ID Q2SZS1_BURTA Unreviewed; 1035 AA.
AC Q2SZS1;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 125.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=kdpD {ECO:0000313|EMBL:ABC36846.1};
GN OrderedLocusNames=BTH_I1024 {ECO:0000313|EMBL:ABC36846.1};
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CCUG 48851 /
OS CIP 106301 / E264).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848 {ECO:0000313|EMBL:ABC36846.1, ECO:0000313|Proteomes:UP000001930};
RN [1] {ECO:0000313|EMBL:ABC36846.1, ECO:0000313|Proteomes:UP000001930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264
RC {ECO:0000313|Proteomes:UP000001930};
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(2005).
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; CP000086; ABC36846.1; -; Genomic_DNA.
DR RefSeq; WP_009892254.1; NZ_CP008785.1.
DR AlphaFoldDB; Q2SZS1; -.
DR DNASU; 3848362; -.
DR KEGG; bte:BTH_I1024; -.
DR HOGENOM; CLU_000445_113_2_4; -.
DR Proteomes; UP000001930; Chromosome I.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd01987; USP_OKCHK; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 1.20.120.620; Backbone structure of the membrane domain of e. Coli histidine kinase receptor kdpd; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR038318; KdpD_sf.
DR InterPro; IPR025201; KdpD_TM.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR003852; Sig_transdc_His_kinase_KdpD_N.
DR PANTHER; PTHR45569; SENSOR PROTEIN KDPD; 1.
DR PANTHER; PTHR45569:SF1; SENSOR PROTEIN KDPD; 1.
DR Pfam; PF13493; DUF4118; 1.
DR Pfam; PF13492; GAF_3; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF02702; KdpD; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ABC36846.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABC36846.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 684..908
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 903..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..990
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1035 AA; 111179 MW; A74A7AA42F7D096E CRC64;
MNRPDPDQLL DKIQREEEKQ QRGKLKIFFG ASAGVGKTYA MLLAARARKQ EGVDVVVGIV
ETHGRSETAS LLDGLDVLPL MQIEYRGRTI GEFDLDAALA RKPQLVLVDE LAHSNVPGAR
HLKRWQDVYE LLDAGIDVYT TVNVQHLESL NDVVGAITGI RVWETVPDRV FDVADEVTLV
DLPAEELLSR LREGKVYMAQ QAERAVRNFF RKGNLIALRE LALRRTADRV DAQMREYRAD
RSIQRIWQAR ERLLVCVGPG PEAPTLVRAA ARLAASLKAD WLAVYVETPR LARLPDALRQ
RTLNALKLAA ELGAETATLT GADAVAALIG YAQVRNASKI VAGGSSKTGF LRRFSRPFGE
RLAERAGDVD LMLIRASAGE DARTPLDAGA RAWRDTLSSV VDGRSPPRNY GYAAAICALI
TGVANLLQGH LDLTNLVMLY LLGVVFSAVR LGRGPGVVQS FLSVAAFDYF FVPPRMSFSV
TDTQYLLTFF GMLLTSLVIS HLTSSLTRGA TIAQRRERRT SAMYAMAREL GAALTAEQIV
EIGSRHVSEV FRARVAILLP DSGDKIQQKI ENPDEAVTIT GAALDIDVGQ WVYDQQKPAG
HGTDTLPAAT ALYLPLKAPM RTRGVLAVVT KDPGELEVPE QQRMLDAFAA QIALAVERVH
YVEIARDALV NMESERLRNS LLSAISHDLR TPLTAIVGLS SMLANARGGG SSAREDELVE
SIHDEALRMT GIVTNLLDMA RLQAGSLQLK RQWSLLEETV GAALAACKRV LARHPARVRL
PADLPLLQTD AVLMERLFAN LFENAAKYTP LDTPIEIGAE RIVDDSRPFV RVFVDDHGPG
LPAGMEARIF EKFTRGEKES ATPGIGLGLA ICRAIVDAHG GKIGALNRLG PDGKVEGARF
WFTLPVDTPP PEPGAGDDAP DDEAGEAGAA GAAAGGADEA AAGGPSAGEP PAGAGSRSVF
GDRFAAARAA GEFDAEERTA GERESGGRTA GDRAPDAAAD PARPASGQAA AASSAPRRAE
GAPSPVSNEH PHAHE
//
