ID G2EAH8_9FLAO Unreviewed; 926 AA.
AC G2EAH8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 2.
DT 08-NOV-2023, entry version 59.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BZARG_2170 {ECO:0000313|EMBL:EGV44563.2};
OS Bizionia argentinensis JUB59.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Bizionia.
OX NCBI_TaxID=1046627 {ECO:0000313|EMBL:EGV44563.2, ECO:0000313|Proteomes:UP000003730};
RN [1] {ECO:0000313|EMBL:EGV44563.2, ECO:0000313|Proteomes:UP000003730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JUB59 {ECO:0000313|EMBL:EGV44563.2,
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:EGV44563.2}.
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DR EMBL; AFXZ01000005; EGV44563.2; -; Genomic_DNA.
DR RefSeq; WP_040287937.1; NZ_AFXZ01000005.1.
DR AlphaFoldDB; G2EAH8; -.
DR STRING; 1046627.BZARG_2170; -.
DR PATRIC; fig|1046627.3.peg.549; -.
DR eggNOG; COG0642; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR OrthoDB; 9811889at2; -.
DR Proteomes; UP000003730; Unassembled WGS sequence.
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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
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; 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; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
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; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
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; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EGV44563.2};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000003730};
KW Transferase {ECO:0000313|EMBL:EGV44563.2}.
FT DOMAIN 156..226
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 278..348
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 419..641
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 655..776
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 799..917
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 705
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 850
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 926 AA; 106020 MW; CE5C29086C8892C1 CRC64;
MENKHLKYNQ GKKDLISRFK TLSDRYSDSL DFLVHSVAEL TDMALCTVVF FEEGDSFILA
STDDSVLKIW PKDSYDPEQF TDNNNLKFDI PTSALGKIEV KFWKTQFILN SENKPIATLN
IFDDKDRILT KSDERTLKRA ASQITKWIAS KTKEQQLKKI DNLFELSNDL IGITTFEGTF
AKINPTFSKT LGWSHDELMQ TPCINFVHAD DVAKTVAMTQ NLVRGKSVVH FTNRYNTKHN
GVKWIEWTCT PELETRLVFA IGRDVTEYVE REQLLKKSEQ NFRNLFDNIQ GILCIHDLEG
NFLEVNQQGL LSTEYSEEEM RHSTLFNLIV PERHDEVKQY LIAIEKHGKA SGEMSIVKKS
GERAIWYFMS TMDEDAAGNK RILANVQDIT ERLKLDKALK TAKEAAEEAF KVKSEFIANM
SHEIRTPLNG IIGFTELALE TNLDETQRQY LEIINQSGVS LYSIINDILD FSKMESNSMK
LEVDRIEVEQ VISEAFNIVS YGINKKGLEM LMDIDHNIPR YIWADAMRMK QIFVNLLGNA
LKFTEKGEIK LYIKILKDHG SNKMLLRFGV KDTGIGIHEN KQEEIFHAFS QEDGSITKQY
GGTGLGLTIS NKLLALGNSK LQLESVQGKG SNFFFDLELK VEIEELKNGL QDIKKVLIVD
DNENNRKILR RMLEIKDIEV EEADSGLKAL MIMMKESEFD VIIMDYHMPV MDGIETIRKI
KGLQQPSDTR EQPFIVLYSS SDDDHLQKAC DELEVESRLV KPIRMKQMYK MLSELKSLTK
EKNINIQEIP APKKDYNLKI LVAEDNDINM HLTKIFLKNL LPDSTIIEAK NGDEALEKYR
SENPDLVLMD VQMPKLNGLE ATRKIRNIEE HVEVPIIALT AGSLPGEMEK CLQAGMNDFL
AKPILKQNLS NMLSKWLGIP SLKVEK
//