ID A0A1I4LS81_9BACL Unreviewed; 717 AA.
AC A0A1I4LS81;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN03159341_11256 {ECO:0000313|EMBL:SFL93706.1};
OS Paenibacillus sp. 1_12.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1566278 {ECO:0000313|EMBL:SFL93706.1, ECO:0000313|Proteomes:UP000198699};
RN [1] {ECO:0000313|EMBL:SFL93706.1, ECO:0000313|Proteomes:UP000198699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1_12 {ECO:0000313|EMBL:SFL93706.1,
RC ECO:0000313|Proteomes:UP000198699};
RA de Groot N.N.;
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; FOTE01000012; SFL93706.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4LS81; -.
DR STRING; 1566278.SAMN03159341_11256; -.
DR Proteomes; UP000198699; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR InterPro; IPR008979; Galactose-bd-like_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; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR PANTHER; PTHR45453:SF1; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR Pfam; PF07695; 7TMR-DISM_7TM; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
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; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SFL93706.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 218..243
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 250..267
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 319..338
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 371..390
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 396..417
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 480..704
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 453..480
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 717 AA; 80771 MW; 4F4A25A05E7BA9E4 CRC64;
MVWISKYYLH YIWILVLYAI LLLSISGCEA DQPVSSPRPL SGWEAVQGVQ NLRDWNFGSN
GIAALNGQWE FYWAQLLIPA QIADMQDQER PRHWIGLPQA WNGQEIDGER ISGMGYATFH
LQVQLAPSSR VLAVELPMIR TAYRMWINGQ FVANGGRVGQ DRDTSVPVNY PQLVLFPQAG
AEKLDIVMQV SNFDHRYGGI ENELLLGEAK QMVSHHDWLM GVDMLLVGSL LLMGFYNLGL
FLIRMKEKSP LYLGLFCLLV GVRAMLVGEG AMFKLFPRLN WVTSIRMEYV CFYLGTAAAL
VFCYSLYRKE TSRTIVQITL FSCAVFTAAT LLAPPWIFTS MLMIYQWLNA AVCVSLIITL
MRAFAAKREG ALLILSGVII YMILAAIDAA EYDRWIGFRG LSPWGLFCVI FLASFVISMK
SVQAFASVET LSRELRDLNM RLEYRIKERT TELEQSNLTL AKTNEDLARL ETSRRHLLSN
ISHDLGTPMT LIQGYVEALI DRVVVGTEQQ DKYLKLILSR IMGLNRLIAD LFQLSKLEAR
QIDFYMQELT IKQFIAYFSE RYVVEVHNAG LQFEFLPSTT APPEDSDKAM MIDMNRMDQV
FTNLVHNAIK HTSAGGLIQV LLQEDERTLM IKVQDTGSGI EPDDLPYVFD RFYKKDKSRN
SAAGGSGLGL AIAKEIVEFH GGSIWAESLS GQGALICLEL PLKEAAPKDT QSLGNPS
//