(data stored in ACNUC7421 zone)

SWISSPROT: RSBT_BACSU

ID   RSBT_BACSU              Reviewed;         133 AA.
AC   P42411;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   11-DEC-2019, entry version 115.
DE   RecName: Full=Serine/threonine-protein kinase RsbT;
DE            EC=2.7.11.1;
DE   AltName: Full=Anti-sigma-B factor RsbT;
DE   AltName: Full=Switch protein/serine kinase;
GN   Name=rsbT; Synonyms=ycxT; OrderedLocusNames=BSU04690;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC   3610 / VKM B-501;
RX   PubMed=8002610; DOI=10.1128/jb.177.1.123-133.1995;
RA   Wise A.A., Price C.W.;
RT   "Four additional genes in the sigB operon of Bacillus subtilis that control
RT   activity of the general stress factor sigma B in response to environmental
RT   signals.";
RL   J. Bacteriol. 177:123-133(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Kasahara Y., Nakai S., Lee S., Sadaie Y., Ogasawara N.;
RT   "A 148 kbp sequence of the region between 35 and 47 degree of the Bacillus
RT   subtilis genome.";
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 113-133.
RC   STRAIN=168 / BSA46;
RX   PubMed=8002609; DOI=10.1128/jb.177.1.114-122.1995;
RA   Voelker U., Dufour A., Haldenwang W.G.;
RT   "The Bacillus subtilis rsbU gene product is necessary for RsbX-dependent
RT   regulation of sigma B.";
RL   J. Bacteriol. 177:114-122(1995).
RN   [5]
RP   FUNCTION.
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC   3610 / VKM B-501;
RX   PubMed=8824586; DOI=10.1101/gad.10.18.2265;
RA   Yang X., Kang C.M., Brody M.S., Price C.W.;
RT   "Opposing pairs of serine protein kinases and phosphatases transmit signals
RT   of environmental stress to activate a bacterial transcription factor.";
RL   Genes Dev. 10:2265-2275(1996).
RN   [6]
RP   FUNCTION, AND MUTAGENESIS OF ASP-78.
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC   3610 / VKM B-501;
RX   PubMed=9786195; DOI=10.1046/j.1365-2958.1998.01052.x;
RA   Kang C.M., Vijay K., Price C.W.;
RT   "Serine kinase activity of a Bacillus subtilis switch protein is required
RT   to transduce environmental stress signals but not to activate its target
RT   PP2C phosphatase.";
RL   Mol. Microbiol. 30:189-196(1998).
CC   -!- FUNCTION: Provides the crucial link between the upstream module
CC       (communication of environmental stress) and the downstream module
CC       (integration of the environmental signals with signals of energy
CC       stress) that compose the signal transduction pathway controlling the
CC       sigma-B factor. Phosphorylates and inactivates its specific antagonist
CC       protein RsbS thanks to its serine kinase activity. Upon phosphorylation
CC       of RsbS, RsbT is released to stimulate RsbU, a PP2C phosphatase,
CC       thereby initiating the signaling cascade that ultimately activates
CC       sigma-B. The activity of the RsbU phosphatase may be stimulated by a
CC       long-lived interaction with RsbT and the serine kinase function of RsbT
CC       is not required to directly modify RsbU. Also phosphorylates RsbR
CC       thanks to its threonine kinase activity, preventing it to phosphorylate
CC       RsbT. {ECO:0000269|PubMed:8824586, ECO:0000269|PubMed:9786195}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1;
CC   -!- INTERACTION:
CC       P42410:rsbS; NbExp=2; IntAct=EBI-5247957, EBI-5247936;
CC       O31435:ybdM; NbExp=3; IntAct=EBI-5247957, EBI-5255200;
DR   EMBL; L35574; AAA85082.1; -; Genomic_DNA.
DR   EMBL; AB001488; BAA19306.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12276.1; -; Genomic_DNA.
DR   EMBL; X81652; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; G69701; G69701.
DR   RefSeq; NP_388350.1; NC_000964.3.
DR   RefSeq; WP_003246640.1; NZ_JNCM01000031.1.
DR   SMR; P42411; -.
DR   DIP; DIP-402N; -.
DR   IntAct; P42411; 7.
DR   STRING; 224308.BSU04690; -.
DR   PaxDb; P42411; -.
DR   PRIDE; P42411; -.
DR   EnsemblBacteria; CAB12276; CAB12276; BSU04690.
DR   GeneID; 938168; -.
DR   KEGG; bsu:BSU04690; -.
DR   PATRIC; fig|224308.179.peg.497; -.
DR   eggNOG; ENOG4105QD0; Bacteria.
DR   eggNOG; COG2172; LUCA.
DR   HOGENOM; HOG000269930; -.
DR   InParanoid; P42411; -.
DR   KO; K17752; -.
DR   OMA; DQSCVKI; -.
DR   PhylomeDB; P42411; -.
DR   BioCyc; BSUB:BSU04690-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   Pfam; PF13581; HATPase_c_2; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P42411.
DR   SWISS-2DPAGE; P42411.
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..133
FT                   /note="Serine/threonine-protein kinase RsbT"
FT                   /id="PRO_0000097472"
FT   MUTAGEN         78
FT                   /note="D->N: Loss of kinase activity towards RsbS. Loss of
FT                   the ability to activate sigma-B in response to salt and
FT                   ethanol stress while retaining the ability to respond to
FT                   energy stress."
FT                   /evidence="ECO:0000269|PubMed:9786195"
SQ   SEQUENCE   133 AA;  14349 MW;  B9B5CF507F747F7B CRC64;
     MNDQSCVRIM TEWDIVAARQ LGRNVAKELG FGTVDQARIT TAISELARNI YLYAGKGQIG
     IEQVADRGKK GLKIIAEDQG PGIPDIRKVM EDGFSTSGGL GAGLPGVKRL MDEFSLNSVA
     GEGTEIQAIK WLR
//

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