ID A0A1G7LTR1_9EURY Unreviewed; 654 AA.
AC A0A1G7LTR1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05216218_10722 {ECO:0000313|EMBL:SDF52907.1};
OS Halorientalis regularis.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halorientalis.
OX NCBI_TaxID=660518 {ECO:0000313|EMBL:SDF52907.1, ECO:0000313|Proteomes:UP000199076};
RN [1] {ECO:0000313|EMBL:SDF52907.1, ECO:0000313|Proteomes:UP000199076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBRC-M 10760 {ECO:0000313|EMBL:SDF52907.1,
RC ECO:0000313|Proteomes:UP000199076};
RA de Groot N.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; FNBK01000007; SDF52907.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7LTR1; -.
DR STRING; 660518.SAMN05216218_10722; -.
DR OrthoDB; 8127at2157; -.
DR Proteomes; UP000199076; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd14686; bZIP; 1.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
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; IPR001357; BRCT_dom.
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; IPR031621; HisKA_7TM.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF16927; HisKA_7TM; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 39..63
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 69..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 102..125
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 145..166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 178..199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 236..308
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 258..290
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 399..595
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 589..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 362..396
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 629..643
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 654 AA; 71443 MW; 21CEAAEA3965342C CRC64;
MEVQVTPYTL PLGFAVVIAT VGAVIAWRQR KGRTEIWAMG VQISLALWSL FTLLTVSTVS
LFWKRLWFAL FLPTIPLLVV TAWLFTVHFV GRRDWLTRPR VIALLAFPVV TLAFTLTGGI
HGLFLVDVCV DRSGSFALLT YEFGVGVYAM GAVAYSIAIG YNALLARRML RSRNVYRQIS
AVVFVATLAI GVVTVLSLVD LSPFPHFMLV PFVYLVVGVV LLLGTGSVTF VRMVPIDRVL
AVVGSRFDST VPLARDFVLE AVDNGIIVVD DEDRIVDINS TAKRMLGLDQ PVGQHLAAVV
RPEWVLECGE VGPVLYGNEP VHELDDEAWV ETPDGERCYQ VTISALGEGE QARAHVVLLH
DITDRKRRAE QLQEQKETLR SRKQQLEHQN ERLDQFAGIV SHDLRNPLNV TSGYLELFDA
RIEGDDDTVE VEAETVRELA RATDRMEGII DDALTLAREG KAVTETEAVD LAETAETAWE
TVDTAEATLT VDADAVIAAD RGRLRTIFEN LFRNAVEHGR GDVTVTVGAL DRNAVTGFVV
ADDGPGIPDE KKDEVFEHGF TTSDDGTGFG LAIVHDVASA HGWDVTVTDS ETGVTASETS
GGSEDERSES SGGARFEFTG VDRAGGDPRI GGTLDREQDP SPRPEADNQP ATED
//
