YWQJ_BACSU
ID YWQJ_BACSU Reviewed; 602 AA.
AC P96722; Q795B6;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Toxin YwqJ {ECO:0000303|PubMed:34280190};
GN Name=ywqJ; OrderedLocusNames=BSU36190;
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;
RX PubMed=9353933; DOI=10.1099/00221287-143-10-3313;
RA Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V.,
RA Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G.,
RA Kunst F., Danchin A., Glaser P.;
RT "The Bacillus subtilis genome from gerBC (311 degrees) to licR (334
RT degrees).";
RL Microbiology 143:3313-3328(1997).
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 INDENTIFICATION OF TOXIN-IMMUNITY PAIR, AND PROBABLE SUBUNIT.
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, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION
RP 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; no effect is seen on DNA or rRNA. Co-overexpression with
CC cognate immunity protein YwqK does not cause growth arrest. The toxic
CC effect is dependent on the epsA and tapA operons which are required for
CC biofilm formation (PubMed:34280190). Its toxic effects are probably
CC neutralized by its cognate immunity protein YwqK, but not by immunity
CC proteins specific to other toxins with the LXG domain (Probable). May
CC have deaminase activity (Probable). {ECO:0000269|PubMed:34280190,
CC ECO:0000305|PubMed:22200572, ECO:0000305|PubMed:34280190}.
CC -!- SUBUNIT: Probably interacts with cognate immunity protein YwqK but not
CC with non-cognate immunity proteins. The interaction inhibits the toxic
CC activity of YwqJ. {ECO:0000305|PubMed:22200572}.
CC -!- INTERACTION:
CC P96722; O31501: swrC; NbExp=3; IntAct=EBI-5243080, EBI-5242442;
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; 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 ywqH-ywqI-ywqJ-ywqK-nfi operon
CC has no visible growth phenotype, however it is out-competed by wild-
CC type cells. {ECO:0000269|PubMed:34280190}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the LXG family.
CC {ECO:0000303|PubMed:22200572}.
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DR EMBL; Z92952; CAB07448.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15636.1; -; Genomic_DNA.
DR PIR; E70067; E70067.
DR RefSeq; NP_391500.1; NC_000964.3.
DR RefSeq; WP_003243987.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P96722; -.
DR IntAct; P96722; 27.
DR STRING; 224308.BSU36190; -.
DR PaxDb; P96722; -.
DR PRIDE; P96722; -.
DR EnsemblBacteria; CAB15636; CAB15636; BSU_36190.
DR GeneID; 936885; -.
DR KEGG; bsu:BSU36190; -.
DR PATRIC; fig|224308.179.peg.3916; -.
DR eggNOG; COG5444; Bacteria.
DR OMA; YDKKAFH; -.
DR BioCyc; BSUB:BSU36190-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR InterPro; IPR006829; LXG_dom.
DR InterPro; IPR027797; PT-TG_dom.
DR InterPro; IPR025968; YwqJ_deaminase.
DR Pfam; PF04740; LXG; 1.
DR Pfam; PF14449; PT-TG; 1.
DR Pfam; PF14431; YwqJ-deaminase; 1.
DR PROSITE; PS51756; LXG; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Reference proteome; Secreted.
FT CHAIN 1..602
FT /note="Toxin YwqJ"
FT /id="PRO_0000360801"
FT DOMAIN 1..235
FT /note="LXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01092"
FT COILED 6..41
FT /evidence="ECO:0000255"
FT COILED 227..251
FT /evidence="ECO:0000255"
SQ SEQUENCE 602 AA; 66690 MW; 3D3B2E0CDBD457A9 CRC64;
MSKVFESKSL IEEAKSRKKQ YETLEEQLNT LKKAFQGVAD LGDNFKGNGA DNIKDFFQGQ
AEIVDSWLTL VSAQIAFLNG ISGDIKDQEL NDSYVETSFL DHELPNGDLK ASEIVSAHKE
EIDSILSGIS DIIDLDMYTL DDYADKMGDA QKIRRDTITA VDKLDESLTT EYQNLESLDN
AVLTKYSVLM QATSNGKSAS PMYYDKKAFH SNEVYKSVIE VENQGTTYID AKTQQAEARR
LQEKAEEEAN KPWYEKTWDG VCNFTGEVTG YYDYKRATEG VDPVTGEKLS TAERVTAGAM
AAAGFIPVVG WAGRAFKGGK AIYKTGKAAI AAEHALDAYK TGKSLDILKM TEMGAYGLVA
SNGFSEAVTG RDMFGNKVSE EKRKQGALEA ITIIGGAGLA HYFDRLYQKN APYVNKVSNE
SLISNIAKTT EEKQTRLQYL RNKHGVLSKE DLHHRINLRA EVLNELSRIK SSGLTKKQRG
PAVAGVLDKK TGNYYFGINN IDGKPPKVLH PLIHDRIVNM PTELKEGYIK TSGAGSHAEV
NALNEALLQR PDADLKDLMV YVVSARKINK KMPEGVPMPR CPHCEYITQN TNYIPEALKY
GK
