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Database: UniProt
Entry: P13800
LinkDB: P13800
Original site: P13800 
ID   DEGU_BACSU              Reviewed;         229 AA.
AC   P13800;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 2.
DT   18-SEP-2019, entry version 139.
DE   RecName: Full=Transcriptional regulatory protein DegU;
DE   AltName: Full=Protease production enhancer protein;
GN   Name=degU; Synonyms=iep; OrderedLocusNames=BSU35490;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DOMAIN.
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
RT   positive and negative effects on production of extracellular
RT   proteases.";
RL   J. Bacteriol. 170:3593-3600(1988).
RN   [2]
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
RT   genes with similarities to the conserved procaryotic family of two-
RT   component signalling systems.";
RL   J. Bacteriol. 170:5102-5109(1988).
RN   [3]
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.,
RA   Karamata D., Klier A., Rapoport G., Dedonder R.;
RT   "Deduced polypeptides encoded by the Bacillus subtilis sacU locus
RT   share homology with two-component sensor-regulator systems.";
RL   J. Bacteriol. 170:5093-5101(1988).
RN   [4]
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
RT   subtilis chromosome.";
RL   Microbiology 142:3079-3088(1996).
RN   [5]
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.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   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.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   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   [6]
RP   FUNCTION, AND PHOSPHORYLATION BY DEGS.
RC   STRAIN=168 / CU741;
RX   PubMed=2123196;
RA   Mukai K., Kawata M., Tanaka T.;
RT   "Isolation and phosphorylation of the Bacillus subtilis degS and degU
RT   gene products.";
RL   J. Biol. Chem. 265:20000-20006(1990).
RN   [7]
RP   FUNCTION, PHOSPHORYLATION BY DEGS, AND MUTAGENESIS OF HIS-12; ASP-56;
RP   THR-98; VAL-131 AND ARG-184.
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   ACTIVITY REGULATION.
RX   PubMed=1459944; DOI=10.1128/jb.174.24.7954-7962.1992;
RA   Mukai K., Kawata-Mukai M., Tanaka T.;
RT   "Stabilization of phosphorylated Bacillus subtilis DegU by DegR.";
RL   J. Bacteriol. 174:7954-7962(1992).
RN   [9]
RP   FUNCTION, ACTIVITY REGULATION, DEPHOSPHORYLATION BY DEGS, AND
RP   MUTAGENESIS OF HIS-12 AND ASP-56.
RX   PubMed=1321152;
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
RT   expression of genetic competence in Bacillus subtilis.";
RL   J. Biol. Chem. 267:14509-14514(1992).
RN   [10]
RP   FUNCTION IN COMK EXPRESSION.
RC   STRAIN=168 / CU741;
RX   PubMed=8955341; DOI=10.1016/s0014-5793(96)01170-2;
RA   Ogura M., Tanaka T.;
RT   "Bacillus subtilis DegU acts as a positive regulator for comK
RT   expression.";
RL   FEBS Lett. 397:173-176(1996).
RN   [11]
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
RT   DegS-DegU regulon by transcriptomics and proteomics.";
RL   Mol. Genet. Genomics 268:455-467(2002).
RN   [12]
RP   FUNCTION, DNA-BINDING, ACTIVITY REGULATION, INDUCTION, AND MUTAGENESIS
RP   OF ASP-56.
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).
CC   -!- FUNCTION: Member of the two-component regulatory system DegS/DegU,
CC       which plays an important role in the transition growth phase.
CC       Involved in the control of expression of different cellular
CC       functions, including production of degradative enzymes such as the
CC       neutral and alkaline proteases, flagellum formation, biofilm
CC       formation, and competence for DNA uptake. Positively or negatively
CC       regulates expression of many different genes. The phosphorylated
CC       form is required for synthesis of degradative enzymes, flagellum
CC       formation and biofilm formation. The unphosphorylated form is
CC       required for expression of genetic competence, via induction of
CC       comK. {ECO:0000269|PubMed:12471443, ECO:0000269|PubMed:1321152,
CC       ECO:0000269|PubMed:17850253, ECO:0000269|PubMed:1901568,
CC       ECO:0000269|PubMed:2123196, ECO:0000269|PubMed:8955341}.
CC   -!- ACTIVITY REGULATION: Phosphorylated and unphosphorylated forms are
CC       both active and have different functions. A low concentration of
CC       phospho-DegU is sufficient to activate transcription of flagellar
CC       genes, but a higher concentration of phospho-DegU is required for
CC       transcription of other genes. Phosphorylated DegU is stabilized by
CC       DegR. {ECO:0000269|PubMed:1321152, ECO:0000269|PubMed:1459944,
CC       ECO:0000269|PubMed:17850253}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: Phosphorylated DegU activates its own expression.
CC       {ECO:0000269|PubMed:17850253}.
