ID A0A2A2I9A3_9BACI Unreviewed; 335 AA.
AC A0A2A2I9A3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, 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=CIL05_18785 {ECO:0000313|EMBL:PAV28152.1};
OS Virgibacillus profundi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX NCBI_TaxID=2024555 {ECO:0000313|EMBL:PAV28152.1, ECO:0000313|Proteomes:UP000218887};
RN [1] {ECO:0000313|EMBL:PAV28152.1, ECO:0000313|Proteomes:UP000218887}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IO3-P3-H5 {ECO:0000313|EMBL:PAV28152.1,
RC ECO:0000313|Proteomes:UP000218887};
RA Xu B., Hu B., Wang J., Zhu Y., Huang L., Du W., Huang Y.;
RT "Virgibacillus indicus sp. nov. and Virgibacillus profoundi sp. nov, two
RT moderately halophilic bacteria isolated from marine sediment by using the
RT Microfluidic Streak Plate.";
RL Submitted (AUG-2017) 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:PAV28152.1}.
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DR EMBL; NPOA01000015; PAV28152.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2I9A3; -.
DR OrthoDB; 9780487at2; -.
DR Proteomes; UP000218887; 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; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR PANTHER; PTHR45453:SF2; TWO-COMPONENT SENSOR HISTIDINE KINASE; 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 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 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 125..335
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 335 AA; 39133 MW; 0BC0EA6F5F0BFDE0 CRC64;
MERKGMRDFL KDNLPFILFF YSQCVLIIGI AQLASIIAGQ SMGPDILIYL IVLPTFCLIV
FLLFRYGKFR DFYIKHEQAI ESFPEAPNHL LENIKRQHDI KTNRYAEEVD KLEQQKQLEF
NFIQQWVHQM KTPVSVMHLT MQKEKLNLPE DYYHSMTEEL ERLQQGLDLV LYQSRLQKFD
RDFHVQKLAL KPMVTDVIQE FKSSFIRHHV FPTVTIDETI TVATDPKWFR FVITQLLSNA
IKYSKESSDK IYFTVMEKAK TLTLEIRDTG HGIPTQDLNR VFDPFFTGLN GRTFRESTGM
GLYLSKQICD ALGHDLEITS VQDKGTAVTI TFQNP
//
