YEEF_BACSU
ID YEEF_BACSU Reviewed; 669 AA.
AC O31506; O30581;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Toxin YeeF {ECO:0000303|PubMed:34280190};
DE AltName: Full=DNase YeeF {ECO:0000303|PubMed:34280190};
GN Name=yeeF; OrderedLocusNames=BSU06810;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Borriss R., Schroeter R.;
RT "The 55-58 degree segment of the Bacillus subtilis chromosome, a region
RT spanning from the purA gene cluster to the cotJ operon.";
RL Submitted (JUL-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 SEQUENCE REVISION TO 58-60; 66; 218-223 AND C-TERMINUS.
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 [4]
RP INDENTIFICATION OF TOXIN-IMMUNITY PAIR, AND INTERACTION WITH YEZG.
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 [5]
RP SUBCELLULAR LOCATION.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=22882210; DOI=10.1111/j.1365-2958.2012.08205.x;
RA Yepes A., Schneider J., Mielich B., Koch G., Garcia-Betancur J.C.,
RA Ramamurthi K.S., Vlamakis H., Lopez D.;
RT "The biofilm formation defect of a Bacillus subtilis flotillin-defective
RT mutant involves the protease FtsH.";
RL Mol. Microbiol. 86:457-471(2012).
RN [6]
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 YezG 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). Binds DNA
CC in the presence and absence of YezG (By similarity).
CC {ECO:0000250|UniProtKB:E0TU96, ECO:0000269|PubMed:34280190}.
CC -!- SUBUNIT: Interacts with cognate immunity protein YezG but not with non-
CC cognate immunity protein YobK. The interaction probably inhibits the
CC toxic activity of YeeF. {ECO:0000269|PubMed:22200572}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22882210}.
CC Membrane raft {ECO:0000269|PubMed:22882210}. Note=Present in detergent-
CC resistant membrane (DRM) fractions that may be equivalent to eukaryotic
CC membrane rafts; these rafts include proteins involved in signaling,
CC molecule trafficking and protein secretion (PubMed:22882210). Delivery
CC to target cells requires the type VII secretion system (T7SS) and YukE
CC (PubMed:34280190). {ECO:0000269|PubMed:22882210,
CC ECO:0000269|PubMed:34280190}.
CC -!- INDUCTION: Expressed on rich and minimal solid media likely in early
CC stationary phase; dependent on DegSU. Not expressed in liquid LB, but
CC only under conditions that promote biofilm formation.
CC {ECO:0000269|PubMed:34280190}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the yeeF-yezG 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB66479.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF012532; AAB66479.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AL009126; CAB12501.2; -; Genomic_DNA.
DR PIR; A69793; A69793.
DR RefSeq; NP_388563.2; NC_000964.3.
DR RefSeq; WP_003242909.1; NZ_JNCM01000032.1.
DR AlphaFoldDB; O31506; -.
DR IntAct; O31506; 1.
DR MINT; O31506; -.
DR STRING; 224308.BSU06812; -.
DR PRIDE; O31506; -.
DR EnsemblBacteria; CAB12501; CAB12501; BSU_06812.
DR GeneID; 938753; -.
DR KEGG; bsu:BSU06812; -.
DR PATRIC; fig|224308.179.peg.740; -.
DR eggNOG; COG5444; Bacteria.
DR OMA; YEMEQEW; -.
DR PhylomeDB; O31506; -.
DR BioCyc; BSUB:BSU06812-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.570.10; -; 1.
DR InterPro; IPR044929; DNA/RNA_non-sp_Endonuclease_sf.
DR InterPro; IPR044927; Endonuclea_NS_2.
DR InterPro; IPR006829; LXG_dom.
DR Pfam; PF13930; Endonuclea_NS_2; 1.
DR Pfam; PF04740; LXG; 1.
DR PROSITE; PS51756; LXG; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; DNA-binding; Hydrolase; Membrane; Nuclease;
KW Reference proteome; Toxin.
FT CHAIN 1..669
FT /note="Toxin YeeF"
FT /id="PRO_0000360798"
FT DOMAIN 1..235
FT /note="LXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01092"
FT REGION 561..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2..39
FT /evidence="ECO:0000255"
FT COILED 100..171
FT /evidence="ECO:0000255"
FT COILED 226..258
FT /evidence="ECO:0000255"
FT CONFLICT 58..60
FT /note="HDH -> TTN (in Ref. 1; AAB66479)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="Q -> R (in Ref. 1; AAB66479)"
FT /evidence="ECO:0000305"
FT CONFLICT 218..223
FT /note="KGDIEK -> RRHLKR (in Ref. 1; AAB66479)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 669 AA; 74488 MW; 9856E5A56E559FEE CRC64;
MKVFEAKTLL SEATDRAKEY KELRTQMVNL RKALKGVADL SDSEFSGKGA SNIKAFYHDH
VGVADQWIDY IDMKIAFFNS IAGAAEDKGL SDAYIEESFL EHELANANKK SKSIMSEQKK
AMKDILNDID DILPLDLFST ETFKDELADA NDKRKKTLEK LDALDEDLKT EYALSEPNEQ
FIKSDFQKLQ EATGKGKNAT PIHYNAKAYR ESDIHKKKGD IEKRTEAYLK IKKEEAKERE
IEKLKERLKN YDYADADEFY EMAKTIGYEN LTAEQQRYFT QIENTRELEA GFKGVAVGLY
DSGKDAVVGL WDMVTDPGGT VEAITGAMAH PIKTYEAISA AIEESYQKDM VNGDTYSRAR
WVSYAVGTVV TSIVGTKGVG AVSKTGTAAK VTTKVKTAAS KSATAQKAIT VSKQTVDHIK
QKVNTGIEVS KKHVKTKLNQ IGDLTLADIL PYHPRHDLVP AGVPYNAVNG VTLKEGLQKF
AKVILPKPYG TSSSGRRTPA PHVPPVTVKY GEHFARWSRK KVLKPNIIYK TKEGYTYTTD
NYGRITSVKA DLQLGEAKRN QYAQTNAGKP QDRKPDDDGG HLIATQFKGS GQFDNIVPMN
SQINRSGGKW YEMEQEWAKA LSKKPPKKVA VQIEPVYSGD SLRPSYFDVT YKIGSRKEIS
VSIKNQPGG
