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Database: UniProt
Entry: A0A117SDG8_9FLAO
LinkDB: A0A117SDG8_9FLAO
Original site: A0A117SDG8_9FLAO 
ID   A0A117SDG8_9FLAO        Unreviewed;       601 AA.
AC   A0A117SDG8;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   13-SEP-2023, entry version 24.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=APF83_11990 {ECO:0000313|EMBL:KUO65495.1};
OS   Lutibacter sp. BRH_c52.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Lutibacter.
OX   NCBI_TaxID=1734397 {ECO:0000313|EMBL:KUO65495.1, ECO:0000313|Proteomes:UP000054346};
RN   [1] {ECO:0000313|EMBL:KUO65495.1, ECO:0000313|Proteomes:UP000054346}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c52 {ECO:0000313|EMBL:KUO65495.1};
RA   Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (OCT-2015) 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};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:KUO65495.1}.
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DR   EMBL; LOEY01000061; KUO65495.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A117SDG8; -.
DR   Proteomes; UP000054346; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; 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   InterPro; IPR011620; Sig_transdc_His_kinase_LytS_TM.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR   PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF07694; 5TM-5TMR_LYT; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 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; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        40..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        71..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        99..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        133..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          205..259
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          280..332
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          371..600
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          320..367
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   601 AA;  67980 MW;  D29714D5B345EBBB CRC64;
     MKESILIGLL QNAALLIALS MLYQNFWIKN EGPKSISEKF IAGLVLACIG IILMSTPWMM
     VPGISFDMRS VLLSISGLFF GPIPTIITML AAGAVRLSIG GAGLWMGLAV ILFSGSIGLL
     WRKFRPNWKS NNYYLELLAM GLIVHIIMSV CSVFLPSDMM FPTLKTIAIP IIFIYTPVTM
     LLGILMVNQY KNWKNELAQL KLQEYERRFT QILESGNVLS LLLNNDGTIN FCNDYLLRIT
     GYEREEVLGK NWFDIFIPDT ERPKLKQLFS VGMDIKEFSK NYENSILAKT GEELIISWYN
     IVLRSDNNEV LGTASIGVNI TESKRHEKNL KEKNAEIEAQ NEEYRKINQE LQKAKEQAEQ
     SDRLKSAFLA NMSHEIRTPM NSILGFSDLL KESKLTSDKR TKYISVIEHS GKRMLNIIDD
     IVLISKIESG NIEIQNFKCN INEQIVSIYD SFKEEIAQKG IDFSYKNALL DNEAIINTDG
     EKLYAVLVNL IKNAIKFTHK GSVEFGYILK KDSAPAELEF FVKDTGVGVS QEQKDLIFER
     FRQGSEALNR NYEGAGLGLT ISKAFVEMLG GRIWVESEDE NCALGENGTT IFYFTTPYDI
     K
//
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