Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Signal transduction histidine-protein kinase/phosphatase DegS

Gene

degS

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Member of the two-component regulatory system DegS/DegU, which plays an important role in the transition growth phase. Involved in the control of expression of different cellular functions, including production of degradative enzymes such as the neutral and alkaline proteases, flagellum formation and biofilm formation. Acts as both a protein kinase that undergoes autophosphorylation and subsequently transfers the phosphate to DegU, and a protein phosphatase that dephosphorylates phospho-DegU.6 Publications

Catalytic activityi

ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.

Enzyme regulationi

Regulated via serine phosphorylation of its input domain. Phosphotransfer from DegS to DegU is stimulated by phosphorylation on Ser-76 and by DegQ.2 Publications

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Kinase, Protein phosphatase, Transferase

Keywords - Biological processi

Two-component regulatory system

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciBSUB:BSU35500-MONOMER.
BRENDAi2.7.13.3. 658.

Names & Taxonomyi

Protein namesi
Recommended name:
Signal transduction histidine-protein kinase/phosphatase DegS (EC:2.7.13.3, EC:3.1.3.-)
Gene namesi
Name:degS
Synonyms:sacU
Ordered Locus Names:BSU35500
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi76 – 761S → A: Lack of phosphorylation by YbdM. 1 Publication
Mutagenesisi76 – 761S → D: Shows increased phosphorylation, as well as increased autophosphorylation and phosphotransfer to DegU. Negatively affects competence development. 1 Publication
Mutagenesisi193 – 1931A → V: Retains its autophosphorylation activity, but cannot phosphorylate DegU. 1 Publication
Mutagenesisi218 – 2181G → E: Retains its autophosphorylation activity, but shows a decrease in DegU phosphorylation activity. Decreases the rate of dephosphorylation of DegU. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 385385Signal transduction histidine-protein kinase/phosphatase DegSPRO_0000074756Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei76 – 761Phosphoserine2 Publications
Modified residuei189 – 1891Phosphohistidine; by autocatalysisPROSITE-ProRule annotation

Post-translational modificationi

Autophosphorylated. Phosphorylated in vitro at Ser-76 by the serine/threonine-protein kinase YbdM, which stimulates the phosphate transfer to DegU.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP13799.
PRIDEiP13799.

PTM databases

iPTMnetiP13799.

Interactioni

Protein-protein interaction databases

IntActiP13799. 6 interactions.
STRINGi224308.Bsubs1_010100019201.

Structurei

3D structure databases

ProteinModelPortaliP13799.
SMRiP13799. Positions 177-384.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini183 – 385203Histidine kinasePROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili31 – 141111Sequence analysisAdd
BLAST

Sequence similaritiesi

Contains 1 histidine kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG4105BZU. Bacteria.
ENOG410XNMH. LUCA.
HOGENOMiHOG000235655.
InParanoidiP13799.
KOiK07777.
OMAiPAQMMAN.
OrthoDBiEOG6W9X4M.
PhylomeDBiP13799.

Family and domain databases

Gene3Di3.30.565.10. 1 hit.
InterProiIPR008595. DegS.
IPR003594. HATPase_C.
IPR005467. His_kinase_dom.
IPR011712. Sig_transdc_His_kin_sub3_dim/P.
IPR016381. Sig_transdc_His_kinase_DegS.
[Graphical view]
PfamiPF05384. DegS. 1 hit.
PF02518. HATPase_c. 1 hit.
PF07730. HisKA_3. 1 hit.
[Graphical view]
PIRSFiPIRSF003169. STHK_DegS. 1 hit.
SMARTiSM00387. HATPase_c. 1 hit.
[Graphical view]
SUPFAMiSSF55874. SSF55874. 1 hit.
PROSITEiPS50109. HIS_KIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P13799-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKTKMDSKV LDSILMKMLK TVDGSKDEVF QIGEQSRQQY EQLVEELKQI
60 70 80 90 100
KQQVYEVIEL GDKLEVQTRH ARNRLSEVSR NFHRFSEEEI RNAYEKAHKL
110 120 130 140 150
QVELTMIQQR EKQLRERRDD LERRLLGLQE IIERSESLVS QITVVLNYLN
160 170 180 190 200
QDLREVGLLL ADAQAKQDFG LRIIEAQEEE RKRVSREIHD GPAQMLANVM
210 220 230 240 250
MRSELIERIF RDRGAEDGFQ EIKNLRQNVR NALYEVRRII YDLRPMALDD
260 270 280 290 300
LGLIPTLRKY LYTTEEYNGK VKIHFQCIGE TEDQRLAPQF EVALFRLAQE
310 320 330 340 350
AVSNALKHSE SEEITVKVEI TKDFVILMIK DNGKGFDLKE AKEKKNKSFG
360 370 380
LLGMKERVDL LEGTMTIDSK IGLGTFIMIK VPLSL
Length:385
Mass (Da):44,958
Last modified:December 1, 1992 - v2
Checksum:i871109565A7E78F1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23558 Genomic DNA. Translation: AAA22732.1.
M23649 Genomic DNA. Translation: AAA22734.1.
U56901 Genomic DNA. Translation: AAC44937.1.
AL009126 Genomic DNA. Translation: CAB15567.1.
M21658 Genomic DNA. Translation: AAA22544.1.
PIRiB30191. RGBSDS.
RefSeqiNP_391430.1. NC_000964.3.
WP_003227983.1. NZ_JNCM01000033.1.

