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Database: UniProt
Entry: A0A1C0YKW8_9BACL
LinkDB: A0A1C0YKW8_9BACL
Original site: A0A1C0YKW8_9BACL 
ID   A0A1C0YKW8_9BACL        Unreviewed;       381 AA.
AC   A0A1C0YKW8;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, 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=A6M13_08840 {ECO:0000313|EMBL:OCS87822.1};
OS   Caryophanon tenue.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Caryophanon.
OX   NCBI_TaxID=33978 {ECO:0000313|EMBL:OCS87822.1, ECO:0000313|Proteomes:UP000093199};
RN   [1] {ECO:0000313|EMBL:OCS87822.1, ECO:0000313|Proteomes:UP000093199}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14152 {ECO:0000313|EMBL:OCS87822.1,
RC   ECO:0000313|Proteomes:UP000093199};
RA   Verma A., Pal Y., Krishnamurthi S.;
RT   "Caryophanon tenue genome sequencing.";
RL   Submitted (JUL-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:OCS87822.1}.
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DR   EMBL; MASJ01000003; OCS87822.1; -; Genomic_DNA.
DR   RefSeq; WP_066543662.1; NZ_MASJ01000003.1.
DR   AlphaFoldDB; A0A1C0YKW8; -.
DR   STRING; 33978.A6M13_08840; -.
DR   OrthoDB; 9781904at2; -.
DR   Proteomes; UP000093199; 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   SUPFAM; SSF57997; Tropomyosin; 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:UP000093199};
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          184..381
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          105..146
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   381 AA;  44263 MW;  E48AEFA5545A3662 CRC64;
     MFLNNPIDIT AIDQIFNRML ETITSSKDDI FIISEQSRRS FDEMRKELEY IRAQLSQIIT
     ESDVLERRTQ LARQRLVTVS KAFDQFSEEQ IREAYESAND LQVQLSINQA TEKQLRERRD
     DLERRLRALE ETIERAEHIV NQVNVVINYL TADLKNVAPA LENAKMKHEF SIQIIEAQEE
     ERKRLSREIH DGPAQMLANV LMRTDLIERT YREKGIDRAL EEIASLKVNV RNALHEVRRI
     IYDLRPMALD DLGIVPTLRK YLSTVEEYNP GIRINFVSNG AERRIPSNYE VSIFRLVQEC
     VTNSVKHGKT HEVWVKIEWL KSAVNIVVKD NGVGFDRNIV KEKSFGLIGM RERVDLLKGS
     MQVESEPNKG TIMLFKIPLA I
//
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