ID G2EB46_9FLAO Unreviewed; 864 AA.
AC G2EB46;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BZARG_729 {ECO:0000313|EMBL:EGV44471.1};
OS Bizionia argentinensis JUB59.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Bizionia.
OX NCBI_TaxID=1046627 {ECO:0000313|EMBL:EGV44471.1, ECO:0000313|Proteomes:UP000003730};
RN [1] {ECO:0000313|EMBL:EGV44471.1, ECO:0000313|Proteomes:UP000003730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JUB59 {ECO:0000313|EMBL:EGV44471.1,
RC ECO:0000313|Proteomes:UP000003730};
RX PubMed=18842857; DOI=10.1099/ijs.0.65599-0;
RA Bercovich A., Vazquez S.C., Yankilevich P., Coria S.H., Foti M.,
RA Hernandez E., Vidal A., Ruberto L., Melo C., Marenssi S., Criscuolo M.,
RA Memoli M., Arguelles M., Mac Cormack W.P.;
RT "Bizionia argentinensis sp. nov., isolated from surface marine water in
RT Antarctica.";
RL Int. J. Syst. Evol. Microbiol. 58:2363-2367(2008).
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:EGV44471.1}.
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DR EMBL; AFXZ01000009; EGV44471.1; -; Genomic_DNA.
DR RefSeq; WP_008635740.1; NZ_AFXZ01000009.1.
DR AlphaFoldDB; G2EB46; -.
DR STRING; 1046627.BZARG_729; -.
DR PATRIC; fig|1046627.3.peg.760; -.
DR eggNOG; COG4251; Bacteria.
DR OrthoDB; 9124519at2; -.
DR Proteomes; UP000003730; 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; 2.
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; 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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
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; 1.
DR Pfam; PF13426; PAS_9; 2.
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); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000003730};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 186..207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 639..864
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 864 AA; 98957 MW; 33F487936FE81FE9 CRC64;
MDFKRVYTSS KTYYILTIVA FAILAFTITI AYKQVLRMQS SAEMVSHSLH VYNGISLLTA
HFTQADSEEL RDELLKPGDS NLAFETYREE GRVSIDSLQL LISDNPSQIE RLDRIKVLLD
DLYEQLQDLN DVDYEADNTI LQYRGAQKTV ISITLYQLRS IKEKMIVEEQ RLMEQRKKAY
ASNKTLAPKI LLFLAFIALM VFVLSFIRIY RNKARIRESE NFLKSVLATT DNVVNYYEPI
FNEKNEIIDF KVVFANECNR DYFGLEPDKM LGRSVIKLFP HLKGSVDFEK LKTSYLNSEK
VKFDSKITMN DSVMWFHSFV TPLSEGVLIT ARNSSVEEEA KNIQLNLKKR LENQNLKLLD
SRALLANIFK SISHVVMHFK SIRNTEGAIV DFQILFVNDR INPITGQIPE EIKNKNVSEI
YPDIFENGVF EHLVNTIEVN KHTEYEVPFE KNSKTHWFNA TAIKLGDGVT VTIRETTGEK
EKSDELRKLN DQLVIRNSIL TDAESIAKIG SFLWYMDSDT TEISENFYRL LGYEPNEFKS
SLKKFRDFIH QDDLALYDLK AEAYFKGETS EEYTYRIMTK TGAVKYVKTN GQFLNRNGKQ
VMIGVVQDVT QSIHAAEEIR KSNLDLKQSN AELESFNRVA SHDLQEPLRK IQLFISRIED
VDGGTFSVKS QNYFEKVKNG AERMQGLIQN LLSYSRIDNS KTDLELIDLN HVLDKVKDDL
VASINDTGAE ITSDKLPNIN GVFFQMEQLF ANLIANALKY KNAATSPQIQ IQVQKVAGTD
LPDHLLSTSK QYHKITFIDN GIGFDSKHAN KIFEVFQRLH QKTEYSGTGI GLAICKKIVE
NHNGFIFATG ELGKGAQFII YLPA
//