CC   -!- DOMAIN: The N-terminal region acts as an inhibitor, whereas the C-
CC       terminal region carries enhancing activity.
CC       {ECO:0000269|PubMed:3136143}.
CC   -!- PTM: Phosphorylated and dephosphorylated by DegS.
CC       {ECO:0000269|PubMed:1901568, ECO:0000269|PubMed:2123196}.
DR   EMBL; M21658; AAA22545.1; -; Genomic_DNA.
DR   EMBL; M23558; AAA22733.1; -; Genomic_DNA.
DR   EMBL; M23649; AAA22735.1; -; Genomic_DNA.
DR   EMBL; U56901; AAC44938.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15566.1; -; Genomic_DNA.
DR   PIR; C30191; RGBSXD.
DR   RefSeq; NP_391429.1; NC_000964.3.
DR   RefSeq; WP_003219701.1; NZ_JNCM01000033.1.
DR   SMR; P13800; -.
DR   STRING; 224308.BSU35490; -.
DR   jPOST; P13800; -.
DR   PaxDb; P13800; -.
DR   PRIDE; P13800; -.
DR   EnsemblBacteria; CAB15566; CAB15566; BSU35490.
DR   GeneID; 936751; -.
DR   GeneID; 9778660; -.
DR   KEGG; bsu:BSU35490; -.
DR   PATRIC; fig|224308.179.peg.3840; -.
DR   eggNOG; ENOG4105WH1; Bacteria.
DR   eggNOG; COG2197; LUCA.
DR   HOGENOM; HOG000034813; -.
DR   InParanoid; P13800; -.
DR   KO; K07692; -.
DR   OMA; DHPMWRD; -.
DR   PhylomeDB; P13800; -.
DR   BioCyc; BSUB:BSU35490-MONOMER; -.
DR   PRO; PR:P13800; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd06170; LuxR_C_like; 1.
DR   CDD; cd00156; REC; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR000792; Tscrpt_reg_LuxR_C.
DR   Pfam; PF00196; GerE; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00038; HTHLUXR.
DR   SMART; SM00421; HTH_LUXR; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF46894; SSF46894; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   PROSITE; PS00622; HTH_LUXR_1; 1.
DR   PROSITE; PS50043; HTH_LUXR_2; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   1: Evidence at protein level;
KW   Activator; Complete proteome; Cytoplasm; DNA-binding; Phosphoprotein;
KW   Reference proteome; Repressor; Transcription;
KW   Transcription regulation; Two-component regulatory system.
FT   CHAIN         1    229       Transcriptional regulatory protein DegU.
FT                                /FTId=PRO_0000081099.
FT   DOMAIN        5    121       Response regulatory.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00169}.
FT   DOMAIN      159    224       HTH luxR-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00411}.
FT   DNA_BIND    183    202       H-T-H motif. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00411}.
FT   MOD_RES      56     56       4-aspartylphosphate. {ECO:0000305}.
FT   MUTAGEN      12     12       H->L: Increases the stability of
FT                                phosphorylated form.
FT                                {ECO:0000269|PubMed:1321152,
FT                                ECO:0000269|PubMed:1901568}.
FT   MUTAGEN      56     56       D->A: Prevents both swarming motility and
FT                                pellicle formation.
FT                                {ECO:0000269|PubMed:1321152,
FT                                ECO:0000269|PubMed:17850253,
FT                                ECO:0000269|PubMed:1901568}.
FT   MUTAGEN      56     56       D->N: Lack of phosphorylation. Decreases
FT                                degradative enzyme production, but allows
FT                                full expression of late competence genes.
FT                                {ECO:0000269|PubMed:1321152,
FT                                ECO:0000269|PubMed:17850253,
FT                                ECO:0000269|PubMed:1901568}.
FT   MUTAGEN      98     98       T->I: Increases phosphorylation.
FT                                {ECO:0000269|PubMed:1901568}.
FT   MUTAGEN     131    131       V->L: Increases phosphorylation.
FT                                {ECO:0000269|PubMed:1901568}.
FT   MUTAGEN     184    184       R->C: Does not affect phosphorylation.
FT                                {ECO:0000269|PubMed:1901568}.
SQ   SEQUENCE   229 AA;  25867 MW;  F059DC9237DC264A CRC64;
     MTKVNIVIID DHQLFREGVK RILDFEPTFE VVAEGDDGDE AARIVEHYHP DVVIMDINMP
     NVNGVEATKQ LVELYPESKV IILSIHDDEN YVTHALKTGA RGYLLKEMDA DTLIEAVKVV
     AEGGSYLHPK VTHNLVNEFR RLATSGVSAH PQHEVYPEIR RPLHILTRRE CEVLQMLADG
     KSNRGIGESL FISEKTVKNH VSNILQKMNV NDRTQAVVVA IKNGWVEMR
//
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