YQCG_BACSU
ID YQCG_BACSU Reviewed; 531 AA.
AC P45942;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Toxin YqcG {ECO:0000303|PubMed:22200572};
DE AltName: Full=DNase YqcG {ECO:0000303|PubMed:34280190};
GN Name=yqcG; OrderedLocusNames=BSU25860;
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 / JH642;
RX PubMed=7704261; DOI=10.1099/13500872-141-2-323;
RA Takemaru K., Mizuno M., Sato T., Takeuchi M., Kobayashi Y.;
RT "Complete nucleotide sequence of a skin element excised by DNA
RT rearrangement during sporulation in Bacillus subtilis.";
RL Microbiology 141:323-327(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / JH642;
RX PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA Kobayashi Y.;
RT "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT Bacillus subtilis genome containing the skin element and many sporulation
RT genes.";
RL Microbiology 142:3103-3111(1996).
RN [3]
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 [4]
RP IDENTIFICATION.
RX PubMed=7489895; DOI=10.1016/0378-1119(95)00636-k;
RA Medigue C., Moszer I., Viari A., Danchin A.;
RT "Analysis of a Bacillus subtilis genome fragment using a co-operative
RT computer system prototype.";
RL Gene 165:GC37-GC51(1995).
RN [5]
RP INCORRECT FUNCTION AS AN RNASE, FUNCTION AS A TOXIN, AND EXPRESSION IN
RP 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 [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 YqcF 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: Probably interacts with cognate immunity protein YqcF but not
CC with non-cognate immunity proteins. The interaction inhibits the toxic
CC activity of YqcF (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; 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 yqcF-yqcG 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 379-531) 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. {ECO:0000269|PubMed:22200572}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D32216; BAA06964.1; -; Genomic_DNA.
DR EMBL; D84432; BAA12428.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14527.1; -; Genomic_DNA.
DR PIR; F69949; F69949.
DR RefSeq; NP_390463.1; NC_000964.3.
DR RefSeq; WP_004399034.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P45942; -.
DR STRING; 224308.BSU25860; -.
DR PaxDb; P45942; -.
DR PRIDE; P45942; -.
DR EnsemblBacteria; CAB14527; CAB14527; BSU_25860.
DR GeneID; 937792; -.
DR KEGG; bsu:BSU25860; -.
DR PATRIC; fig|224308.179.peg.2810; -.
DR eggNOG; COG5444; Bacteria.
DR OMA; WIDLIEM; -.
DR BioCyc; BSUB:BSU25860-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; IPR026835; YqcG.
DR Pfam; PF14410; GH-E; 1.
DR Pfam; PF04740; LXG; 1.
DR Pfam; PF14449; PT-TG; 1.
DR PROSITE; PS51756; LXG; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Hydrolase; Nuclease; Reference proteome; Secreted; Toxin.
FT CHAIN 1..531
FT /note="Toxin YqcG"
FT /id="PRO_0000049777"
FT DOMAIN 1..235
FT /note="LXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01092"
FT REGION 408..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2..39
FT /evidence="ECO:0000255"
FT COILED 139..171
FT /evidence="ECO:0000255"
FT COMPBIAS 408..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 531 AA; 59669 MW; C9A39C032891B220 CRC64;
MKVFEAKTLL TEAEKRAQEY KDLKSKMVKL KKAFKAVADL DDSEFSGKGA NNIKSFYEDQ
AGIADQWIDL IEMKISFLTS IPGFLEDANL SDAYIEETFL AHELANAYTK SKSIMSEQKK
AMKDILNDIN DILPLDLFST ETFKNELSSA EKKRKEAIEK MDEVDQNLTS EYGLSEANEQ
MIQADYQALM NATAKGKSAS PIHYNAKAYR DSEIHKMTED VKKQSTDYIS FKDQQAEQRR
IAKEQEELAN RPWYEKSWDA VCNFTGEVSG YYDYKRAADG VDPVTGEKLT AGQRVAAGAM
AAAGYIPIVG WAGKLAKGGK AVYSTSKALY RADKALDVYK TPKTFHALQN SSKGLYGLAS
ANGFSEAITG RDMFGNKVSK ERQEQSLSGA MAMLVPFGAR GINKKLNAKS SSRVSEASTN
TSKKPKVPKT YKRPTYFRKG VRDKVWENAK DSTGSVKDPL TKQVMKKDEP WDMGHKPGYE
FRKHQQSAME RNISRKQFLD EHNNPDHYQP ELPSSNRSHK GEDMTDDYFG D
