ID A0A0G1VEX6_9BACT Unreviewed; 677 AA.
AC A0A0G1VEX6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=UY35_C0003G0047 {ECO:0000313|EMBL:KKW04870.1};
OS Candidatus Saccharibacteria bacterium GW2011_GWC2_48_9.
OC Bacteria; Candidatus Saccharibacteria.
OX NCBI_TaxID=1619071 {ECO:0000313|EMBL:KKW04870.1, ECO:0000313|Proteomes:UP000034790};
RN [1] {ECO:0000313|EMBL:KKW04870.1, ECO:0000313|Proteomes:UP000034790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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: 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:KKW04870.1}.
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DR EMBL; LCPR01000003; KKW04870.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1VEX6; -.
DR STRING; 1619071.UY35_C0003G0047; -.
DR Proteomes; UP000034790; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 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; 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; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 2.
DR Pfam; PF08448; PAS_4; 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; 3.
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); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:KKW04870.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:KKW04870.1}.
FT DOMAIN 220..272
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 273..343
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 346..399
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 463..677
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 394..456
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 677 AA; 77487 MW; 208211DDEA642B50 CRC64;
MPETLDYASI FNILPEQYVV FDPKDRDFVM VAASNEYLHI TGKRRKDVIG KKLFDVFPDT
SELAVKTGQG ELSKSLEAVL RTHEPDSTGL IRYDLADKTG DMQVRFWRAT HYPIIKGGKC
VAIIQSTADV TELVKSNEQL KLANLKLEEA MVTGLIGSWS WDIQKDVVTA DKGLANLFGV
SQSKALEGLP LKTFIDSIYK EDRTHVSALI EETLKNGKDF ESEYRTIDSE GNIRWVIARG
RVERNAEGAA VQFPGVMIDI SSRKHAEEKL KDSEERLRFM ADTMPQLVWI TRPDGYHEYY
NRHWYEYTGT QEGDTDGEGW NNLFHADDQA EARKTWLKSL KTGEPYEMKY RLYNAKTNQY
RWVIGRALPY KNDKNEIVKW YGTCTDIDDS IKEIEKRKKL ETQLQLEKER LESRVAERTS
QLKLTNEGLR DEIKKRQDVE QKLRQYGDEL KRSNKELEEF AYVSSHDLQE PLRKIQAFGD
LLVSEYSEGL GDGNEYLSRI QSSASRMSKL IEDLLAFSRV TTKPAVTSNV DLNEVLADTT
ADIEERIKRE HGKVVIKSTL PVVCADETHM RQLFQNVISN ALKFHAPDRD PVIEIDYTSD
DKYHKISVKD NGIGIDDKYQ QKIFAVFQRL HAKQAFEGTG IGLAVCKKIV ERYNGNIEVT
SKLNKGTIFT VNLPKGD
//
