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Anti-sigma-B factor antagonist (Anti-anti-sigma-B factor)

 RSBV_BACSU              Reviewed;         109 AA.
P17903;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
01-NOV-1990, sequence version 1.
16-JAN-2019, entry version 131.
RecName: Full=Anti-sigma-B factor antagonist;
AltName: Full=Anti-anti-sigma-B factor;
Name=rsbV; OrderedLocusNames=BSU04710;
Bacillus subtilis (strain 168).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=224308;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=2170324; DOI=10.1128/jb.172.10.5575-5585.1990;
Kalman S., Duncan M.L., Thomas S.M., Price C.W.;
"Similar organization of the sigB and spoIIA operons encoding
alternate sigma factors of Bacillus subtilis RNA polymerase.";
J. Bacteriol. 172:5575-5585(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=3027048; DOI=10.1128/jb.169.2.771-778.1987;
Duncan M.L., Kalman S.S., Thomas S.M., Price C.W.;
"Gene encoding the 37,000-dalton minor sigma factor of Bacillus
subtilis RNA polymerase: isolation, nucleotide sequence, chromosomal
locus, and cryptic function.";
J. Bacteriol. 169:771-778(1987).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
Kasahara Y., Nakai S., Lee S., Sadaie Y., Ogasawara N.;
"A 148 kbp sequence of the region between 35 and 47 degree of the
Bacillus subtilis genome.";
Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
PubMed=9384377; DOI=10.1038/36786;
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus
subtilis.";
Nature 390:249-256(1997).
[5]
FUNCTION.
STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 /
NCIMB 3610 / VKM B-501;
PubMed=1592822; DOI=10.1128/jb.174.11.3695-3706.1992;
Boylan S.A., Rutherford A., Thomas S.M., Price C.W.;
"Activation of Bacillus subtilis transcription factor sigma B by a
regulatory pathway responsive to stationary-phase signals.";
J. Bacteriol. 174:3695-3706(1992).
[6]
FUNCTION.
STRAIN=PY22;
PubMed=8468294; DOI=10.1128/jb.175.8.2347-2356.1993;
Benson A.K., Haldenwang W.G.;
"Regulation of sigma B levels and activity in Bacillus subtilis.";
J. Bacteriol. 175:2347-2356(1993).
[7]
FUNCTION.
PubMed=8144446; DOI=10.1128/jb.176.7.1813-1820.1994;
Dufour A., Haldenwang W.G.;
"Interactions between a Bacillus subtilis anti-sigma factor (RsbW) and
its antagonist (RsbV).";
J. Bacteriol. 176:1813-1820(1994).
[8]
FUNCTION.
STRAIN=PY22;
PubMed=8808936; DOI=10.1128/jb.178.18.5456-5463.1996;
Voelker U., Voelker A., Haldenwang W.G.;
"Reactivation of the Bacillus subtilis anti-sigma B antagonist, RsbV,
by stress- or starvation-induced phosphatase activities.";
J. Bacteriol. 178:5456-5463(1996).
[9]
MUTAGENESIS OF SER-56.
STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 /
NCIMB 3610 / VKM B-501;
PubMed=8824586; DOI=10.1101/gad.10.18.2265;
Yang X., Kang C.M., Brody M.S., Price C.W.;
"Opposing pairs of serine protein kinases and phosphatases transmit
signals of environmental stress to activate a bacterial transcription
factor.";
Genes Dev. 10:2265-2275(1996).
[10]
SUBUNIT.
STRAIN=SG38;
PubMed=12270815; DOI=10.1128/JB.184.20.5583-5589.2002;
Delumeau O., Lewis R.J., Yudkin M.D.;
"Protein-protein interactions that regulate the energy stress
activation of sigma(B) in Bacillus subtilis.";
J. Bacteriol. 184:5583-5589(2002).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-56 AND THR-57,
AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=168;
PubMed=17218307; DOI=10.1074/mcp.M600464-MCP200;
Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
Mann M.;
"The serine/threonine/tyrosine phosphoproteome of the model bacterium
Bacillus subtilis.";
Mol. Cell. Proteomics 6:697-707(2007).
-!- FUNCTION: Positive regulator of sigma-B activity. Non-
phosphorylated RsbV binds to RsbW, preventing its association with
sigma-B. When phosphorylated, releases RsbW, which is then free to
complex with and inactivate sigma-B. {ECO:0000269|PubMed:1592822,
ECO:0000269|PubMed:8144446, ECO:0000269|PubMed:8468294,
ECO:0000269|PubMed:8808936}.
-!- SUBUNIT: Monomer (Probable). In stressed cells, forms a complex
with RsbW. The predominant form of this complex has a
stoichiometry of 2:2 (one dimer of RsbW is bound by two monomers
of RsbV). Binds to RsbW in the presence of low levels of ATP or
under conditions of energy or environmental stress (through
dephosphorylation by RsbP or RsbU). {ECO:0000269|PubMed:12270815,
ECO:0000305}.
-!- PTM: Phosphorylated by RsbW on a serine residue. Dephosphorylated
by RsbP or RsbU. {ECO:0000269|PubMed:17218307}.
