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   01-MAY-2013, entry version 58.
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;
OC   Brevibacillus.
OX   NCBI_TaxID=1393;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Alk36;
RX   PubMed=7765823; DOI=10.1007/s002530050220;
RA   Louw M.E., Reid S.J., James M.D., Watson T.G.;
RT   "Cloning and sequencing the degS-degU operon from an alkalophilic
RT   Bacillus 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
CC       as both a protein kinase that undergoes autophosphorylation and
CC       subsequently transfers the phosphate to DegU, and a protein
CC       phosphatase that dephosphorylates phospho-DegU (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + protein L-histidine = ADP + protein N-
CC       phospho-L-histidine.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- PTM: Autophosphorylated (By similarity).
CC   -!- SIMILARITY: Contains 1 histidine kinase domain.
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DR   EMBL; L15444; AAC41438.1; -; Genomic_DNA.
DR   PIR; I39834; I39834.
DR   ProteinModelPortal; P54663; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to 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:0023014; P:signal transduction by phosphorylation; IEA:GOC.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR008595; DegS.
DR   InterPro; IPR003594; HATPase_ATP-bd.
DR   InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR   InterPro; IPR005467; Sig_transdc_His_kinase_core.
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; ATP_bd_ATPase; 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       Signal transduction histidine-protein
FT                                kinase/phosphatase DegS.
FT                                /FTId=PRO_0000074755.
FT   DOMAIN      188    384       Histidine kinase.
FT   MOD_RES     194    194       Phosphohistidine; by autocatalysis (By
FT                                similarity).
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
//