Genome annotation databases

EnsemblBacteriaiCAB15567; CAB15567; BSU35500.
GeneIDi936752.
KEGGibsu:BSU35500.
PATRICi18979108. VBIBacSub10457_3716.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23558 Genomic DNA. Translation: AAA22732.1.
M23649 Genomic DNA. Translation: AAA22734.1.
U56901 Genomic DNA. Translation: AAC44937.1.
AL009126 Genomic DNA. Translation: CAB15567.1.
M21658 Genomic DNA. Translation: AAA22544.1.
PIRiB30191. RGBSDS.
RefSeqiNP_391430.1. NC_000964.3.
WP_003227983.1. NZ_JNCM01000033.1.

3D structure databases

ProteinModelPortaliP13799.
SMRiP13799. Positions 177-384.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP13799. 6 interactions.
STRINGi224308.Bsubs1_010100019201.

PTM databases

iPTMnetiP13799.

Proteomic databases

PaxDbiP13799.
PRIDEiP13799.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15567; CAB15567; BSU35500.
GeneIDi936752.
KEGGibsu:BSU35500.
PATRICi18979108. VBIBacSub10457_3716.

Phylogenomic databases

eggNOGiENOG4105BZU. Bacteria.
ENOG410XNMH. LUCA.
HOGENOMiHOG000235655.
InParanoidiP13799.
KOiK07777.
OMAiPAQMMAN.
OrthoDBiEOG6W9X4M.
PhylomeDBiP13799.

Enzyme and pathway databases

BioCyciBSUB:BSU35500-MONOMER.
BRENDAi2.7.13.3. 658.

Family and domain databases

Gene3Di3.30.565.10. 1 hit.
InterProiIPR008595. DegS.
IPR003594. HATPase_C.
IPR005467. His_kinase_dom.
IPR011712. Sig_transdc_His_kin_sub3_dim/P.
IPR016381. Sig_transdc_His_kinase_DegS.
[Graphical view]
PfamiPF05384. DegS. 1 hit.
PF02518. HATPase_c. 1 hit.
PF07730. HisKA_3. 1 hit.
[Graphical view]
PIRSFiPIRSF003169. STHK_DegS. 1 hit.
SMARTiSM00387. HATPase_c. 1 hit.
[Graphical view]
SUPFAMiSSF55874. SSF55874. 1 hit.
PROSITEiPS50109. HIS_KIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Localization of Bacillus subtilis sacU(Hy) mutations to two linked genes with similarities to the conserved procaryotic family of two-component signalling systems."
    Henner D.J., Yang M., Ferrari E.
    J. Bacteriol. 170:5102-5109(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Deduced polypeptides encoded by the Bacillus subtilis sacU locus share homology with two-component sensor-regulator systems."
    Kunst F., Debarbouille M., Msadek T., Young M., Maueel C., Karamata D., Klier A., Rapoport G., Dedonder R.
    J. Bacteriol. 170:5093-5101(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Sequence of the 305 degrees-307 degrees region of the Bacillus subtilis chromosome."
    Soldo B., Lazarevic V., Mauel C., Karamata D.
    Microbiology 142:3079-3088(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  4. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  5. "Cloning and characterization of Bacillus subtilis iep, which has positive and negative effects on production of extracellular proteases."
    Tanaka T., Kawata M.
    J. Bacteriol. 170:3593-3600(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 253-385.
    Strain: 168.
  6. "Isolation and phosphorylation of the Bacillus subtilis degS and degU gene products."
    Mukai K., Kawata M., Tanaka T.
    J. Biol. Chem. 265:20000-20006(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, AUTOPHOSPHORYLATION.
    Strain: 168 / CU741.
  7. "Mutational analysis of the Bacillus subtilis DegU regulator and its phosphorylation by the DegS protein kinase."
    Dahl M.K., Msadek T., Kunst F., Rapoport G.
    J. Bacteriol. 173:2539-2547(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, AUTOPHOSPHORYLATION.
    Strain: 168.
  8. "Altered phosphorylation of Bacillus subtilis DegU caused by single amino acid changes in DegS."
    Tanaka T., Kawata M., Mukai K.
    J. Bacteriol. 173:5507-5515(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A KINASE AND A PHOSPHATASE, MUTAGENESIS OF GLY-218.
  9. "The phosphorylation state of the DegU response regulator acts as a molecular switch allowing either degradative enzyme synthesis or expression of genetic competence in Bacillus subtilis."
    Dahl M.K., Msadek T., Kunst F., Rapoport G.
    J. Biol. Chem. 267:14509-14514(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A KINASE AND A PHOSPHATASE, MUTAGENESIS OF ALA-193 AND GLY-218.
  10. "Bacillus subtilis functional genomics: genome-wide analysis of the DegS-DegU regulon by transcriptomics and proteomics."
    Mader U., Antelmann H., Buder T., Dahl M.K., Hecker M., Homuth G.
    Mol. Genet. Genomics 268:455-467(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis."
    Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R., Mann M.
    Mol. Cell. Proteomics 6:697-707(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: 168.
  12. "Gradual activation of the response regulator DegU controls serial expression of genes for flagellum formation and biofilm formation in Bacillus subtilis."
    Kobayashi K.
    Mol. Microbiol. 66:395-409(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION.
  13. "Bacillus subtilis two-component system sensory kinase DegS is regulated by serine phosphorylation in its input domain."
    Jers C., Kobir A., Sondergaard E.O., Jensen P.R., Mijakovic I.
    PLoS ONE 6:E14653-E14653(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, PHOSPHORYLATION AT SER-76, MUTAGENESIS OF SER-76.

Entry informationi

Entry nameiDEGS_BACSU
AccessioniPrimary (citable) accession number: P13799
Secondary accession number(s): P19590
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: December 1, 1992
Last modified: June 8, 2016
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.