-!- SIMILARITY: Belongs to the anti-sigma-factor antagonist family.
{ECO:0000305}.
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EMBL; M34995; AAA22711.1; -; Genomic_DNA.
EMBL; L35574; AAA85084.1; -; Genomic_DNA.
EMBL; AB001488; BAA19308.1; -; Genomic_DNA.
EMBL; AL009126; CAB12278.1; -; Genomic_DNA.
PIR; A36131; A36131.
RefSeq; NP_388352.1; NC_000964.3.
RefSeq; WP_003234298.1; NZ_JNCM01000031.1.
ProteinModelPortal; P17903; -.
SMR; P17903; -.
BioGrid; 857505; 1.
DIP; DIP-92N; -.
IntAct; P17903; 1.
STRING; 224308.Bsubs1_010100002663; -.
iPTMnet; P17903; -.
jPOST; P17903; -.
PaxDb; P17903; -.
PRIDE; P17903; -.
EnsemblBacteria; CAB12278; CAB12278; BSU04710.
GeneID; 939930; -.
KEGG; bsu:BSU04710; -.
PATRIC; fig|224308.179.peg.499; -.
eggNOG; ENOG4105WN5; Bacteria.
eggNOG; COG1366; LUCA.
HOGENOM; HOG000270156; -.
InParanoid; P17903; -.
KO; K04749; -.
OMA; VYTAPKL; -.
PhylomeDB; P17903; -.
BioCyc; BSUB:BSU04710-MONOMER; -.
Proteomes; UP000001570; Chromosome.
GO; GO:0043856; F:anti-sigma factor antagonist activity; IBA:GO_Central.
GO; GO:0045152; F:antisigma factor binding; IEA:InterPro.
Gene3D; 3.30.750.24; -; 1.
InterPro; IPR003658; Anti-sigma_ant.
InterPro; IPR002645; STAS_dom.
InterPro; IPR036513; STAS_dom_sf.
Pfam; PF01740; STAS; 1.
SUPFAM; SSF52091; SSF52091; 1.
TIGRFAMs; TIGR00377; ant_ant_sig; 1.
PROSITE; PS50801; STAS; 1.
1: Evidence at protein level;
Complete proteome; Phosphoprotein; Reference proteome.
CHAIN 1 109 Anti-sigma-B factor antagonist.
/FTId=PRO_0000194185.
DOMAIN 3 109 STAS. {ECO:0000255|PROSITE-
ProRule:PRU00198}.
MOD_RES 52 52 Phosphoserine.
{ECO:0000269|PubMed:17218307}.
MOD_RES 56 56 Phosphoserine.
{ECO:0000269|PubMed:17218307}.
MOD_RES 57 57 Phosphothreonine.
{ECO:0000269|PubMed:17218307}.
MUTAGEN 56 56 S->A: Loss of phosphorylation. Interacts
strongly with RsbW.
{ECO:0000269|PubMed:8824586}.
MUTAGEN 56 56 S->D: No interaction with RsbW.
{ECO:0000269|PubMed:8824586}.
SEQUENCE 109 AA; 11939 MW; 12CB03E940463F2C CRC64;
MNINVDVKQN ENDIQVNIAG EIDVYSAPVL REKLVPLAEQ GADLRICLKD VSYMDSTGLG
VFVGTFKMVK KQGGSLKLEN LSERLIRLFD ITGLKDIIDI SAKSEGGVQ


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[sigF Rv3286c] RNA polymerase sigma factor SigF (Sigma factor SigF) (Alternative RNA polymerase sigma factor SigF) (RNA polymerase sigma-F factor) (Sigma-F factor) (Stress response/stationary phase sigma factor SigF)
[csfB gin yaaM BSU00240] Anti-sigma-G factor Gin (Protein CsfB)
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[rshA MSMEG_1915 MSMEI_1875] Anti-sigma factor RshA (Regulator of SigH) (Sigma-H anti-sigma factor RshA)
[MPR1] N-acetyltransferase MPR1 (EC 2.3.1.271) ((S)-1-pyrroline-5-carboxylate acetyltransferase) (L-azetidine-2-carboxylate acetyltransferase) (AZC acetyltransferase) (Sigma1278b gene for proline-analog resistance 1)
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[FLO11 MAL5 MUC1 S1 S2 YIR019C] Flocculation protein FLO11 (Flo11p) (Flocculin-11) (Mucin-like protein 1)
[ASF1B] Histone chaperone ASF1B (Anti-silencing function protein 1 homolog B) (hAsf1) (hAsf1b) (CCG1-interacting factor A-II) (CIA-II) (hCIA-II)
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[sigM Rv3911] ECF RNA polymerase sigma factor SigM (ECF sigma factor SigM) (Alternative RNA polymerase sigma factor SigM) (RNA polymerase sigma-M factor) (Sigma-M factor)
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[sigH rpoE MSMEG_1914 MSMEI_1874] ECF RNA polymerase sigma factor SigH (ECF sigma factor SigH) (Alternative RNA polymerase sigma factor SigH) (RNA polymerase sigma-H factor) (Sigma-H factor)
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Bibliography :