BSRG_BACSU
ID BSRG_BACSU Reviewed; 38 AA.
AC L8EAY0;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Small toxic protein BsrG {ECO:0000303|PubMed:22229825};
GN Name=bsrG {ECO:0000303|PubMed:18948176}; ORFNames=BSU_21546;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
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 [2]
RP IDENTIFICATION, AND INDUCTION.
RC STRAIN=168;
RX PubMed=18948176; DOI=10.1016/j.gene.2008.09.024;
RA Saito S., Kakeshita H., Nakamura K.;
RT "Novel small RNA-encoding genes in the intergenic regions of Bacillus
RT subtilis.";
RL Gene 428:2-8(2009).
RN [3]
RP IDENTIFICATION, AND DISCUSSION OF FUNCTION.
RC STRAIN=168;
RX PubMed=20525796; DOI=10.1093/nar/gkq454;
RA Irnov I., Sharma C.M., Vogel J., Winkler W.C.;
RT "Identification of regulatory RNAs in Bacillus subtilis.";
RL Nucleic Acids Res. 38:6637-6651(2010).
RN [4]
RP FUNCTION AS A TOXIN-ANTITOXIN SYSTEM, INDUCTION, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF 5-GLU--VAL-21; GLU-5; ILE-11; 16-LEU--LYS-38 AND ILE-27.
RC STRAIN=168 / DB104;
RX PubMed=22229825; DOI=10.1111/j.1365-2958.2011.07952.x;
RA Jahn N., Preis H., Wiedemann C., Brantl S.;
RT "BsrG/SR4 from Bacillus subtilis--the first temperature-dependent type I
RT toxin-antitoxin system.";
RL Mol. Microbiol. 83:579-598(2012).
RN [5]
RP INDUCTION.
RC STRAIN=168 / DB104;
RX PubMed=23969414; DOI=10.1093/nar/gkt735;
RA Jahn N., Brantl S.;
RT "One antitoxin--two functions: SR4 controls toxin mRNA decay and
RT translation.";
RL Nucleic Acids Res. 41:9870-9880(2013).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=168 / 1A100;
RX PubMed=26234942; DOI=10.1111/mmi.13146;
RA Jahn N., Brantl S., Strahl H.;
RT "Against the mainstream: the membrane-associated type I toxin BsrG from
RT Bacillus subtilis interferes with cell envelope biosynthesis without
RT increasing membrane permeability.";
RL Mol. Microbiol. 98:651-666(2015).
RN [7]
RP INDUCTION.
RC STRAIN=168 / DB104;
RX PubMed=26802042; DOI=10.1099/mic.0.000247;
RA Jahn N., Brantl S.;
RT "Heat-shock-induced refolding entails rapid degradation of bsrG toxin mRNA
RT by RNases Y and J1.";
RL Microbiology 162:590-599(2016).
CC -!- FUNCTION: Toxic component of a type I toxin-antitoxin (TA) system;
CC expression in the absence of cognate antisense antitoxin SR4 RNA leads
CC to cell lysis (PubMed:22229825, PubMed:23969414). Induced expression
CC causes membrane invaginations that dislocate the cell wall synthesis
CC machinery, leading to eventual death. Unlike many type I TA systems it
CC does not form pores (PubMed:26234942). Base pairing occurs between the
CC 3' UTRs of bsrG mRNA and SR4 RNA, which leads to initiation of
CC degradation by RNase III (rnc) followed by the action of RNase Y (rny)
CC and RNase R (rnr). Not toxic when expressed in E.coli (PubMed:22229825,
CC PubMed:23969414). When induced during logarithmic growth it only slowly
CC exerts its toxic effect. Expression during log growth leads to
CC significant disturbances of cell envelope biosynthesis and cell
CC morphology, causing cell membrane invaginations and delocalization of
CC cell division and cell wall synthesis machinery. Cell lysis depends on
CC mreB, lytC and lytD, suggesting expression of bsrG triggers autolysis
CC rather than disintegration of the membrane. Additionally expression of
CC bsrG also inhibits transcription (PubMed:26234942).
CC {ECO:0000269|PubMed:22229825, ECO:0000269|PubMed:23969414,
CC ECO:0000269|PubMed:26234942}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26234942};
CC Single-pass membrane protein {ECO:0000255}. Note=Fusion of GFP to the
CC C-terminus renders the protein non-toxic but still able to associate
CC with the membrane. {ECO:0000269|PubMed:26234942}.
CC -!- INDUCTION: Accumulates by 4 hours post-innoculation and into stationary
CC phase in rich media; maximum expression occurs at 6 hours
CC (PubMed:18948176). Low expression early in rich and minimal medium,
CC higher expression after. The antitoxin antisense RNA SR4 is
CC constitutively expressed at a constant level in all growth conditions
CC and media tested. bsrG mRNA levels decrease rapidly upon 48 degrees
CC Celsius heat shock (PubMed:22229825, PubMed:26802042). SR4 RNA not only
CC base pairs with bsrG mRNA promoting its degradation, but also inhibits
CC its translation as it sequesters the Shine-Dalgarno sequence
CC (PubMed:23969414). {ECO:0000269|PubMed:18948176,
CC ECO:0000269|PubMed:22229825, ECO:0000269|PubMed:23969414,
CC ECO:0000269|PubMed:26802042}.
CC -!- DISRUPTION PHENOTYPE: Non-essential, it can be deleted. The gene for
CC the antisense antitoxin SR4 RNA cannot be deleted.
CC {ECO:0000269|PubMed:22229825}.
CC -!- MISCELLANEOUS: Encoded in the SPbeta prophage; retention of this TA
CC system may prevent the bacterium from losing SPbeta from its genome.
CC {ECO:0000303|PubMed:22229825}.
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DR EMBL; AL009126; CCQ48598.1; -; Genomic_DNA.
DR RefSeq; WP_009967548.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; L8EAY0; -.
DR STRING; 224308.BSU21546; -.
DR PaxDb; L8EAY0; -.
DR EnsemblBacteria; CCQ48598; CCQ48598; BSU_21546.
DR PATRIC; fig|224308.179.peg.2352; -.
DR BioCyc; BSUB:MON8J2-46; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR031616; BsrE-like.
DR Pfam; PF16935; Hol_Tox; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Toxin-antitoxin system;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..38
FT /note="Small toxic protein BsrG"
FT /id="PRO_0000450220"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MUTAGEN 5..21
FT /note="ESLMIMINFGGLILNTV->QSLMKMINFGGLILNTG: No longer
FT toxic."
FT /evidence="ECO:0000269|PubMed:22229825"
FT MUTAGEN 5
FT /note="E->K: No longer toxic."
FT /evidence="ECO:0000269|PubMed:22229825"
FT MUTAGEN 11
FT /note="I->MIMI: No longer toxic."
FT /evidence="ECO:0000269|PubMed:22229825"
FT MUTAGEN 16..38
FT /note="Missing: No longer toxic."
FT /evidence="ECO:0000269|PubMed:22229825"
FT MUTAGEN 27
FT /note="I->TVLLIFNI: No longer toxic."
FT /evidence="ECO:0000269|PubMed:22229825"
SQ SEQUENCE 38 AA; 4336 MW; F901056DE725D2A4 CRC64;
MTVYESLMIM INFGGLILNT VLLIFNIMMI VTSSQKKK
