ID A0A0W7YQB1_9BACI Unreviewed; 419 AA.
AC A0A0W7YQB1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AK833_01070 {ECO:0000313|EMBL:KUF37287.1};
OS Lysinibacillus sp. F5.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=1700846 {ECO:0000313|EMBL:KUF37287.1, ECO:0000313|Proteomes:UP000053086};
RN [1] {ECO:0000313|EMBL:KUF37287.1, ECO:0000313|Proteomes:UP000053086}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F5 {ECO:0000313|EMBL:KUF37287.1,
RC ECO:0000313|Proteomes:UP000053086};
RA Chan X.Y., Chan K.G., Hong K.W., Tan A., Chen J.W.;
RT "Draft Genome of marine Lysinibacillus sp. F5.";
RL Submitted (OCT-2015) 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:KUF37287.1}.
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DR EMBL; LKIE01000002; KUF37287.1; -; Genomic_DNA.
DR RefSeq; WP_051891648.1; NZ_LKIE01000002.1.
DR AlphaFoldDB; A0A0W7YQB1; -.
DR OrthoDB; 1674512at2; -.
DR Proteomes; UP000053086; 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:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065:SF34; SPORULATION KINASE A; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000313|EMBL:KUF37287.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
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 58..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 153..177
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 212..413
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 419 AA; 46792 MW; 117D88EEFB07BE0F CRC64;
MQSKLSMTRA SLTWIFIIAV LTAIGSEIKI MPFANTTFRF GLGTIIFFLC TLLKPTPIIL
AGIATSIVTT IFRVINSTLH NVPISESLFN HLPAALFYVL FAVCLQILDI QQYREKPLKL
GLLVAFSEVI SNLAEQIFRF FVQNYTFLFL HDLLILLAVA ILRSFFVVGI YSSILIAEQK
KRVQEMLNIG SDLYVETLYL KKSMNHIETI TASGYELYRQ LKVLGYRAES LQALHIAQEI
HEVKKDSQRI YAGISKIVGE RSFGPFVLSE LLHYIEEGNR KYAELLGKDI QFNTCIDFDF
QTKEHIALLA LLNNLSANAV EAIEEQGIIS IAIGRQEDNT VITVCDNGQG ISQADISVIF
EPGYTTKFNI DGVAATGIGL SHVAELVEKL KGSITVDSDD QYTTFKIIIP TQTIQTGET
//
