ID A0A365TED1_9EURY Unreviewed; 780 AA.
AC A0A365TED1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DMJ13_10175 {ECO:0000313|EMBL:RBI62239.1};
OS halophilic archaeon.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales.
OX NCBI_TaxID=29295 {ECO:0000313|EMBL:RBI62239.1, ECO:0000313|Proteomes:UP000252983};
RN [1] {ECO:0000313|EMBL:RBI62239.1, ECO:0000313|Proteomes:UP000252983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H22 {ECO:0000313|EMBL:RBI62239.1,
RC ECO:0000313|Proteomes:UP000252983};
RA Chen S.;
RT "Draft genome sequence of Haloarchaeon sp. H22 isolated from a salt mine.";
RL Submitted (JUL-2018) 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};
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:RBI62239.1}.
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DR EMBL; QNGA01000002; RBI62239.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A365TED1; -.
DR Proteomes; UP000252983; 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; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
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; 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; 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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
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; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:RBI62239.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000252983};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 6..120
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 132..202
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 416..485
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 488..538
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 549..780
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 664..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 246..273
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 524..553
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 674..688
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 780 AA; 85496 MW; 7C8EC5CFF431C385 CRC64;
MTDQIRVLHV DPLSDTGAPP AELDDQSSDM SVVSATGQTA LDALAEGTVD CVVSGYALPE
SDGLVLLERV RDRHPDLPFV LCTTSGDEHV AADAVAAGVT GYVPADVDGD RVGAVLAEVR
RSVTDRSRPR RKFDRYRSIV QAMGDGVYTL DRSGTITAVN DTLEDLSGYD REELVGEHVS
VLLSEGDVAE GERLIRDLLR DDERDVGKLP MTLHTADGAS IPCETRIGLL NDGDRFRGTV
GVLRSIADHE DIKRQLRDEK QKTEELHEIA SEMVACQTAD EIYDLTVEAA EGILEFDICG
VDVVEDGYIV PKAISTGMTD DGYTELEADE GIAGQTIQNG ESYVIDDVRE VEDASPAQSE
YRSLVSVPLG EMGVFQAGSR EVGAFDDDDV ELIELLLSHA VEALRRVHSQ EALRESEEKY
RTLVEQSHDA IYIYRDEEFL FVNQRVCELT GYSRSELYGM KVWDVLHPDE RERVKRIARQ
RIEGNHPPHY EARIVTKAGS VRHMEFSVCV ISYEGETAHL GSARDVTERK ARKEELERQN
ERLEEFASVV SHDLRNPLNV AQGHLELARE RGEDRHFEKT AGALARMEDL IRDLLTLARQ
GQVVSETETV ELEPVVRQAW ATVETEEGSL VVEDSVEVEA DEGRLTELFE NLFRNAVEHA
GPAPTVRVGR LDAASAERPP RADDADGDSS DGSAAVSSES GGDGARQGTK RTEDGFYVAD
DGPGIPPEQR DAVFEHGHTT AADGSGLGLS IVKGIAEAHG WTIAVREGDR GGARFEIRSA
//
