ID A0A3A1R7N7_9BACI Unreviewed; 371 AA.
AC A0A3A1R7N7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 18-JUN-2025, entry version 29.
DE RecName: Full=Signal transduction histidine-protein kinase/phosphatase DegS {ECO:0000256|PIRNR:PIRNR003169};
DE EC=2.7.13.3 {ECO:0000256|PIRNR:PIRNR003169};
DE EC=3.1.3.- {ECO:0000256|PIRNR:PIRNR003169};
GN ORFNames=D3H55_01650 {ECO:0000313|EMBL:RIW39112.1};
OS Bacillus salacetis.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2315464 {ECO:0000313|EMBL:RIW39112.1, ECO:0000313|Proteomes:UP000265801};
RN [1] {ECO:0000313|EMBL:RIW39112.1, ECO:0000313|Proteomes:UP000265801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKP7-4 {ECO:0000313|EMBL:RIW39112.1,
RC ECO:0000313|Proteomes:UP000265801};
RA Daroonpunt R., Tanasupawat S., Yiamsombut S.;
RT "Bacillus saliacetes sp. nov., isolated from Thai shrimp paste (Ka-pi).";
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Member of the two-component regulatory system DegS/DegU,
CC which plays an important role in the transition growth phase.
CC {ECO:0000256|PIRNR:PIRNR003169}.
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 ECO:0000256|PIRNR:PIRNR003169};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR003169}.
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:RIW39112.1}.
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DR EMBL; QXIR01000001; RIW39112.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A1R7N7; -.
DR OrthoDB; 9781904at2; -.
DR Proteomes; UP000265801; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR CDD; cd16917; HATPase_UhpB-NarQ-NarX-like; 1.
DR Gene3D; 1.20.5.1930; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR008595; DegS.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR050482; Sensor_HK_TwoCompSys.
DR InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR InterPro; IPR016381; Sig_transdc_His_kinase_DegS.
DR PANTHER; PTHR24421; NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED; 1.
DR PANTHER; PTHR24421:SF55; SENSOR HISTIDINE KINASE YDFH; 1.
DR Pfam; PF05384; DegS; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF07730; HisKA_3; 1.
DR PIRSF; PIRSF003169; STHK_DegS; 1.
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, ECO:0000256|PIRNR:PIRNR003169};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR003169};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR003169};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR003169};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR003169};
KW Protein phosphatase {ECO:0000256|PIRNR:PIRNR003169};
KW Reference proteome {ECO:0000313|Proteomes:UP000265801};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR003169};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012,
KW ECO:0000256|PIRNR:PIRNR003169}.
FT DOMAIN 174..371
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 102..136
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 371 AA; 42768 MW; DAAAB5192F503446 CRC64;
MLDNILEQMI DTVGRSKQDV FEIGEQCRQD YESITDELKV IRESVFKVIK EGDELEQKSR
FSRRRLSEVS QHFQNFSEEQ VREAYEKAHD LQMKLSLNRQ TEARLRERRD DLERRIKNLQ
DTIDRAEQLN SQISVVLNYL SSDLKLMGAA LEDAKERHDF GLQIIEAQEE ERKKLSREIH
DGPAQMLANV LLRSDLIDRV YRENGAIAAL GEIKDLKKMV RSALYEVRRI IYDLRPMALD
DLGLVPTLTK YLSTIEEYHR STNIRFVNVG QEKRLPSKYE VALFRLIQES VQNALKHSEA
AEILVKLEIT KEKVTVIIKD NGKGFDIKEK KSGSFGIMGM KERVEILDGE MSIDSKVGSG
TVILVQVPLT A
//
