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Database: UniProt
Entry: A0A0G0LIY6_9BACT
LinkDB: A0A0G0LIY6_9BACT
Original site: A0A0G0LIY6_9BACT 
ID   A0A0G0LIY6_9BACT        Unreviewed;       559 AA.
AC   A0A0G0LIY6;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   13-SEP-2023, entry version 30.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=UT09_C0008G0010 {ECO:0000313|EMBL:KKQ87905.1};
OS   Parcubacteria group bacterium GW2011_GWF2_38_8.
OC   Bacteria.
OX   NCBI_TaxID=1618961 {ECO:0000313|EMBL:KKQ87905.1, ECO:0000313|Proteomes:UP000034262};
RN   [1] {ECO:0000313|EMBL:KKQ87905.1, ECO:0000313|Proteomes:UP000034262}
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:KKQ87905.1}.
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DR   EMBL; LBVM01000008; KKQ87905.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0LIY6; -.
DR   Proteomes; UP000034262; 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; 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; 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; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF13596; PAS_10; 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; 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   Kinase {ECO:0000313|EMBL:KKQ87905.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000313|EMBL:KKQ87905.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        15..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        49..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        131..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        172..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          277..327
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          340..552
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   559 AA;  63465 MW;  C78C25C75E0897C0 CRC64;
     MFKEGLMRME LVERIYWLIL LRWIAVLGLF ITTYIASGVF DVVTWVAPLY IIGIIIGLSN
     AGFMFFIKVL RKKTFSSVQK HAGIQIMLDL LFLTCLIYFA GGIENPFIFY FLFHVIIAGI
     LLEKKYSYMQ ATFGVCIFAL LISLEYYAVI PHQPLKIFST FAFGKELWRS EVYILGIFFA
     LASTIFISVY FVTSIMDRLR KSRDDVLFEI RSTIENMAEG VIFIDSNDKI TMCNKEIEKT
     WKVKREEIIN KSVKDGQTPY LGGVASRITE KFRNGIVTSQ HQEIRIKGGF LYNTYTAVSD
     HNGKYWGTVL TSHDITERKR LEQQLLHSER LATIGEMSAK VAHEIRNPLS SISLNTELLY
     DEICNYNGAK NSEAENLIKS ILNEVDSLTE ISDEYLRFAR FPKLEIRPAN INNVLIELTK
     FFNKEMAQRG ISLKENYASN LPQILLDTNQ IKQAFLNILK NSFESMPEGG KLSISTRLKD
     ENVEINVTDT GSGINRSDIR RVFDPFYSTK VKGTGLGLAL AMKTVEGHGG DIICKSTITK
     GTTMIVSFPV KGCGDEIIE
//
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