ID M0JQC0_HALVA Unreviewed; 1299 AA.
AC M0JQC0;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=C437_05180 {ECO:0000313|EMBL:EMA09865.1};
OS Haloarcula vallismortis ATCC 29715.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=662477 {ECO:0000313|EMBL:EMA09865.1, ECO:0000313|Proteomes:UP000011534};
RN [1] {ECO:0000313|EMBL:EMA09865.1, ECO:0000313|Proteomes:UP000011534}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29715 {ECO:0000313|EMBL:EMA09865.1,
RC ECO:0000313|Proteomes:UP000011534};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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}.
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:EMA09865.1}.
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DR EMBL; AOLQ01000015; EMA09865.1; -; Genomic_DNA.
DR RefSeq; WP_004515835.1; NZ_AOLQ01000015.1.
DR PATRIC; fig|662477.6.peg.986; -.
DR OrthoDB; 230688at2157; -.
DR Proteomes; UP000011534; 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 GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 4.
DR CDD; cd00156; REC; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 1.
DR Gene3D; 3.30.450.40; -; 2.
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; 5.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 4.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 3.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 4.
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; 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); 5.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EMA09865.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 13..129
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 144..214
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 343..394
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 597..631
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 634..686
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 818..887
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 890..942
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1107..1299
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 1299 AA; 144161 MW; 53EE262E3CDEFB36 CRC64;
MSYTGGGTPD AIHVLYINDD GDFAELAQTK LANISSDFEV TTVGTVEAAL ELLGTSTVDC
VVTSYSLPDG TGIDFLNRLQ AEQYELPTIL FTGRGSERIA SEATQAGVSD YIPINTGQNS
FELLARRIRT LVEAARKQVV AERLSDRFQR TLERATDAIY AVDDEWQIEY INEKMARRVD
RDPDAIVGAT IWDEFPSIVG TELEDKYRTA METGEPVSFE QHLGEPFNYW VEVRAFPDND
GLTVFSRETT AERERELELE RSETILQNIH DVVFVLNDEG TIEFANAASK RLISEEGTAQ
LTGKRLKAVV GDRISAADKE RFTEAVDSTF NEIESDGGVT GLYDADLQLD ITADGDRRTF
DVRITPFRSQ KTQQVLVVAR DITEQTEAKR QLERERDALR ELQTIMARSD ASAETRLREL
LELGCQTLGL DIGIVSRIQG NSYTVKSVHA PDSEIESGDQ FALESTYCEE VVGTDAVCSF
ADAVTDGRET HPAYREFELE SYIGVPLVVN GERYGTVNFS SPTTRVAPFG KLERTFVELL
SELVSAEISR GQDRADLQRQ EFLFERVQDI ADIGVWEYFP STGDLDWSDG VRRIHGVGDE
YDPVLGDAVE FYHPDDRETI TGAVERAIED REPYDLDLRI VRTDGEIRDV RAWGERIDGT
QDDEPVLRGV FQDITERKAE ERAHRELAQE YEALLNTSGD AIFMLDVETA GDEPSFEFAR
LSPGYELQTG LTTDEVRGQT PREVFGDDRG AELAANYTRC VEQREPISYQ EELDIAPDAR
FWDTSLAPVI LGDEIVRVVG IARNVTEQVK RERKLETTNQ RLESLIEATP LTVMEIDTDG
TVVRWNDGAE NMFGWSREEV LGEPNPIIPD ERQSEFASHR DRALSGKPIR GKEVRRERKD
GEKLDLLLSV TPITAPDGEI TSVLAVLEDI TEQKKLESKL RSLQATARRL SAAQSSDEIG
DIAVEAAGDI LGFELTGIWE YADQTDELVP LSASAATREL LDELPRLEAG ETLAWEAFEA
SELRQYDDLQ SEASLDAGGT ELKSGLFVPL GEFGLMGVGA PQDQTFSEAD MDLFRILGST
VKAAFTRASR ETELQRQNER LDEFSSVVAH DLRNPLSIAI GFLDIVEETG DLTHIDRIES
AHDRMERLID DLLTLARGES TVTETKQIDL KTMTTEAWGY VDTADATLTV ADTVPTVAGD
ASRLTQLFEN LFRNAIEHGG KDVTVTVGQL EDGDGFYVAD DGEGIPPAKR DEVLEHGVTS
TNGGTGFGLS IVEDIAKAHG WTIRVTAGAA GGARFEFCY
//
