(data stored in ACNUC7421 zone)

SWISSPROT: RSBV_BACSU

ID   RSBV_BACSU              Reviewed;         109 AA.
AC   P17903;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   11-DEC-2019, entry version 136.
DE   RecName: Full=Anti-sigma-B factor antagonist;
DE   AltName: Full=Anti-anti-sigma-B factor;
GN   Name=rsbV; OrderedLocusNames=BSU04710;
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;
RX   PubMed=2170324; DOI=10.1128/jb.172.10.5575-5585.1990;
RA   Kalman S., Duncan M.L., Thomas S.M., Price C.W.;
RT   "Similar organization of the sigB and spoIIA operons encoding alternate
RT   sigma factors of Bacillus subtilis RNA polymerase.";
RL   J. Bacteriol. 172:5575-5585(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=3027048; DOI=10.1128/jb.169.2.771-778.1987;
RA   Duncan M.L., Kalman S.S., Thomas S.M., Price C.W.;
RT   "Gene encoding the 37,000-dalton minor sigma factor of Bacillus subtilis
RT   RNA polymerase: isolation, nucleotide sequence, chromosomal locus, and
RT   cryptic function.";
RL   J. Bacteriol. 169:771-778(1987).
RN   [3]
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   [4]
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   [5]
RP   FUNCTION.
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC   3610 / VKM B-501;
RX   PubMed=1592822; DOI=10.1128/jb.174.11.3695-3706.1992;
RA   Boylan S.A., Rutherford A., Thomas S.M., Price C.W.;
RT   "Activation of Bacillus subtilis transcription factor sigma B by a
RT   regulatory pathway responsive to stationary-phase signals.";
RL   J. Bacteriol. 174:3695-3706(1992).
RN   [6]
RP   FUNCTION.
RC   STRAIN=PY22;
RX   PubMed=8468294; DOI=10.1128/jb.175.8.2347-2356.1993;
RA   Benson A.K., Haldenwang W.G.;
RT   "Regulation of sigma B levels and activity in Bacillus subtilis.";
RL   J. Bacteriol. 175:2347-2356(1993).
RN   [7]
RP   FUNCTION.
RX   PubMed=8144446; DOI=10.1128/jb.176.7.1813-1820.1994;
RA   Dufour A., Haldenwang W.G.;
RT   "Interactions between a Bacillus subtilis anti-sigma factor (RsbW) and its
RT   antagonist (RsbV).";
RL   J. Bacteriol. 176:1813-1820(1994).
RN   [8]
RP   FUNCTION.
RC   STRAIN=PY22;
RX   PubMed=8808936; DOI=10.1128/jb.178.18.5456-5463.1996;
RA   Voelker U., Voelker A., Haldenwang W.G.;
RT   "Reactivation of the Bacillus subtilis anti-sigma B antagonist, RsbV, by
RT   stress- or starvation-induced phosphatase activities.";
RL   J. Bacteriol. 178:5456-5463(1996).
RN   [9]
RP   MUTAGENESIS OF SER-56.
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   [10]
RP   SUBUNIT.
RC   STRAIN=SG38;
RX   PubMed=12270815; DOI=10.1128/jb.184.20.5583-5589.2002;
RA   Delumeau O., Lewis R.J., Yudkin M.D.;
RT   "Protein-protein interactions that regulate the energy stress activation of
RT   sigma(B) in Bacillus subtilis.";
RL   J. Bacteriol. 184:5583-5589(2002).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-56 AND THR-57, AND
RP   IDENTIFICATION BY 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: Positive regulator of sigma-B activity. Non-phosphorylated
CC       RsbV binds to RsbW, preventing its association with sigma-B. When
CC       phosphorylated, releases RsbW, which is then free to complex with and
CC       inactivate sigma-B. {ECO:0000269|PubMed:1592822,
