B1T0X6_9BURK            Unreviewed;       455 AA.
AC   B1T0X6;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   24-JAN-2024, entry version 74.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=BamMEX5DRAFT_1442 {ECO:0000313|EMBL:EDT42778.1};
OS   Burkholderia ambifaria MEX-5.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=396597 {ECO:0000313|EMBL:EDT42778.1, ECO:0000313|Proteomes:UP000004814};
RN   [1] {ECO:0000313|EMBL:EDT42778.1, ECO:0000313|Proteomes:UP000004814}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MEX-5 {ECO:0000313|EMBL:EDT42778.1,
RC   ECO:0000313|Proteomes:UP000004814};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L.,
RA   Tiedje J., Richardson P.;
RT   "Sequencing of the draft genome and assembly of Burkholderia ambifaria MEX-
RT   5.";
RL   Submitted (MAR-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};
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:EDT42778.1}.
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DR   EMBL; ABLK01000029; EDT42778.1; -; Genomic_DNA.
DR   RefSeq; WP_006757430.1; NZ_ABLK01000029.1.
DR   AlphaFoldDB; B1T0X6; -.
DR   PATRIC; fig|396597.7.peg.6867; -.
DR   Proteomes; UP000004814; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR013727; 2CSK_N.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR   PANTHER; PTHR45436:SF1; SENSOR PROTEIN QSEC; 1.
DR   Pfam; PF08521; 2CSK_N; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EDT42778.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004814};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        163..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          242..455
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   455 AA;  49443 MW;  FD39E76702A01118 CRC64;
     MAHSLRGRLL WWLLLPLAAF VLIAGAMSYD TARRTAALVQ DSALVASART IGEDVEWRNG
     RPAADVPPAA LEIFESPSRD SVFYKVIDGH GRLLAGNPAL EAPARHGVDP TLYATTLDDL
     PLRAAAYDRQ LYDEGQVETV TVVVAKTTRS YDAMVATIWR PQLVRLSLML VLAIVLVYLG
     LTLELRPLMK LKDDVADRGP MELEPIRPER LQHELRPIVD AINQCIARLN THTATQRRFI
     ADAAHQLRTP IAVLDTQIQY AQQRGNGDPD LASVLDSMQR SSRKMADVTD KLLLLAHAEA
     TPPTLLTHRV DLAAVVSSVL EETIVLAQRR DIDLGADLGE RLDVAGSDSL LTALVMNLVD
     NAVRYTQPGG RVTVVARRDG DAVVLDVVDN GPGIPAEARP HVFKRFYRVA ADTEGSGLGL
     AIVREIAQAH GGSVMLAPGP GNRGIVVTVR LPAFD
//
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