ID A0A1H1IXF1_9BURK Unreviewed; 1645 AA.
AC A0A1H1IXF1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05443245_5778 {ECO:0000313|EMBL:SDR41948.1};
OS Paraburkholderia fungorum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=134537 {ECO:0000313|EMBL:SDR41948.1, ECO:0000313|Proteomes:UP000183487};
RN [1] {ECO:0000313|Proteomes:UP000183487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GAS106B {ECO:0000313|Proteomes:UP000183487};
RA Varghese N.;
RL Submitted (OCT-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};
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DR EMBL; FNKP01000002; SDR41948.1; -; Genomic_DNA.
DR Proteomes; UP000183487; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 2.
DR CDD; cd00130; PAS; 1.
DR CDD; cd18161; REC_hyHK_blue-like; 1.
DR Gene3D; 1.10.287.130; -; 2.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 3.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 2.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 2.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF00072; Response_reg; 3.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 2.
DR SMART; SM00388; HisKA; 2.
DR SMART; SM00448; REC; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 2.
DR SUPFAM; SSF52172; CheY-like; 3.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 2.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 2.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 3.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 369..597
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 658..774
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 994..1046
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1132..1355
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1375..1491
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1530..1644
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 707
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1425
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1579
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1645 AA; 179806 MW; 086C4A5294FCA0E1 CRC64;
MKEPDRFLPD APPAEVAAPS FLAGGGELGA LIRAYDWSRT ELGDPDTWPQ GLKIAIRIML
TSRQPIWIGW GKELLYFYND PYKSIIGGKH PVALGQPTHV VWREIWSDIE PLLNTALAGA
EGIFVEQKLL IMERNGFPEE TYYTFSYSPI PGDDGEPGGI ICANSDDTAR VVGERQLALL
KELAAASPDG RDWREACQLS AAALRTNPQD LPFALLYAGA PGSDTVTLVG ASGIVPGQPG
APESMRLDGD GNDAPSWPVA DVVRIQAPQM VRGLIERFGA ALPGGPWHLA PEQAVILPVS
AGSETAHTVV LVAGLNPCRL FNDEYRSFLN LTAGQIGAAI GYAQAYEEER RRAEALAEID
RAKTTFFSNI SHEFRTPLTL MLGPLEELLA RPPLPVSMDN DAQHANPDDR ALIEITHRNG
LRLLKLVNAL LDFSRIEAGR MQIHPQPTDI ASFTAELASL FESAIQAAGL RLELQIPSRP
VIARLDREMW EKVVMNLLSN AYKFTFFGTI RVAVQATEDG GVEVSVADSG IGIAQEEVPR
LFERFHRVAG APGRSVEGSG IGLAMVQELV KLHGGTVRVD SELGKGACFT VALPRVAMLP
PTGDEAVRAA MSPNARTYVD AALRWSPENE ILAEDVPQNP TVTAGSTSSG HASATPAHLL
VVDDNADLRE YMSRILRAAG YDVHLATDGE AALAAARADP PDLVLSDVMM PRLDGFGLLR
ELRADPVLRE TPVVMLSARA GEEARVDGIE QGADDYLTKP FSSRELLARV AGNLQLARLR
RETEMKLREE SRTLEILNRV GSTVAAELDL KRAVQIVTDA ATELTGAAFG SFFYNVLDEQ
GGSYMLYTLS GVPQDTFEKF PMPRNTGVFA PTFGGEGIVR SDDITKDPRY GHNAPHRGMP
EGHLKVRSYL AAPVQSRNGE VVGGLFFGHP ESGVFTERAE RIVAGIAAQA AIAIDNARLY
EAAQREIAER TRAQNALRDL NETLERRVIE AVTDRDRLWE LSEDLLVVAD IEGRLQRVSP
SWSSMLGHNL HWLKSRSYVD LVHPDDIGIV GMHLAELRRT GVPVRYENRF RRIDGTWRWV
AWTLALDPDT ERIHGVGRDV TADKETTEAL YHAEEALRMA QKMEAIGKLT GGVAHDFNNL
LQVIGGNLQL LAKDVAGSEK PEQRVRNALA GVARGANLAS QLLAFGRRQP LAPKVVNLGR
FVRGLDDMLR RALGDGVEIE TIVSGGLWNT LVDPFQVENA LLNLAINSRD AMNGHGRLTI
EAGNAALDDA YAKRNAEVTP GQYVMLAVTD TGAGMSPEVR ERVFEPFFTT KPEGQGTGLG
LSMVYGFVKQ SGGHVKIYSE RGHGTTIRVY LPRVREEEDL ETNIDAGPAK GGRETILVAE
DDEEVRTTVV EMLSDLGYRV LKAKDAQSAL AIVESGVPID ILFTDVVMPG PLRSTELARK
ARERLPSIAV LFTSGYTDNA IVHSGRLDEG IELLSKPYTH EALARKVRYV LQTQNPQAVE
LAELEQERLQ IDPPVTSASA DSFTPEVRMR ILLVEDDELI RVSTAELLRT FDFDILEAEG
EEDAKRILSE HAINVMLTDV GLAGKSGVDL AMDVCRERPD LRVIFLTGYD LVLTPEQREV
LPHAISLRKP YELTHLIDAL NAPQS
//
