YOKI_BACSU
ID YOKI_BACSU Reviewed; 571 AA.
AC O31998;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Toxin YokI {ECO:0000303|PubMed:22200572};
DE AltName: Full=DNase YokL {ECO:0000303|PubMed:34280190};
DE AltName: Full=SPbeta prophage-derived protein YokI;
GN Name=yokI; OrderedLocusNames=BSU21580;
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 SEQUENCE REVISION TO 49.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [3]
RP FUNCTION AS A TOXIN, 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 YokJ does not cause growth
CC arrest. The toxic effect is dependent on the epsA and tapA operons
CC which are required for biofilm formation (PubMed:34280190). The C-
CC terminus (residues 449-571) inhibits growth upon expression in E.coli
CC which is neutralized by cognate immunity protein YokJ, but not by
CC immunity proteins specific to other toxins with the LXG domain
CC (PubMed:22200572). {ECO:0000269|PubMed:22200572,
CC ECO:0000269|PubMed:34280190}.
CC -!- SUBUNIT: Probably interacts with cognate immunity protein YokJ but not
CC with non-cognate immunity proteins. The interaction inhibits the toxic
CC activity of YokJ (Probable). {ECO:0000305}.
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 yokI-yokJ 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 suggested to be an RNase.
CC {ECO:0000305|PubMed:22200572}.
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DR EMBL; AL009126; CAB14076.2; -; Genomic_DNA.
DR RefSeq; NP_390041.2; NC_000964.3.
DR RefSeq; WP_004398855.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; O31998; -.
DR STRING; 224308.BSU21580; -.
DR PaxDb; O31998; -.
DR PRIDE; O31998; -.
DR EnsemblBacteria; CAB14076; CAB14076; BSU_21580.
DR GeneID; 939115; -.
DR KEGG; bsu:BSU21580; -.
DR PATRIC; fig|224308.179.peg.2356; -.
DR eggNOG; COG5444; Bacteria.
DR OMA; HELTHAK; -.
DR PhylomeDB; O31998; -.
DR BioCyc; BSUB:BSU21580-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR InterPro; IPR006829; LXG_dom.
DR InterPro; IPR028900; Tox-SHH_dom.
DR Pfam; PF04740; LXG; 1.
DR Pfam; PF15652; Tox-SHH; 1.
DR PROSITE; PS51756; LXG; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Hydrolase; Nuclease; Reference proteome; Secreted; Toxin.
FT CHAIN 1..571
FT /note="Toxin YokI"
FT /id="PRO_0000360799"
FT DOMAIN 1..235
FT /note="LXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01092"
FT COILED 5..39
FT /evidence="ECO:0000255"
FT COILED 141..192
FT /evidence="ECO:0000255"
SQ SEQUENCE 571 AA; 64261 MW; CA98432F16F4716D CRC64;
MKVFEADSLL SEADKRTKEY KELRSQMVKL KKAFKAVADL DDSKFSGKGA DNIKAFYHDH
VGVTDQWIDL IDMKIVFLSS ISAKLEDAKM SDAYIEESFL EHELVNAYTK SKSIMSEQKK
AMKDILNDIN DILPLEIFST EDFKDKLSSA DDKREKTIDK INKLDEDLKT EYAETEQNEQ
FIQQDFKKLQ ESTGKGKNAT PIHYSAKAYR ESDIHKKKGD IEQHSEAYLT VKKEEAKERE
IKELKKKLND GVSDPDEYLE IAKKVGYENL EPAQVQLAVQ IEQAKQLEGA GEITWDIVKG
VGVGLYDVGK DTVTGLWDFI TDPGETLSAL GNAVIHPVKT YDAISAAIEE SYQKDMVNGD
AYSRSRWVTY AIGSVAAAVI GTKGAGAINK ADAAGKVINK ASQAGKKIKD VKIPDLLPYN
PKYDLAMAGD VPYNVVDGEN LKNQLMSFAK GSDKEVKPFD VVDYRPSNSP LENHHGVMDV
WAKHNVPNYV SRGSNTPTVA LTKEQHNATK KVYREWLFEK TGKKVGGKVN WKEVSPREIQ
ELTEKMFDAA NVPKEARQQY YNAFNQYNFR K
