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 03-AUG-2022, entry version 146.
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 / NRRL NRS-744 / 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 / NRRL NRS-744 / 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 PDB; 6M36; X-ray; 3.40 A; B/D/F/H/J/L/N/P=2-104.
DR PDB; 6M37; X-ray; 3.10 A; B/D=2-104.
DR PDBsum; 6M36; -.
DR PDBsum; 6M37; -.
DR AlphaFoldDB; P17903; -.
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; BSU_04710.
DR GeneID; 939930; -.
DR KEGG; bsu:BSU04710; -.
DR PATRIC; fig|224308.179.peg.499; -.
DR eggNOG; COG1366; Bacteria.
DR InParanoid; P17903; -.
DR OMA; MNLAINI; -.
DR PhylomeDB; P17903; -.
DR BioCyc; BSUB:BSU04710-MON; -.
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;
KW 3D-structure; 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"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:6M37"
FT STRAND 13..23
FT /evidence="ECO:0007829|PDB:6M37"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:6M37"
FT HELIX 27..39
FT /evidence="ECO:0007829|PDB:6M37"
FT STRAND 44..54
FT /evidence="ECO:0007829|PDB:6M37"
FT HELIX 56..71
FT /evidence="ECO:0007829|PDB:6M37"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:6M37"
FT HELIX 83..91
FT /evidence="ECO:0007829|PDB:6M37"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:6M37"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:6M37"
SQ SEQUENCE 109 AA; 11939 MW; 12CB03E940463F2C CRC64;
MNINVDVKQN ENDIQVNIAG EIDVYSAPVL REKLVPLAEQ GADLRICLKD VSYMDSTGLG
VFVGTFKMVK KQGGSLKLEN LSERLIRLFD ITGLKDIIDI SAKSEGGVQ
