ID H1S0Q8_9BURK Unreviewed; 813 AA.
AC H1S0Q8;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=OR16_05999 {ECO:0000313|EMBL:EHP43917.1};
OS Cupriavidus basilensis OR16.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=1127483 {ECO:0000313|EMBL:EHP43917.1, ECO:0000313|Proteomes:UP000005808};
RN [1] {ECO:0000313|EMBL:EHP43917.1, ECO:0000313|Proteomes:UP000005808}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OR16 {ECO:0000313|EMBL:EHP43917.1,
RC ECO:0000313|Proteomes:UP000005808};
RX PubMed=22461549; DOI=10.1128/JB.06752-11;
RA Cserhati M., Kriszt B., Szoboszlay S., Toth A., Szabo I., Tancsics A.,
RA Nagy I., Horvath B., Nagy I., Kukolya J.;
RT "De Novo Genome Project of Cupriavidus basilensis OR16.";
RL J. Bacteriol. 194:2109-2110(2012).
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 -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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:EHP43917.1}.
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DR EMBL; AHJE01000015; EHP43917.1; -; Genomic_DNA.
DR RefSeq; WP_006156976.1; NZ_AHJE01000015.1.
DR AlphaFoldDB; H1S0Q8; -.
DR PATRIC; fig|1127483.3.peg.1198; -.
DR Proteomes; UP000005808; Unassembled WGS sequence.
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; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
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; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
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; 2.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:EHP43917.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:EHP43917.1}.
FT DOMAIN 78..301
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 319..441
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 469..585
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 625..729
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 37..71
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 373
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 518
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 664
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 813 AA; 88081 MW; CE15AFF7066ABCA1 CRC64;
MRFPVRNPAT QEVVGVGAVG IDITEQVEAN HRLTFLSQTL ERRVEERTRE LAQANAELVV
AKQEAESAAH AKASFLANMS HEIRTPMNAV IGMAHLALRT RLDDKQRGYL EKIQHSGQHL
LEIIDDILDL SKIEAGKLEI ERVDFSLERM LRTVSDLVAE RAVAKHLELI VEVAPDVPDS
LRGDPLRLRQ ILINFANNAV KFTHQGEIVI RVERHGAGDS QPRIRLRFEV RDTGIGIDAA
TCSRLFQSFE QADASTTRRY GGSGLGLAIC RRLVELMGGT LGVQSTLGQG SNFWFELDLL
AGKRRPASAT LAPQLAGCRL LVADDHDYAR QVIIAMLRNF GFRVDEAASG RAALAMIAQA
DEAADPYQAV FIDWKMPGLD GIETARHIDA MRLRHPRPRR VMITAHGREE VLREGERSGF
DATLIKPVSA SLLLEATVRT LAPDHDAAPE AAEPHAAALD ATPELPSARV LLVEDNDINR
EVAVHLLQAA GIYPDTAENG AVALNLLQAG AYDLVLMDVQ MPVMDGFEAT RHIREIPAFA
SLPVVAMTAN ALPEDRARCL EAGMNDHIAK PISPPAFYAM LRQWLAVPGG DDAARQAGSR
PAWVDALATS AHLDVSGGLG RVSGRVEVYR QLLDRFASGY ADMPDRIGER LARGDRDGAL
ALAHSLKGLA ANLGAMAISG AAATLEASLQ LPHAPGRPDP VTLLAALRTT FLPLLAILRM
HLPTEPAAMD AGAPDGAGSL ADPDVTPQAV LEILREQLEE GDSAANHTFA RYRDRLARLL
SADACLRLQA QLERYDYLAA LATLATREGG IAP
//
