ID A0A1V2A4G3_9BACI Unreviewed; 388 AA.
AC A0A1V2A4G3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=BTO28_15695 {ECO:0000313|EMBL:OMP65820.1};
OS Domibacillus epiphyticus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Domibacillus.
OX NCBI_TaxID=1714355 {ECO:0000313|EMBL:OMP65820.1, ECO:0000313|Proteomes:UP000188613};
RN [1] {ECO:0000313|EMBL:OMP65820.1, ECO:0000313|Proteomes:UP000188613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAB 38 {ECO:0000313|EMBL:OMP65820.1,
RC ECO:0000313|Proteomes:UP000188613};
RA Verma A., Ojha A.K., Krishnamurthi S.;
RT "Domibacillus sp. SAB 38T whole genome sequencing.";
RL Submitted (DEC-2016) 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|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:OMP65820.1}.
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DR EMBL; MSFI01000030; OMP65820.1; -; Genomic_DNA.
DR RefSeq; WP_076768007.1; NZ_MSFI01000030.1.
DR AlphaFoldDB; A0A1V2A4G3; -.
DR STRING; 1714355.BTO28_15695; -.
DR OrthoDB; 9781904at2; -.
DR Proteomes; UP000188613; 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; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
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; SIGNAL TRANSDUCTION HISTIDINE-PROTEIN KINASE_PHOSPHATASE DEGS; 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:UP000188613};
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 183..384
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 61..124
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 388 AA; 44838 MW; 3A5E1DDAD24404B6 CRC64;
MSIRNSDTKL LDTILDKMVE TVDQSKDQIF SIAEQSRVDY ETLMTELELV KSHIHFAIIE
QEDLERKVKM ARRRLSEVSK DFSVYSEEVV REAYEKAHEL QMKLLVLRQN EKQLMERRND
LDRRLLSVNK TIERAEHLVS QTAVVLNYLT QDMKQFGQAL EDARLKQAFG LRVMEAQEEE
RKRLSREIHD GPAQMMANVL MRSDLIEKLY RERNVEDAFK EIRDLKKMVR SALYEVRRII
YDLRPMALDD LGLIPTLKKY LATVSDYNRS KSAEPDIEFV NIGMDKRLPS KLEVALFRLI
QESVQNALKH ADASSIMVKL EIKRDQVLAV VKDNGKGFLV NEKKSGSFGI MGMKERVELL
EGDITLHSKP GEGTAVLISV PVLEQTLN
//
