ID H8GWE2_DEIGI Unreviewed; 1094 AA.
AC H8GWE2;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=DGo_CA1765 {ECO:0000313|EMBL:AFD25692.1};
OS Deinococcus gobiensis (strain DSM 21396 / JCM 16679 / CGMCC 1.7299 / I-0).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=745776 {ECO:0000313|EMBL:AFD25692.1, ECO:0000313|Proteomes:UP000007575};
RN [1] {ECO:0000313|EMBL:AFD25692.1, ECO:0000313|Proteomes:UP000007575}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21396 / JCM 16679 / CGMCC 1.7299 / I-0
RC {ECO:0000313|Proteomes:UP000007575};
RX PubMed=22470573; DOI=10.1371/journal.pone.0034458;
RA Yuan M., Chen M., Zhang W., Lu W., Wang J., Yang M., Zhao P., Tang R.,
RA Li X., Hao Y., Zhou Z., Zhan Y., Yu H., Teng C., Yan Y., Ping S., Wang Y.,
RA Lin M.;
RT "Genome sequence and transcriptome analysis of the radioresistant bacterium
RT Deinococcus gobiensis: insights into the extreme environmental
RT adaptations.";
RL PLoS ONE 7:E34458-E34458(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};
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DR EMBL; CP002191; AFD25692.1; -; Genomic_DNA.
DR AlphaFoldDB; H8GWE2; -.
DR STRING; 745776.DGo_CA1765; -.
DR KEGG; dgo:DGo_CA1765; -.
DR PATRIC; fig|745776.4.peg.1813; -.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG3614; Bacteria.
DR eggNOG; COG3829; Bacteria.
DR eggNOG; COG4251; Bacteria.
DR HOGENOM; CLU_275541_0_0_0; -.
DR Proteomes; UP000007575; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 3.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.350; CHASE domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
DR InterPro; IPR006189; CHASE_dom.
DR InterPro; IPR042240; CHASE_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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR42878:SF7; BACTERIOPHYTOCHROME; 1.
DR PANTHER; PTHR42878; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF03924; CHASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM01079; CHASE; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 2.
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 SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50839; CHASE; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:AFD25692.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:AFD25692.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 35..215
FT /note="CHASE"
FT /evidence="ECO:0000259|PROSITE:PS50839"
FT DOMAIN 322..367
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 385..437
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 504..564
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 565..601
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 635..687
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 874..1088
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 298..325
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 829..867
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1094 AA; 120253 MW; D7E2A786283D5767 CRC64;
MRFEREVSAH ASALRQRVSD FDKLLQATRA FWLTGNTDVT PAAFARFSEE LNLRRRYPDV
QALGYAAWVP SGDTAPLETL LGSLGQSGFR VRPQTTSAGP RAPVVLIAPD TAQNEPVLGF
DLYSEAHRRS ALTRAQRSGE FQTTLPITLA TPDSAGRPLR GLLLVLPVWR PDLVGTGGTG
GTGQAAGQSR DQSSAGVLTG FIYVAVRADI FLASLGSAYR EPGIRSRLVM GGQPLVTGAA
PTGEFRMQER ATLAGLDWTT TYAAPASFGR DIFGFSPVLI FLMGMLLAGL SFRLTQAQVR
AREQAEAANR DLREAQVRQA RAYAELEAIF QSMQDAAAFT DGQGLVRTVN RALAQQFGYG
DTELLGQPLS ALHLDRRLDK RSTFQSVTTP YARRDGSRFY GEAQRTEVRS PAGELLGLLE
VIRDVSERVG AEQALQAAGK RSQAVLDAIP HVVWVSEPGG ALTYENVQHR RRLGTDSLRS
RVHPQDRAAY EQMWRDAYAL QAPSESEVRL RVAGPGRAGP QNLRDRWFEL RVAPLLNDQG
EVREWVASAT DIHDRLLAER LAQRNEERYR GVIEGMPQIV WLTDPQGVPT YFNRRWEEYV
GAGRAPQGLL PTLHPDDRSD YQRRWMAAIR AGQAFEAEHR LLGEDGSYRT FVTRGLPVRD
AAGQIIEWVG TSTDVDDSVY AENAARLLAD VSEELTARVN DPLAARADKY RTVMNLVTDR
QMVAAGMWTL PALDLLVSSR TGTDWGAPPL MDAVRRVAGR AAEREDPEYL TDEALLSAAG
VAGLVLCPLT GLDGTLRGVL GLAYRHALRD RDHELVQELC KRLSTALDND ALRERAVAAQ
RELRALNLSL EERVHRRTLE LEEANRELEA FSYSVSHDLR TPLRHILGFS EMLGKDAGAA
LSPKGQRYLT VISDAAGRMS GLIDSLLEFS RMGRTPLRQT PVALGELVRG AWANLDPDRQ
GRQVTLDLGE LPTVPGDAAL LDLVFQNLLS NAIKYSRGRP EARVTVRAHE APDGVRVTVS
DNGVGFDPKY ADKLFGVFQR LHRAEDFEGT GIGLANVRRI VTRHGGTVGA ESLPGEGATF
WITLPLAPRS QETR
//
