ID A0A401I623_9BACL Unreviewed; 590 AA.
AC A0A401I623;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=PA598K_05055 {ECO:0000313|EMBL:GBF76577.1};
OS Paenibacillus sp. 598K.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1117987 {ECO:0000313|EMBL:GBF76577.1, ECO:0000313|Proteomes:UP000288287};
RN [1] {ECO:0000313|EMBL:GBF76577.1, ECO:0000313|Proteomes:UP000288287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=598K {ECO:0000313|EMBL:GBF76577.1,
RC ECO:0000313|Proteomes:UP000288287};
RA Mizushima D., Miyazaki T., Shiwa Y., Kimura K., Fujita N., Yoshikawa H.,
RA Kimura A., Kitamura S., Hara H., Funane K.;
RT "A novel intracellular dextranase derived from Paenibacillus sp. 598K with
RT an ability of degrading cycloisomaltooligosaccharides.";
RL Submitted (MAR-2018) 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 -!- 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:GBF76577.1}.
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DR EMBL; BFBX01000091; GBF76577.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401I623; -.
DR Proteomes; UP000288287; 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; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal 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; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000288287};
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 138..158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 170..191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 237..255
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 261..289
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 296..320
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 326..344
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 383..587
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 590 AA; 66971 MW; 39BB9AB9B4C6D3B9 CRC64;
MHWETDSPAP DGSPPVRTDW FKIADHEPLV SLPEQVSAAS LRLQLPELPW EHNTLFIERL
YGQNVQIYIG GELLYEAERN HLFDVHQILI PIEPTHAGQE LMIRVDTATA RIGLDQPVVV
GEYGPLLKQY VQQGLFDIVL GAAFVFIALI MLVCSAFLQR EQLKRWISLL LIILPTGMLI
ITYSPYLYTF YPQIGKFAFH LFDLSLLVLL PSLTYFFERM MEGRKLGFVT KFRKFQVGYS
LFCLVCSIIN ILTDYHYYDI YFLITVTALG CIMLVQLSIL FICSVYFAFK GNKVALIFST
GFMIFAMLGI IDLMLFYLRA GNYDLILWKW GIVCFVVSLI IILGRRFASD HKQLITYSKE
LEMFNTRLQR SEKMEIISGL AASVAHEVRN PLQVTRGFLQ LLRENSSAKD RHYMALAIDE
LDRASHIITD FLTFAKPELE EVSILNIALE LKHIEGILRP LANLQGGTIV LDIPAQLYIQ
GNSSKLKQAF INIIKNSIEA LNGQGEIRIW AYKEQEDVVV HIKDDGEGMN ASELAKLGEP
YFSNKTKGTG LGLMVTFRII EVMQGKLEFR SVKGVGTEAV LRFPSVSAPL
//
