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Database: UniProt
Entry: A0A1D8P8T7_9FLAO
LinkDB: A0A1D8P8T7_9FLAO
Original site: A0A1D8P8T7_9FLAO 
ID   A0A1D8P8T7_9FLAO        Unreviewed;      1107 AA.
AC   A0A1D8P8T7;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=LPB138_09855 {ECO:0000313|EMBL:AOW20959.1};
OS   Urechidicola croceus.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Urechidicola.
OX   NCBI_TaxID=1850246 {ECO:0000313|EMBL:AOW20959.1, ECO:0000313|Proteomes:UP000176050};
RN   [1] {ECO:0000313|EMBL:AOW20959.1, ECO:0000313|Proteomes:UP000176050}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LPB0138 {ECO:0000313|EMBL:AOW20959.1,
RC   ECO:0000313|Proteomes:UP000176050};
RA   Kim E., Yi H.;
RT   "Lutibacter sp. LPB0138, isolated from marine gastropod.";
RL   Submitted (OCT-2016) 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};
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DR   EMBL; CP017478; AOW20959.1; -; Genomic_DNA.
DR   RefSeq; WP_070237123.1; NZ_CP017478.1.
DR   AlphaFoldDB; A0A1D8P8T7; -.
DR   STRING; 1850246.LPB138_09855; -.
DR   KEGG; lul:LPB138_09855; -.
DR   OrthoDB; 9811889at2; -.
DR   Proteomes; UP000176050; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 3.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.40.50.2300; -; 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; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
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; 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; 3.
DR   PANTHER; PTHR43047:SF5; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF13185; GAF_2; 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; PF08448; PAS_4; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 3.
DR   SMART; SM00091; PAS; 3.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 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; 1.
DR   PROSITE; PS50112; PAS; 3.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000176050};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          200..270
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          339..387
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          393..445
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          446..499
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          750..967
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          992..1107
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          503..530
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         1042
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1107 AA;  127168 MW;  2C9BB10B1435E7E6 CRC64;
     MKEKVSPKTI LDYHTCSSHE NENKSTLKAM NDKYFTFFEY APIALWIEDF SSVKRYIDGI
     VQANNTTIPE FIEANPHITS HLASLVTVKE VNNAAVSLYK AKSKKDLIQN LEKVFTPDSN
     RGFERLVVDL LCGKTENSVE TINKTFSNDI INILIKVKIA DGSEESLEQV IVSVEDITER
     VKTRNVLIEN ALSKKKSDKT KHLLSNTLSS IRDGLVILDA NSNYTYVNKK ATEFLGKSYD
     ELIGKNIWNE FPERKGDIFY DNYQEAIKTK KPMSFENFYE PWGRWFENRI IPSKDNILIF
     FDETTERKDN ENRIKTAYNI INKSSSVAIL CKNEWNFPIE FASENSIQLF GYSHNELLSN
     KINIHNTVHP DDLEYFRTNV FSLGKKDKSQ GFRPRPFRII TKNGEMKWVQ ANIDIIKNDR
     NEVTHIQGIV EDITERKKTE DLFFESSQRL KHQFNHTPLA SIMWDLDFNL IEWNKSAERI
     FGYCENEAKG KKIKDLITPP YLVDEMSNIV DNLLNEKGSL RNTNDNLTKN GKIITCDWYN
     VVLKDTEGNV IGVASLVDDI TERVKKERLE EVLYNISKAA SIIDNFNNFS VFIKEELNKI
     IDTRNFYIAL YNKESDIITT PVFVDETEQL EEFPAKDTLT GYVIKNNKPL LLKNKDYLKL
     IEQGEVKLVG KHAAIWVGVP LKIKGEAVGA IVVQNYTNQN AFNENDVNLL EFVADQISTT
     IQRKKSEKEL KDALIKAQES DKLKSSFLAN MSHEIRTPMN GIIGFSELFL DSDLSTSQRK
     KYAEIVIDSS KQLLSIVNDI LDISKIEAGV IKLTNENVNL NSLLNILYNF YKPIAEENNI
     KLKCHKGLKD NLSNIEIDKT KLHQILTNLI SNAFKFTDYG EIQFGYELKK DHLEFYVKDT
     GSGIEEQLQD KIFDRFIQAN NDLSKMNKGT GLGLSITKKF IELFNGEIWL SSSKNGTDFY
     FTIPYSKSSS HLNLQTLIDN KNEVVVNEKE ITILVVEDEE YNMMYINELF SKTNFRVIEA
     YNGKEAIEIF ENHPEIDLIL MDMKMPIMNG KDAMVSIKKE KPDLPIIALS AFAMETDKTE
     AINNGFDAYL TKPINKNLLF KKINNFV
//
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