ID A0A4P6ZZ83_9BACL Unreviewed; 381 AA.
AC A0A4P6ZZ83;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 18-JUN-2025, entry version 30.
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=E2636_11635 {ECO:0000313|EMBL:QBP41757.1};
OS Paenisporosarcina antarctica.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Caryophanaceae;
OC Paenisporosarcina.
OX NCBI_TaxID=417367 {ECO:0000313|EMBL:QBP41757.1, ECO:0000313|Proteomes:UP000294292};
RN [1] {ECO:0000313|EMBL:QBP41757.1, ECO:0000313|Proteomes:UP000294292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6503 {ECO:0000313|EMBL:QBP41757.1,
RC ECO:0000313|Proteomes:UP000294292};
RA Rong J.-C., Chi N.-Y., Zhang Q.-F.;
RT "Complete genome sequence of Paenisporosarcina antarctica CGMCC 1.6503T.";
RL Submitted (MAR-2019) 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}.
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DR EMBL; CP038015; QBP41757.1; -; Genomic_DNA.
DR RefSeq; WP_134210333.1; NZ_CP038015.1.
DR AlphaFoldDB; A0A4P6ZZ83; -.
DR KEGG; panc:E2636_11635; -.
DR OrthoDB; 9781904at2; -.
DR Proteomes; UP000294292; Chromosome.
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:UP000294292};
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..380
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 83..138
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 381 AA; 43894 MW; E88B68A88F84D3E5 CRC64;
MSGKKVDINS LNHIFSQMVQ TMNRSKNDIF IISEQNRQSL LQMQKELEIV HSKLAAVLIE
GDLLVEETRI SRKTLGDVSK HFNTFTEEQV REAYEQANDL QIKLSINRTE DRQLHERRDD
LERRLNELND SILHADQLAG QANVVTNYLT SDLKNVGPAL ETAKLKQDFS LKIIEAQEEE
RKRLSREIHD GPAQMMANVL VRSDLIERTY RENGIDEALV EITSLKLMVR IALTEVRRII
YDLRPMALDD LGLVPTIRKY LMNIEEYNTG CQINFRSHGE QRRLISNFEI AVFRLVQESV
TNATKHGKCQ NIWVDVEWTP RMVTVTVKDN GTGFDQRLVR ESSFGLIGMQ ERIDLLKGEM
IVKSSLGNGT IMKFKIPLNE E
//