ID A0A069D256_9BACE Unreviewed; 937 AA.
AC A0A069D256;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=JCM15093_1571 {ECO:0000313|EMBL:GAK36410.1};
OS Bacteroides graminisolvens DSM 19988 = JCM 15093.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1121097 {ECO:0000313|EMBL:GAK36410.1, ECO:0000313|Proteomes:UP000027601};
RN [1] {ECO:0000313|EMBL:GAK36410.1, ECO:0000313|Proteomes:UP000027601}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 15093 {ECO:0000313|EMBL:GAK36410.1,
RC ECO:0000313|Proteomes:UP000027601};
RX PubMed=25736980;
RA Inoue J., Oshima K., Suda W., Sakamoto M., Iino T., Noda S., Hongoh Y.,
RA Hattori M., Ohkuma M.;
RT "Distribution and evolution of nitrogen fixation genes in the phylum
RT bacteroidetes.";
RL Microbes Environ. 30:44-50(2015).
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:GAK36410.1}.
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DR EMBL; BAJS01000006; GAK36410.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A069D256; -.
DR STRING; 1121097.GCA_000428125_00701; -.
DR eggNOG; COG3292; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR Proteomes; UP000027601; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA 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 Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
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; IPR013783; Ig-like_fold.
DR InterPro; IPR011110; Reg_prop.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR011123; Y_Y_Y.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF07494; Reg_prop; 3.
DR Pfam; PF07495; Y_Y_Y; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000313|EMBL:GAK36410.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000027601};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 739..760
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 785..937
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 937 AA; 107192 MW; D0B07011CD119392 CRC64;
MKSGLFPATR VYKAELDQSG NEWILTDNGL GLIKKGEKKM TPYFVDAKDG REHADQAFYG
FAESQDELFF ASDRGRVWRY NKKAQRFTLL ELPTKSAVAD IAVVHSSELV AATETDGFFT
YNLKTEKATH YSHIVCSDFP HVPVRSIYVD KKSEVWFEQE LVGTVAHFNP SSKILKVEKM
RVEPGSAYRG HPAFHIHEDS HGTTWVHPYG GGFSYFDRKS NSLIPFYDDL DSPDWRFSNK
MHAAFSDRQG NLWLCSHSKG LEKVTFLTTQ FHLNTPVKHN YESLSNDVRA LFQDKEGNLW
AGLKDGMLRV YNSKQQYLGY LTEQGTIAQS GTPLKGSTYA LTQDRQGILW IATKGDGLVR
AEKRGDRYLL TRYKYSADDI YSLSNDNLYS VFEDSKGRLW IATYGGGINY IEKDKSGKLL
FINHRNNLKG YPIDKCHRAR FITSDRKGNI WVGTTTGAIS FNENFKNPEA IHFHHYSRSS
TNPHSLSNND VHWILATRKG EVYLATFGGG LNKLTGYGKG EEAIFRAYSV ADGLPSDILL
SIREDKQGNL WMSTENGISK FIPSTETFEN YDDRSFTFRV RFNEAASEIT ANGQIFFGAS
GGIFYFNPQK IRKSTFTPHI VFSKLLIANE DIIPGDKSVL KVILDDTREL VLSHKENVFA
IQYAALDYIN PANIQYAYIL EGFEKQWTYA DKLRNATYTN LPKGHYVFKV KSTNSDGVWV
DNVRTLDIEV LPSFWETPFA YFLYVVAILL IILITVYILF TIYRLKHEVS VEQQVSDIKL
RFFTNISHEL RTPLTLIAGP VGYILKNNQL SADVREQLLV VERNTNRMLR LVNQILDFRK
IQNKKMKMQV QRINVVAFTR NIMNNFESLA EEQQIDFIFE TEKDELCLWV DADKFEKILF
NLLSNAFKYT PVGKSITVFI REEENTVSIG VQDQASV
//