CC       ECO:0000269|PubMed:8144446, ECO:0000269|PubMed:8468294,
CC       ECO:0000269|PubMed:8808936}.
CC   -!- SUBUNIT: Monomer (Probable). In stressed cells, forms a complex with
CC       RsbW. The predominant form of this complex has a stoichiometry of 2:2
CC       (one dimer of RsbW is bound by two monomers of RsbV). Binds to RsbW in
CC       the presence of low levels of ATP or under conditions of energy or
CC       environmental stress (through dephosphorylation by RsbP or RsbU).
CC       {ECO:0000269|PubMed:12270815, ECO:0000305}.
CC   -!- PTM: Phosphorylated by RsbW on a serine residue. Dephosphorylated by
CC       RsbP or RsbU. {ECO:0000269|PubMed:17218307}.
CC   -!- SIMILARITY: Belongs to the anti-sigma-factor antagonist family.
CC       {ECO:0000305}.
DR   EMBL; M34995; AAA22711.1; -; Genomic_DNA.
DR   EMBL; L35574; AAA85084.1; -; Genomic_DNA.
DR   EMBL; AB001488; BAA19308.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12278.1; -; Genomic_DNA.
DR   PIR; A36131; A36131.
DR   RefSeq; NP_388352.1; NC_000964.3.
DR   RefSeq; WP_003234298.1; NZ_JNCM01000031.1.
DR   SMR; P17903; -.
DR   BioGrid; 857505; 1.
DR   DIP; DIP-92N; -.
DR   IntAct; P17903; 1.
DR   STRING; 224308.BSU04710; -.
DR   iPTMnet; P17903; -.
DR   jPOST; P17903; -.
DR   PaxDb; P17903; -.
DR   PRIDE; P17903; -.
DR   EnsemblBacteria; CAB12278; CAB12278; BSU04710.
DR   GeneID; 939930; -.
DR   KEGG; bsu:BSU04710; -.
DR   PATRIC; fig|224308.179.peg.499; -.
DR   eggNOG; ENOG4105WN5; Bacteria.
DR   eggNOG; COG1366; LUCA.
DR   HOGENOM; HOG000270156; -.
DR   InParanoid; P17903; -.
DR   KO; K04749; -.
DR   OMA; MNLAINI; -.
DR   PhylomeDB; P17903; -.
DR   BioCyc; BSUB:BSU04710-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0043856; F:anti-sigma factor antagonist activity; IBA:GO_Central.
DR   Gene3D; 3.30.750.24; -; 1.
DR   InterPro; IPR003658; Anti-sigma_ant.
DR   InterPro; IPR002645; STAS_dom.
DR   InterPro; IPR036513; STAS_dom_sf.
DR   Pfam; PF01740; STAS; 1.
DR   SUPFAM; SSF52091; SSF52091; 1.
DR   TIGRFAMs; TIGR00377; ant_ant_sig; 1.
DR   PROSITE; PS50801; STAS; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P17903.
DR   SWISS-2DPAGE; P17903.
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..109
FT                   /note="Anti-sigma-B factor antagonist"
FT                   /id="PRO_0000194185"
FT   DOMAIN          3..109
FT                   /note="STAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT   MOD_RES         52
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:17218307"
FT   MOD_RES         56
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:17218307"
FT   MOD_RES         57
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:17218307"
FT   MUTAGEN         56
FT                   /note="S->A: Loss of phosphorylation. Interacts strongly
FT                   with RsbW."
FT                   /evidence="ECO:0000269|PubMed:8824586"
FT   MUTAGEN         56
FT                   /note="S->D: No interaction with RsbW."
FT                   /evidence="ECO:0000269|PubMed:8824586"
SQ   SEQUENCE   109 AA;  11939 MW;  12CB03E940463F2C CRC64;
     MNINVDVKQN ENDIQVNIAG EIDVYSAPVL REKLVPLAEQ GADLRICLKD VSYMDSTGLG
     VFVGTFKMVK KQGGSLKLEN LSERLIRLFD ITGLKDIIDI SAKSEGGVQ
//

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