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Database: UniProt
Entry: A0A158KDR3_9BURK
LinkDB: A0A158KDR3_9BURK
Original site: A0A158KDR3_9BURK 
ID   A0A158KDR3_9BURK        Unreviewed;       723 AA.
AC   A0A158KDR3;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=AWB66_06004 {ECO:0000313|EMBL:SAL79227.1};
OS   Caballeronia telluris.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=326475 {ECO:0000313|EMBL:SAL79227.1, ECO:0000313|Proteomes:UP000054717};
RN   [1] {ECO:0000313|EMBL:SAL79227.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 22936 {ECO:0000313|EMBL:SAL79227.1};
RA   Oliw E.H.;
RL   Submitted (JAN-2016) 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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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DR   EMBL; FCNZ02000049; SAL79227.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A158KDR3; -.
DR   STRING; 326475.AWB66_06004; -.
DR   Proteomes; UP000054717; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd12914; PDC1_DGC_like; 1.
DR   CDD; cd12915; PDC2_DGC_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; 3.30.450.20; PAS domain; 2.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:SAL79227.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054717};
KW   Transferase {ECO:0000313|EMBL:SAL79227.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        24..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        307..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          368..585
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          609..722
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
SQ   SEQUENCE   723 AA;  78821 MW;  046D12E5E15685CC CRC64;
     MPNEESPTRK TPALSRSFST TRHVLRLVLV IAVVVPLLSL LGYGYLDYTH RTSNVSEAID
     RLARVEQEHA AEVLHLNREM ALRVLDMLND SDDTTLRAHE PSIHAKLSGI AGDFPQVATI
     SVFGADGKLL ANSSYFPAPM ISIAGKHDFS TARANSRPVQ LSLPLLGKIA EADAFATNIG
     RFGTGGTFLG MVSIALRREY FSKFYQELTG GDPALILGLV RQDGAILVRY PDITASGAPA
     VSPTLQPSIA RALQDNPASG HATTTAAVDG AGRMYSFRRV GDVPLYAVSG YATGVIFEQW
     WRHYALVSTL TLLPCVAVWM LVVFSLHHLT AEQIAWEQWQ KEIRARSNAE ESARQSQRMS
     ALGNLVSNVA HDFNNLLMVV SANIEIARRK GYNNLEHEVL TMKRAMINAE SLTRRLLSVA
     RKQPLKQHEV DFSSWLPAVT AIVQTSVGSQ VRLELHIEPE VWKVYVDPTE LELAIINIAV
     NARDATPTGG RFTIRCCNGN LPANGADVSG DEFVILSFTD DGEGMDQDTV RRAFEPLFTT
     KVRGAGTGLG LAQVLATFEQ MGGTARIESV AGLGTTVRLY LPRYKGPADQ KLHGETSAKR
     PETPVSGSTV LLVEDNAEVA AGIAAVLEVF GCHVHHEMSA DAALHVLDSG KKFDVILTEV
     HMPGRLNGID LVERVRRSWP AQKVALMTGY ADELERAERL DVPILAKPFD MEELSALISG
     RPT
//
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