ID W7YPT3_9BACL Unreviewed; 384 AA.
AC W7YPT3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=JCM16418_4747 {ECO:0000313|EMBL:GAF10537.1};
OS Paenibacillus pini JCM 16418.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1236976 {ECO:0000313|EMBL:GAF10537.1, ECO:0000313|Proteomes:UP000019364};
RN [1] {ECO:0000313|EMBL:GAF10537.1, ECO:0000313|Proteomes:UP000019364}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 16418 {ECO:0000313|EMBL:GAF10537.1,
RC ECO:0000313|Proteomes:UP000019364};
RA Yuki M., Oshima K., Suda W., Oshida Y., Kitamura K., Iida Y., Hattori M.,
RA Ohkuma M.;
RT "Draft Genome Sequence of Paenibacillus pini JCM 16418T, Isolated from the
RT Rhizosphere of Pine Tree.";
RL Genome Announc. 2:e00210-14(2014).
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:GAF10537.1}.
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DR EMBL; BAVZ01000026; GAF10537.1; -; Genomic_DNA.
DR RefSeq; WP_036653014.1; NZ_BAZT01000026.1.
DR AlphaFoldDB; W7YPT3; -.
DR STRING; 1236976.JCM16418_4747; -.
DR eggNOG; COG4585; Bacteria.
DR OrthoDB; 9781904at2; -.
DR Proteomes; UP000019364; 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 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:UP000019364};
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 180..379
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 384 AA; 44711 MW; 8A978BF9A423A032 CRC64;
MDVQADAIDR VIKNAIQVME NSKYQMFEIL ETARDELLSL NQELQFVMKE TADTLQKVDQ
LELNYRRSRI RLTEVSRDFV RYKEEDIRQA YEKATQFQLD VMIYREKEMY LKARRDELQK
RARNVENSVE RAESIGSQMG VVLEYLSGEL GQVSKIIETA KNRQLIGLKI ILAQEEERKR
IAREIHDGPA QLLANLVLRT EIVERMLLKQ EFKMVQDEIV DLKGQVRSSL EEMRKVIFNL
RPMALDDLGL IPTLRKYVHD FEKKTRIRTI FETRGKEHRL SSAMEAAIYR LVQEALSNAS
KHACPTFVLV EITYQAQLVK IVVQDNGVGF KLELLEQKSK DHFGLIGMRE RVELLEGRME
IESAENEGTK IVIHIPTNVE KGKE
//