(data stored in ACNUC7421 zone)

SWISSPROT: RSBS_BACSU

ID   RSBS_BACSU              Reviewed;         121 AA.
AC   P42410;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   11-DEC-2019, entry version 119.
DE   RecName: Full=RsbT antagonist protein RsbS;
DE   AltName: Full=Stressosome protein RsbS;
GN   Name=rsbS; Synonyms=ycxS; OrderedLocusNames=BSU04680;
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   FUNCTION, PHOSPHORYLATION AT SER-59, AND MUTAGENESIS OF SER-59.
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   [5]
RP   FUNCTION, PHOSPHORYLATION AT SER-59, AND MUTAGENESIS OF SER-59.
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC   3610 / VKM B-501;
RX   PubMed=8682789; DOI=10.1128/jb.178.13.3846-3853.1996;
RA   Kang C.M., Brody M.S., Akbar S., Yang X., Price C.W.;
RT   "Homologous pairs of regulatory proteins control activity of Bacillus
RT   subtilis transcription factor sigma(b) in response to environmental
RT   stress.";
RL   J. Bacteriol. 178:3846-3853(1996).
RN   [6]
RP   FUNCTION, SUBUNIT, AND REQUIREMENT FOR RSBR PARALOG.
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC   3610 / VKM B-501;
RX   PubMed=15312768; DOI=10.1016/j.jmb.2004.05.043;
RA   Kim T.-J., Gaidenko T.A., Price C.W.;
RT   "A multicomponent protein complex mediates environmental stress signaling
RT   in Bacillus subtilis.";
RL   J. Mol. Biol. 341:135-150(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, 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).
CC   -!- FUNCTION: Negative regulator of sigma-B activity. Non-phosphorylated
CC       RsbS binds to RsbT, preventing its association with RsbU. Requires any
CC       one of RsbRA, RsbRB, RsbRC or RsbRD to sequester RsbT. When RsbS and
CC       the RsbR paralog(s) are phosphorylated, they release RsbT, which can
CC       then bind and activate RsbU. {ECO:0000269|PubMed:15312768,
CC       ECO:0000269|PubMed:8682789, ECO:0000269|PubMed:8824586}.
CC   -!- SUBUNIT: Interacts with RsbRA, RsbRB in the stressosome. The
CC       stressosome probably also contains RsbRC and RsbRD.
CC       {ECO:0000269|PubMed:15312768}.
CC   -!- INTERACTION:
CC       P42411:rsbT; NbExp=2; IntAct=EBI-5247936, EBI-5247957;
CC   -!- PTM: Phosphorylated by RsbT. Dephosphorylated by RsbX.
CC       {ECO:0000269|PubMed:17218307, ECO:0000269|PubMed:8682789,
CC       ECO:0000269|PubMed:8824586}.
DR   EMBL; L35574; AAA85081.1; -; Genomic_DNA.
DR   EMBL; AB001488; BAA19305.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12275.1; -; Genomic_DNA.
DR   PIR; F69701; F69701.
DR   RefSeq; NP_388349.1; NC_000964.3.
DR   RefSeq; WP_003225190.1; NZ_JNCM01000031.1.
DR   SMR; P42410; -.
DR   DIP; DIP-382N; -.
DR   IntAct; P42410; 3.
DR   STRING; 224308.BSU04680; -.
DR   iPTMnet; P42410; -.
DR   jPOST; P42410; -.
DR   PaxDb; P42410; -.
DR   PRIDE; P42410; -.
DR   DNASU; 938157; -.
DR   EnsemblBacteria; CAB12275; CAB12275; BSU04680.
DR   GeneID; 938157; -.
DR   KEGG; bsu:BSU04680; -.
DR   PATRIC; fig|224308.179.peg.496; -.
DR   eggNOG; ENOG4105FUA; Bacteria.
DR   eggNOG; COG1366; LUCA.
DR   HOGENOM; HOG000269818; -.
DR   InParanoid; P42410; -.
DR   KO; K17762; -.
DR   OMA; MSNLMGA; -.
DR   PhylomeDB; P42410; -.
DR   BioCyc; BSUB:BSU04680-MONOMER; -.
DR   PRO; PR:P42410; -.
DR   Proteomes; UP000001570; Chromosome.
DR   Gene3D; 3.30.750.24; -; 1.
DR   InterPro; IPR002645; STAS_dom.
DR   InterPro; IPR036513; STAS_dom_sf.
DR   Pfam; PF01740; STAS; 1.
DR   SUPFAM; SSF52091; SSF52091; 1.
DR   PROSITE; PS50801; STAS; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P42410.
DR   SWISS-2DPAGE; P42410.
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..121
FT                   /note="RsbT antagonist protein RsbS"
FT                   /id="PRO_0000097471"
FT   DOMAIN          4..115
FT                   /note="STAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT   MOD_RES         59
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:17218307,
FT                   ECO:0000269|PubMed:8682789, ECO:0000269|PubMed:8824586"
FT   MUTAGEN         59
FT                   /note="S->A: Loss of phosphorylation and loss of the
FT                   ability to respond to salt stress. Interacts strongly with
FT                   RsbT."
FT                   /evidence="ECO:0000269|PubMed:8682789,
FT                   ECO:0000269|PubMed:8824586"
FT   MUTAGEN         59
FT                   /note="S->D: Loss of interaction with RsbT."
FT                   /evidence="ECO:0000269|PubMed:8682789,
FT                   ECO:0000269|PubMed:8824586"
SQ   SEQUENCE   121 AA;  13311 MW;  64BF3EF7D4A81CDA CRC64;
     MRHPKIPILK LYNCLLVSIQ WELDDQTALT FQEDLLNKIY ETGANGVVID LTSVDMIDSF
     IAKVLGDVIT MSKLMGAKVV LTGIQPAVAV TLIELGIALE EIETALDLEQ GLETLKRELG
     E
//

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