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
//