ID H8H0W6_DEIGI Unreviewed; 738 AA.
AC H8H0W6;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=DGo_PA0099 {ECO:0000313|EMBL:AFD26985.1};
OS Deinococcus gobiensis (strain DSM 21396 / JCM 16679 / CGMCC 1.7299 / I-0).
OG Plasmid P1 {ECO:0000313|EMBL:AFD26985.1,
OG ECO:0000313|Proteomes:UP000007575}.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=745776 {ECO:0000313|EMBL:AFD26985.1, ECO:0000313|Proteomes:UP000007575};
RN [1] {ECO:0000313|EMBL:AFD26985.1, 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};
RC PLASMID=Plasmid P1 {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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002192; AFD26985.1; -; Genomic_DNA.
DR AlphaFoldDB; H8H0W6; -.
DR KEGG; dgo:DGo_PA0099; -.
DR PATRIC; fig|745776.4.peg.3139; -.
DR HOGENOM; CLU_000445_114_41_0; -.
DR OrthoDB; 51401at2; -.
DR Proteomes; UP000007575; Plasmid P1.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 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; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR42878:SF7; BACTERIOPHYTOCHROME; 1.
DR PANTHER; PTHR42878; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:AFD26985.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Plasmid {ECO:0000313|EMBL:AFD26985.1};
KW Transferase {ECO:0000313|EMBL:AFD26985.1}.
FT DOMAIN 82..134
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 519..733
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 125..163
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 321..348
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 738 AA; 80350 MW; 049F1D48CFE60DD6 CRC64;
MTSAELALTP RQLQAIIDAN GDCIKVLDLD ARLLSMNLGG LQVMEIPDFQ QCQYNLLTAF
WEGEGRAQLD AALDAARAGE TRSFEGAART FAGTPKWWSM TVSPLRDDHG HITHLLSTSR
DITARKQAEA AQAAAQAQLA QHAQTLEQQV QAQTRALEER TAALDAFVSF TEAVGTETDT
HRLAAQAVTA VQAQLRDVSV AYYELDADMA VWRGVVWSED VSPDVVAQMQ GGVPLDAPAF
AETVQRGEPV FIGGWDAEGN ALSEATMYGA AGFIPLLIGT EPRGIFAVGK RGAESWPERD
QAIVRAVARG LGLSLERAAQ AGQLRQQRDD LNRRTQELET LLELTEDLGE MPDPVALVAR
AQMLVLRLLP PGFAAYYEVQ EGRWQLRAQT GESGSAVLQA QMEAGFPVGQ TPSFDQIAQT
GRPAFVDSYD PATDIDPEVA QSVAAHATLP LLIGGQVRGL FNVPLFDSRA WTLADQAILL
TTVRHLGAVL ERVERQVQLV RSNAELQAAN QELEAFTYSV SHDLRTPVRH VEGFSALARR
ELTRQDPVRA ERHLDIVTDA AGRMNMLLDA MLTLSRAGRA VLNLQAVPLG TLVDQAVNDV
TLAFPDRPVA WTIGPLPIVQ GDAATLQQVV RHLLENAVKY SQQEEAIQVQ VWVEDREQEW
AVLVRDNGVG FDPQYASKLF GAFQRLHTQQ EFSGTGIGLA TVKRIVTRHG GRVWAEGTLG
EGATFGFSLP KTAPPPAR
//