DEGS_BACSU
ID DEGS_BACSU Reviewed; 385 AA.
AC P13799; P19590;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Signal transduction histidine-protein kinase/phosphatase DegS;
DE EC=2.7.13.3;
DE EC=3.1.3.-;
GN Name=degS; Synonyms=sacU; OrderedLocusNames=BSU35500;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3141378; DOI=10.1128/jb.170.11.5102-5109.1988;
RA Henner D.J., Yang M., Ferrari E.;
RT "Localization of Bacillus subtilis sacU(Hy) mutations to two linked genes
RT with similarities to the conserved procaryotic family of two-component
RT signalling systems.";
RL J. Bacteriol. 170:5102-5109(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3141377; DOI=10.1128/jb.170.11.5093-5101.1988;
RA Kunst F., Debarbouille M., Msadek T., Young M., Maueel C., Karamata D.,
RA Klier A., Rapoport G., Dedonder R.;
RT "Deduced polypeptides encoded by the Bacillus subtilis sacU locus share
RT homology with two-component sensor-regulator systems.";
RL J. Bacteriol. 170:5093-5101(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969505; DOI=10.1099/13500872-142-11-3079;
RA Soldo B., Lazarevic V., Mauel C., Karamata D.;
RT "Sequence of the 305 degrees-307 degrees region of the Bacillus subtilis
RT chromosome.";
RL Microbiology 142:3079-3088(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 253-385.
RC STRAIN=168;
RX PubMed=3136143; DOI=10.1128/jb.170.8.3593-3600.1988;
RA Tanaka T., Kawata M.;
RT "Cloning and characterization of Bacillus subtilis iep, which has positive
RT and negative effects on production of extracellular proteases.";
RL J. Bacteriol. 170:3593-3600(1988).
RN [6]
RP FUNCTION, AND AUTOPHOSPHORYLATION.
RC STRAIN=168 / CU741;
RX PubMed=2123196; DOI=10.1016/s0021-9258(17)45474-3;
RA Mukai K., Kawata M., Tanaka T.;
RT "Isolation and phosphorylation of the Bacillus subtilis degS and degU gene
RT products.";
RL J. Biol. Chem. 265:20000-20006(1990).
RN [7]
RP FUNCTION, AND AUTOPHOSPHORYLATION.
RC STRAIN=168;
RX PubMed=1901568; DOI=10.1128/jb.173.8.2539-2547.1991;
RA Dahl M.K., Msadek T., Kunst F., Rapoport G.;
RT "Mutational analysis of the Bacillus subtilis DegU regulator and its
RT phosphorylation by the DegS protein kinase.";
RL J. Bacteriol. 173:2539-2547(1991).
RN [8]
RP FUNCTION AS A KINASE AND A PHOSPHATASE, AND MUTAGENESIS OF GLY-218.
RX PubMed=1909319; DOI=10.1128/jb.173.17.5507-5515.1991;
RA Tanaka T., Kawata M., Mukai K.;
RT "Altered phosphorylation of Bacillus subtilis DegU caused by single amino
RT acid changes in DegS.";
RL J. Bacteriol. 173:5507-5515(1991).
RN [9]
RP FUNCTION AS A KINASE AND A PHOSPHATASE, AND MUTAGENESIS OF ALA-193 AND
RP GLY-218.
RX PubMed=1321152; DOI=10.1016/s0021-9258(19)49742-1;
RA Dahl M.K., Msadek T., Kunst F., Rapoport G.;
RT "The phosphorylation state of the DegU response regulator acts as a
RT molecular switch allowing either degradative enzyme synthesis or expression
RT of genetic competence in Bacillus subtilis.";
RL J. Biol. Chem. 267:14509-14514(1992).
RN [10]
RP FUNCTION.
RX PubMed=12471443; DOI=10.1007/s00438-002-0774-2;
RA Mader U., Antelmann H., Buder T., Dahl M.K., Hecker M., Homuth G.;
RT "Bacillus subtilis functional genomics: genome-wide analysis of the DegS-
RT DegU regulon by transcriptomics and proteomics.";
RL Mol. Genet. Genomics 268:455-467(2002).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=168;
RX PubMed=17218307; DOI=10.1074/mcp.m600464-mcp200;
RA Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
RA Mann M.;
RT "The serine/threonine/tyrosine phosphoproteome of the model bacterium
RT Bacillus subtilis.";
RL Mol. Cell. Proteomics 6:697-707(2007).
RN [12]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=17850253; DOI=10.1111/j.1365-2958.2007.05923.x;
RA Kobayashi K.;
RT "Gradual activation of the response regulator DegU controls serial
RT expression of genes for flagellum formation and biofilm formation in
RT Bacillus subtilis.";
RL Mol. Microbiol. 66:395-409(2007).
RN [13]
RP ACTIVITY REGULATION, PHOSPHORYLATION AT SER-76, AND MUTAGENESIS OF SER-76.
RX PubMed=21304896; DOI=10.1371/journal.pone.0014653;
RA Jers C., Kobir A., Sondergaard E.O., Jensen P.R., Mijakovic I.;
RT "Bacillus subtilis two-component system sensory kinase DegS is regulated by
RT serine phosphorylation in its input domain.";
RL PLoS ONE 6:E14653-E14653(2011).
