ID L0F692_DESDL Unreviewed; 768 AA.
AC L0F692;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Desdi_0959 {ECO:0000313|EMBL:AGA68478.1};
OS Desulfitobacterium dichloroeliminans (strain LMG P-21439 / DCA1).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=871963 {ECO:0000313|EMBL:AGA68478.1, ECO:0000313|Proteomes:UP000010797};
RN [1] {ECO:0000313|Proteomes:UP000010797}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG P-21439 / DCA1 {ECO:0000313|Proteomes:UP000010797};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Kruse T.,
RA de Vos W.M., Boon N., Smidt H., Woyke T.;
RT "Complete sequence of Desulfitobacterium dichloroeliminans LMG P-21439.";
RL Submitted (FEB-2012) 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; CP003344; AGA68478.1; -; Genomic_DNA.
DR AlphaFoldDB; L0F692; -.
DR STRING; 871963.Desdi_0959; -.
DR KEGG; ddl:Desdi_0959; -.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG4585; Bacteria.
DR eggNOG; COG5000; Bacteria.
DR HOGENOM; CLU_431932_0_0_9; -.
DR Proteomes; UP000010797; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd16917; HATPase_UhpB-NarQ-NarX-like; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.20.5.1930; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR24421; NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF07730; HisKA_3; 1.
DR Pfam; PF13426; PAS_9; 1.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000010797};
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 7..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 167..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 184..236
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 244..331
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 322..372
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 671..764
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 540..575
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 768 AA; 85732 MW; DA0D20D75EE91482 CRC64;
MKLSTKMIII TVILIVVMGL LTMGAISTIV EQAMTQQLEE QGSTYSRMAA DNVANPLLDG
NVLIVQRTIE NLLQTGSGIS YVYVIDNDGK VIAHTFSGGF PSSLTNTNIL KSNQITNTML
LNVQSQGLIR DVGVRILEGL NAEIHVGFSQ DIISQWTYNV RNLMLNLTVY GVLIGAVAAL
VLSTLITRPL KKLASHALRL GKGNLEEDII IRGRDEIVEL AGCLNRMRKD LFTGMQMLRQ
SEESNRTLLE AISAAGEGIV VFQDSENHKS AMTYVNEQYE NLTGYSKEEL FEMEGNEIVD
SESRKQVEEV WVLSERGLIL PKQIEIAIER KDGSKLYLEA SYCNITYEGS QAIICINRDI
TEKKKTSMEI IRKNRELAAL NELSKAISGQ MNFKGKLDEA LNTILQVVGK QAGWILVYNE
RDDVNKAELM CQIGILPEEA LAQTKQFQRC TNFPPPNSNS IQVHSSLSTA CPIKQLYLPD
GTKALSHVYV PLSYKDRVLG VLNIIASDLE SFAKEDLNLL NSIGLQLGVA IENAELWVEL
NKKEILRKQL LNKVITAQEE ERKRISRELH DESSQTIAAL GIGLKSAIEI MQFDQEYALT
VLEDLKNKTS MILKELHQII YDLRPSLLDD LGLMPAIRWY VESRLETTGM KPHVTFAGNP
IRLPDDIEMT IFRIVQESIT NAIKYSNAKN VYVGLQFDLN SLEVFIEDDG VGFNIEKAFS
QIDGKESLGL LGMTERAELV GGEIDIKSRI DSGTRISLKL DFPDFETS
//
