YOBL_BACSU
ID YOBL_BACSU Reviewed; 600 AA.
AC O34330; Q796E2;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Toxin YobL {ECO:0000303|PubMed:22200572};
DE AltName: Full=DNase YobL {ECO:0000303|PubMed:34280190};
GN Name=yobL; OrderedLocusNames=BSU19000;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequence analysis of the Bacillus subtilis chromosome region between the
RT terC and odhAB loci cloned in a yeast artificial chromosome.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP INCORRECT FUNCTION AS AN RNASE, FUNCTION AS A TOXIN, INTERACTION WITH YOBK,
RP AND EXPRESSION IN E.COLI.
RC STRAIN=168;
RX PubMed=22200572; DOI=10.1016/j.febslet.2011.12.020;
RA Holberger L.E., Garza-Sanchez F., Lamoureux J., Low D.A., Hayes C.S.;
RT "A novel family of toxin/antitoxin proteins in Bacillus species.";
RL FEBS Lett. 586:132-136(2012).
RN [4]
RP FUNCTION AS A TOXIN, FUNCTION AS A DNASE, SUBCELLULAR LOCATION, INDUCTION,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=34280190; DOI=10.1371/journal.pgen.1009682;
RA Kobayashi K.;
RT "Diverse LXG toxin and antitoxin systems specifically mediate intraspecies
RT competition in Bacillus subtilis biofilms.";
RL PLoS Genet. 17:e1009682-e1009682(2021).
CC -!- FUNCTION: Toxic component of one of 6 LXG toxin-immunity modules in
CC this strain. They promote kin selection, mediate competition in
CC biofilms, and drive spatial segregation of different strains,
CC indicating that LXG toxins may help avoid warfare between strains in
CC biofilms. Mediates intercellular competition during biofilm formation;
CC disruption of the operon disadvantages the bacteria, but overexpression
CC of the cognate immunity protein restores growth in competition with
CC wild-type. Overexpression alone in situ causes growth arrest but not
CC cell lysis, a large decrease in chromosomal DNA content and the
CC production of anucleate cells. No effect is seen on rRNA. Co-
CC overexpression with cognate immunity protein YobK does not cause growth
CC arrest. The toxic effect is dependent on the epsA and tapA operons
CC which are required for biofilm formation.
CC {ECO:0000269|PubMed:34280190}.
CC -!- SUBUNIT: Interacts with cognate immunity protein YobK but not with non-
CC cognate putative immunity protein YezG. The interaction inhibits the
CC toxic activity of YobL. {ECO:0000269|PubMed:22200572}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:34280190}.
CC Note=Delivery to target cells requires the type VII secretion system
CC (T7SS) and YukE. {ECO:0000269|PubMed:34280190}.
CC -!- INDUCTION: Expressed on rich and minimal solid media likely in early
CC stationary phase; not dependent on DegSU. Not expressed in liquid LB,
CC but only under conditions that promote biofilm formation.
CC {ECO:0000269|PubMed:34280190}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the yobL-yobK operon has no visible
CC growth phenotype, however it is out-competed by wild-type cells.
CC {ECO:0000269|PubMed:34280190}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the LXG family.
CC {ECO:0000303|PubMed:22200572}.
CC -!- CAUTION: Was originally thought to be an RNase; when the C-terminus
CC (residues 449-600) is expressed in E.coli it has RNase, not DNase
CC activity, and inhibits growth upon expression in E.coli. In vitro RNase
CC activity and in vivo growth inhibition are neutralized by cognate
CC immunity protein YobK, but not by immunity proteins specific to other
CC LXG toxins. Mutation of His-562 to Ala leads to loss of growth
CC inhibition and RNase activity in E.coli. {ECO:0000269|PubMed:22200572}.
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DR EMBL; AF027868; AAB84464.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13792.1; -; Genomic_DNA.
DR PIR; C69899; C69899.
DR RefSeq; NP_389781.1; NC_000964.3.
DR RefSeq; WP_004399481.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; O34330; -.
DR IntAct; O34330; 1.
DR MINT; O34330; -.
DR STRING; 224308.BSU19000; -.
DR PaxDb; O34330; -.
DR PRIDE; O34330; -.
DR EnsemblBacteria; CAB13792; CAB13792; BSU_19000.
DR GeneID; 939624; -.
DR KEGG; bsu:BSU19000; -.
DR PATRIC; fig|224308.179.peg.2078; -.
DR eggNOG; COG5444; Bacteria.
DR OMA; MKNGNAP; -.
DR PhylomeDB; O34330; -.
DR BioCyc; BSUB:BSU19000-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR InterPro; IPR026834; LHH.
DR InterPro; IPR006829; LXG_dom.
DR Pfam; PF14411; LHH; 1.
DR Pfam; PF04740; LXG; 1.
DR PROSITE; PS51756; LXG; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Hydrolase; Nuclease; Reference proteome; Secreted; Toxin.
FT CHAIN 1..600
FT /note="Toxin YobL"
FT /id="PRO_0000360800"
FT DOMAIN 1..235
FT /note="LXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01092"
FT COILED 12..40
FT /evidence="ECO:0000255"
FT COILED 141..176
FT /evidence="ECO:0000255"
SQ SEQUENCE 600 AA; 67770 MW; 59D3A3A69B97B6CC CRC64;
MKVFEADSLL FEADKRTKEY KELRSQMVKL KKAFKEVANL DDSEFSGKGA DNIKAFYHGH
VGVTDQWIDL IDMKIAFLSS MSATLEDAKM SDAYIEESFL EHELANAYAK SKSIMSEQKK
AMKDILNNIN DILPLEIFST EDFKDKLSSA DDKREKTIDK LNKLDEDLKT EYAETEPNEQ
FIQQDFKKLQ ESTGKGKNAT PIHYNAKAYR ESDIHKKKGD IEKHSEAYLS VKKEEAKERE
IKELKKKLND GVSDPDEYLE IAKKVGYENL EPTQVQLAVQ IEQAKQLEGA GEITWDIVKG
VGVGLYDVGK DTVTGIWDFI TDPGETLSAL GNAAMHPVKT YDAISAAIEE SYQKDMVNGD
AYSRSRWVTY AIGSVAVAVV GTKGAGAINK ADAAGKVINK ASQAGKKIKD VKIPDLLPYN
PKYKLALADN VPYNVVDSQN LKNELLTNAK KIPDGTRKPF TGQKKSPPWL NKEKYDAYEI
EGKVKAKGKV KDVSRRVYTM KDIDINQKTE FGVTNLQLMK NGNAPYAKDG TQINLHHLIQ
EEPGPMLEIP NSLHTKYSDV IHQLKSDGES FRNDKVLKAQ YESFRKRYWK WRAKQFENEN
