ID A0A4Z0GJ17_9BACL Unreviewed; 390 AA.
AC A0A4Z0GJ17;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 18-JUN-2025, entry version 27.
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=E4665_17360 {ECO:0000313|EMBL:TGA95878.1};
OS Sporolactobacillus shoreae.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Sporolactobacillaceae;
OC Sporolactobacillus.
OX NCBI_TaxID=1465501 {ECO:0000313|EMBL:TGA95878.1, ECO:0000313|Proteomes:UP000298347};
RN [1] {ECO:0000313|EMBL:TGA95878.1, ECO:0000313|Proteomes:UP000298347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BK92 {ECO:0000313|EMBL:TGA95878.1,
RC ECO:0000313|Proteomes:UP000298347};
RX PubMed=25634946; DOI=.1099/ijs.0.000084;
RA Thamacharoensuk T., Kitahara M., Ohkuma M., Thongchul N., Tanasupawat S.;
RT "Sporolactobacillus shoreae sp. nov. and Sporolactobacillus spathodeae sp.
RT nov., two spore-forming lactic acid bacteria isolated from tree barks in
RT Thailand.";
RL Int. J. Syst. Evol. Microbiol. 65:1220-1226(2015).
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:TGA95878.1}.
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DR EMBL; SRJD01000036; TGA95878.1; -; Genomic_DNA.
DR RefSeq; WP_135350059.1; NZ_SRJD01000036.1.
DR AlphaFoldDB; A0A4Z0GJ17; -.
DR OrthoDB; 9781904at2; -.
DR Proteomes; UP000298347; 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:UP000298347};
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 297..385
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 109..143
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 390 AA; 44133 MW; 241FA0606D799C8A CRC64;
MSAGNVNAKS LDEKHLDKII NSMIENVSDS KSQIFDIGEE SRKEYDALTK ELHLVKQELT
GIIERSDKLE LEARMSRGRL AEISRAFDRY GEKDIRTAYE QANQIQNDLS LVRQTEKQMK
ARRNELERRL VQLNSTIKKA ENLVGQVTVV LHYLTSDLMQ IGEVVATARE QRALGLKIIE
AQEEERKRLS REIHDGPAQT LAQVLIGLDV VERVGKREGD EAARRELQKY RVMVQDALAE
VRRIIYDLRP MSLDDLGLVP TLQKYFHRVD SDFPSINIGF KNLGAEKRLQ SRIEAALFRL
VQEAVQNACV HANPSNVRIR LEFRKDEVII LVKDDGAGFD QSVKKEGSYG LIGMKERADL
LNGELTINSS PEHGTTILAA IPIQPGDVLD
//