CC -!- FUNCTION: Member of the two-component regulatory system DegS/DegU,
CC which plays an important role in the transition growth phase. Involved
CC in the control of expression of different cellular functions, including
CC production of degradative enzymes such as the neutral and alkaline
CC proteases, flagellum formation and biofilm formation. Acts as both a
CC protein kinase that undergoes autophosphorylation and subsequently
CC transfers the phosphate to DegU, and a protein phosphatase that
CC dephosphorylates phospho-DegU. {ECO:0000269|PubMed:12471443,
CC ECO:0000269|PubMed:1321152, ECO:0000269|PubMed:17850253,
CC ECO:0000269|PubMed:1901568, ECO:0000269|PubMed:1909319,
CC ECO:0000269|PubMed:2123196}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- ACTIVITY REGULATION: Regulated via serine phosphorylation of its input
CC domain. Phosphotransfer from DegS to DegU is stimulated by
CC phosphorylation on Ser-76 and by DegQ. {ECO:0000269|PubMed:17850253,
CC ECO:0000269|PubMed:21304896}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- PTM: Autophosphorylated. Phosphorylated in vitro at Ser-76 by the
CC serine/threonine-protein kinase YbdM, which stimulates the phosphate
CC transfer to DegU. {ECO:0000269|PubMed:17218307,
CC ECO:0000269|PubMed:21304896}.
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DR EMBL; M23558; AAA22732.1; -; Genomic_DNA.
DR EMBL; M23649; AAA22734.1; -; Genomic_DNA.
DR EMBL; U56901; AAC44937.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15567.1; -; Genomic_DNA.
DR EMBL; M21658; AAA22544.1; -; Genomic_DNA.
DR PIR; B30191; RGBSDS.
DR RefSeq; NP_391430.1; NC_000964.3.
DR RefSeq; WP_003227983.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; P13799; -.
DR SMR; P13799; -.
DR IntAct; P13799; 6.
DR STRING; 224308.BSU35500; -.
DR iPTMnet; P13799; -.
DR jPOST; P13799; -.
DR PaxDb; P13799; -.
DR PRIDE; P13799; -.
DR DNASU; 936752; -.
DR EnsemblBacteria; CAB15567; CAB15567; BSU_35500.
DR GeneID; 936752; -.
DR KEGG; bsu:BSU35500; -.
DR PATRIC; fig|224308.179.peg.3841; -.
DR eggNOG; COG4585; Bacteria.
DR InParanoid; P13799; -.
DR OMA; IIFDLRP; -.
DR PhylomeDB; P13799; -.
DR BioCyc; BSUB:BSU35500-MON; -.
DR BRENDA; 2.7.13.3; 658.
DR Proteomes; UP000001570; Chromosome.
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 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Cytoplasm; Hydrolase; Kinase; Nucleotide-binding;
KW Phosphoprotein; Protein phosphatase; Reference proteome; Transferase;
KW Two-component regulatory system.
FT CHAIN 1..385
FT /note="Signal transduction histidine-protein
FT kinase/phosphatase DegS"
FT /id="PRO_0000074756"
FT DOMAIN 183..385
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT COILED 31..141
FT /evidence="ECO:0000255"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17218307,
FT ECO:0000269|PubMed:21304896"
FT MOD_RES 189
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MUTAGEN 76
FT /note="S->A: Lack of phosphorylation by YbdM."
FT /evidence="ECO:0000269|PubMed:21304896"
FT MUTAGEN 76
FT /note="S->D: Shows increased phosphorylation, as well as
FT increased autophosphorylation and phosphotransfer to DegU.
FT Negatively affects competence development."
FT /evidence="ECO:0000269|PubMed:21304896"
FT MUTAGEN 193
FT /note="A->V: Retains its autophosphorylation activity, but
FT cannot phosphorylate DegU."
FT /evidence="ECO:0000269|PubMed:1321152"
FT MUTAGEN 218
FT /note="G->E: Retains its autophosphorylation activity, but
FT shows a decrease in DegU phosphorylation activity.
FT Decreases the rate of dephosphorylation of DegU."
FT /evidence="ECO:0000269|PubMed:1321152,
FT ECO:0000269|PubMed:1909319"
SQ SEQUENCE 385 AA; 44958 MW; 871109565A7E78F1 CRC64;
MNKTKMDSKV LDSILMKMLK TVDGSKDEVF QIGEQSRQQY EQLVEELKQI KQQVYEVIEL
GDKLEVQTRH ARNRLSEVSR NFHRFSEEEI RNAYEKAHKL QVELTMIQQR EKQLRERRDD
LERRLLGLQE IIERSESLVS QITVVLNYLN QDLREVGLLL ADAQAKQDFG LRIIEAQEEE
RKRVSREIHD GPAQMLANVM MRSELIERIF RDRGAEDGFQ EIKNLRQNVR NALYEVRRII
YDLRPMALDD LGLIPTLRKY LYTTEEYNGK VKIHFQCIGE TEDQRLAPQF EVALFRLAQE
AVSNALKHSE SEEITVKVEI TKDFVILMIK DNGKGFDLKE AKEKKNKSFG LLGMKERVDL
LEGTMTIDSK IGLGTFIMIK VPLSL
