ID   BSRE_BACSU              Reviewed;          30 AA.
AC   A0A2K4Z9J5;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   28-MAR-2018, sequence version 1.
DT   03-AUG-2022, entry version 11.
DE   RecName: Full=Small toxic protein BsrE {ECO:0000303|PubMed:26565032};
GN   Name=bsrE {ECO:0000303|PubMed:18948176}; ORFNames=BSU_18978;
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.
RC   STRAIN=168 / DB104;
RX   PubMed=26565032; DOI=10.1074/jbc.m115.697524;
RA   Meissner C., Jahn N., Brantl S.;
RT   "In Vitro Characterization of the Type I Toxin-Antitoxin System bsrE/SR5
RT   from Bacillus subtilis.";
RL   J. Biol. Chem. 291:560-571(2016).
RN   [5]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168 / DB104;
RX   PubMed=26940229; DOI=10.1080/15476286.2016.1156288;
RA   Mueller P., Jahn N., Ring C., Maiwald C., Neubert R., Meissner C.,
RA   Brantl S.;
RT   "A multistress responsive type I toxin-antitoxin system: bsrE/SR5 from the
RT   B. subtilis chromosome.";
RL   RNA Biol. 13:511-523(2016).
CC   -!- FUNCTION: Toxic component of a type I toxin-antitoxin (TA) system;
CC       overexpression in the absence of cognate antisense antitoxin SR5 RNA
CC       leads to cell lysis (PubMed:26565032, PubMed:26940229). Base pairing
CC       occurs between the 3' UTRs of bsrE mRNA and SR5 RNA which leads to bsrE
CC       mRNA degradation initiated by RNase III (rnc) and RNase J1 (rnjA)
CC       (PubMed:26940229). Genetic evidence suggests an unidentified RNA-
CC       binding protein may exist that promotes TA RNA interaction
CC       (PubMed:26565032). {ECO:0000269|PubMed:26565032,
CC       ECO:0000269|PubMed:26940229}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Accumulates by 2 hours post-innoculation with maximal
CC       expression at 4 hours, and has disappeared by 8 hours in rich media
CC       (PubMed:18948176). Slightly different results were found in another
CC       study; in rich medium, expression increased slowly over time and was
CC       maximal at 6 hours. In minimal medium without glucose expression
CC       decreased as growth progressed, while in minimal medium plus glucose
CC       expression was constant during growth. SR5 antitoxin RNA is always
CC       present at levels equal to or in excess of toxin mRNA. Responds to a
CC       number of different stresses; ethanol, methanol and isopropanol and pH
CC       9.1 stress cause a rapid loss of bsrE and SR5 mRNA, Fe(2+) limitation
CC       and pH 5.3 stress increases the SR5 RNA while oxygen depletion
CC       decreases SR5 with no effect on bsrE mRNA. Heat shock at 48 degrees
CC       Celsius causes a gradual decrease in bsrG mRNA (PubMed:26940229).
CC       {ECO:0000269|PubMed:18948176, ECO:0000269|PubMed:26940229}.
CC   -!- DISRUPTION PHENOTYPE: Non-essential, it can be deleted on rich medium;
CC       the gene for the antisense antitoxin SR5 RNA can also be deleted
CC       without a visible phenotype. {ECO:0000269|PubMed:26940229}.
CC   -!- MISCELLANEOUS: Encoded in the prophage-like P6 region. {ECO:0000305}.
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DR   EMBL; AL009126; SOX90563.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K4Z9J5; -.
DR   EnsemblBacteria; SOX90563; SOX90563; BSU_18978.
DR   BioCyc; BSUB:MON8J2-55; -.
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..30
FT                   /note="Small toxic protein BsrE"
FT                   /id="PRO_0000450219"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   30 AA;  3358 MW;  F3C4F5705DAAF8C0 CRC64;
     MSTFQALMLM LAIGSFIIAL LTYIEKIDLP