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
//