DEGU_BACSU
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 03-AUG-2022, entry version 150.
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 positive
RT and negative effects on production of extracellular 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 genes
RT with similarities to the conserved procaryotic family of two-component
RT 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., 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 [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 subtilis
RT 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., 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 [6]
RP FUNCTION, AND PHOSPHORYLATION BY DEGS.
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, 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 MUTAGENESIS
RP OF HIS-12 AND ASP-56.
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 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 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 DegS-
RT 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 OF
RP 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. 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, biofilm formation, and competence for
CC DNA uptake. Positively or negatively regulates expression of many
CC different genes. The phosphorylated form is required for synthesis of
CC degradative enzymes, flagellum formation and biofilm formation. The
CC unphosphorylated form is required for expression of genetic competence,
CC via induction of comK. {ECO:0000269|PubMed:12471443,
CC ECO:0000269|PubMed:1321152, ECO:0000269|PubMed:17850253,
CC ECO:0000269|PubMed:1901568, ECO:0000269|PubMed:2123196,
CC ECO:0000269|PubMed:8955341}.
CC -!- ACTIVITY REGULATION: Phosphorylated and unphosphorylated forms are both
CC active and have different functions. A low concentration of phospho-
CC DegU is sufficient to activate transcription of flagellar genes, but a
CC higher concentration of phospho-DegU is required for transcription of
CC other genes. Phosphorylated DegU is stabilized by DegR.
CC {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}.
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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 AlphaFoldDB; P13800; -.
DR SMR; P13800; -.
DR STRING; 224308.BSU35490; -.
DR jPOST; P13800; -.
DR PaxDb; P13800; -.
DR PRIDE; P13800; -.
DR EnsemblBacteria; CAB15566; CAB15566; BSU_35490.
DR GeneID; 64305306; -.
DR GeneID; 66324749; -.
DR GeneID; 936751; -.
DR KEGG; bsu:BSU35490; -.
DR PATRIC; fig|224308.179.peg.3840; -.
DR eggNOG; COG2197; Bacteria.
DR InParanoid; P13800; -.
DR OMA; HPMWRDG; -.
DR PhylomeDB; P13800; -.
DR BioCyc; BSUB:BSU35490-MON; -.
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:0045893; P:positive regulation of transcription, DNA-templated; IMP:CACAO.
DR CDD; cd06170; LuxR_C_like; 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; Cytoplasm; DNA-binding; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation;
KW Two-component regulatory system.
FT CHAIN 1..229
FT /note="Transcriptional regulatory protein DegU"
FT /id="PRO_0000081099"
FT DOMAIN 5..121
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 159..224
FT /note="HTH luxR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00411"
FT DNA_BIND 183..202
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00411"
FT MOD_RES 56
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000305"
FT MUTAGEN 12
FT /note="H->L: Increases the stability of phosphorylated
FT form."
FT /evidence="ECO:0000269|PubMed:1321152,
FT ECO:0000269|PubMed:1901568"
FT MUTAGEN 56
FT /note="D->A: Prevents both swarming motility and pellicle
FT formation."
FT /evidence="ECO:0000269|PubMed:1321152,
FT ECO:0000269|PubMed:17850253, ECO:0000269|PubMed:1901568"
FT MUTAGEN 56
FT /note="D->N: Lack of phosphorylation. Decreases degradative
FT enzyme production, but allows full expression of late
FT competence genes."
FT /evidence="ECO:0000269|PubMed:1321152,
FT ECO:0000269|PubMed:17850253, ECO:0000269|PubMed:1901568"
FT MUTAGEN 98
FT /note="T->I: Increases phosphorylation."
FT /evidence="ECO:0000269|PubMed:1901568"
FT MUTAGEN 131
FT /note="V->L: Increases phosphorylation."
FT /evidence="ECO:0000269|PubMed:1901568"
FT MUTAGEN 184
FT /note="R->C: Does not affect phosphorylation."
FT /evidence="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
