ID   DEGS_BREBE              Reviewed;         386 AA.
AC   P54663;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Signal transduction histidine-protein kinase/phosphatase DegS;
DE            EC=2.7.13.3;
DE            EC=3.1.3.-;
GN   Name=degS;
OS   Brevibacillus brevis (Bacillus brevis).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=1393;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Alk36;
RX   PubMed=7765823; DOI=10.1007/bf00170228;
RA   Louw M.E., Reid S.J., James M.D., Watson T.G.;
RT   "Cloning and sequencing the degS-degU operon from an alkalophilic Bacillus
RT   brevis.";
RL   Appl. Microbiol. Biotechnol. 42:78-84(1994).
CC   -!- FUNCTION: Member of the two-component regulatory system DegS/DegU,
CC       which plays an important role in the transition growth phase. Acts as
CC       both a protein kinase that undergoes autophosphorylation and
CC       subsequently transfers the phosphate to DegU, and a protein phosphatase
CC       that dephosphorylates phospho-DegU (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- PTM: Autophosphorylated. {ECO:0000250}.
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DR   EMBL; L15444; AAC41438.1; -; Genomic_DNA.
DR   PIR; I39834; I39834.
DR   AlphaFoldDB; P54663; -.
DR   SMR; P54663; -.
DR   BRENDA; 2.7.13.3; 638.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   Gene3D; 3.30.565.10; -; 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   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; SSF55874; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Hydrolase; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Protein phosphatase; Transferase;
KW   Two-component regulatory system.
FT   CHAIN           1..386
FT                   /note="Signal transduction histidine-protein
FT                   kinase/phosphatase DegS"
FT                   /id="PRO_0000074755"
FT   DOMAIN          188..384
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         194
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   386 AA;  44837 MW;  EE209CB8F663A17E CRC64;
     MPFKGLVVQV ADPQTLDKII DKTLDTVGKS REQIFEISEQ SRNEYVSLEQ ELQEVRMKVA
     EIIDQSDRAE VHARFARNRL AEVSKQFHRY SNEEIRKVYE QANELQVKLA LLQQEEQQLR
     DRRDAIERRL LNLKDTIERA EELVGQMTVV YNFLTGDLRQ VGEALEDARE KQAFGLQIIQ
     AQEEERRKLS REIHDGPAQM MANVLLRSEL VERIYHDKGI DEALKEIRDL RKMVKSSLAE
     VRRIIYDLRR MALDDLGLIP TLKKYVKTFE EHTGIFVDFK HIGKGERFPE HVEIALFRLV
     QEALQNTRKH AKASHVHVKI EEQKTKFTVV IKDNGKGFDQ TEKKEGSFGL VGMKERVNML
     KGQLVIRTKP NDGTTIIISI PITTEE