YNCB_BACSU
ID YNCB_BACSU Reviewed; 211 AA.
AC P94492; Q796H2;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Endonuclease YncB;
DE EC=3.1.-.-;
DE Flags: Precursor;
GN Name=yncB; OrderedLocusNames=BSU17620;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Borchert S., Klein C., Piksa B., Hammelmann M., Entian K.-D.;
RT "Sequencing of a 26 kb region of the Bacillus subtilis genome downstream of
RT spoVJ.";
RL Submitted (AUG-1996) 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 FUNCTION AS A NUCLEASE, DNASE ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=11584000; DOI=10.1074/jbc.m106205200;
RA Sakamoto J.J., Sasaki M., Tsuchido T.;
RT "Purification and characterization of a Bacillus subtilis 168 nuclease,
RT YokF, involved in chromosomal DNA degradation and cell death caused by
RT thermal shock treatments.";
RL J. Biol. Chem. 276:47046-47051(2001).
CC -!- FUNCTION: Shows DNase activity on double strand DNA.
CC {ECO:0000269|PubMed:11584000}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show DNase activity when
CC exposed to thermal stress. Also shows an increased ability of
CC competence. {ECO:0000269|PubMed:11584000}.
CC -!- SIMILARITY: Belongs to the thermonuclease family. {ECO:0000255|PROSITE-
CC ProRule:PRU00272}.
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; U66480; AAB41095.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13646.1; -; Genomic_DNA.
DR PIR; D69888; D69888.
DR RefSeq; NP_389644.1; NC_000964.3.
DR RefSeq; WP_003245469.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P94492; -.
DR SMR; P94492; -.
DR IntAct; P94492; 1.
DR STRING; 224308.BSU17620; -.
DR PaxDb; P94492; -.
DR PRIDE; P94492; -.
DR EnsemblBacteria; CAB13646; CAB13646; BSU_17620.
DR GeneID; 939569; -.
DR KEGG; bsu:BSU17620; -.
DR PATRIC; fig|224308.179.peg.1913; -.
DR eggNOG; COG1525; Bacteria.
DR InParanoid; P94492; -.
DR OMA; YVTNRGF; -.
DR PhylomeDB; P94492; -.
DR BioCyc; BSUB:BSU17620-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR Gene3D; 2.40.50.90; -; 1.
DR InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR016071; Staphylococal_nuclease_OB-fold.
DR InterPro; IPR002071; Thermonucl_AS.
DR Pfam; PF00565; SNase; 1.
DR SMART; SM00318; SNc; 1.
DR SUPFAM; SSF50199; SSF50199; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS01284; TNASE_2; 1.
DR PROSITE; PS50830; TNASE_3; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Endonuclease; Hydrolase; Lipoprotein; Membrane;
KW Metal-binding; Nuclease; Palmitate; Reference proteome; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 20..211
FT /note="Endonuclease YncB"
FT /id="PRO_0000375917"
FT REGION 24..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 91
FT /evidence="ECO:0000250"
FT ACT_SITE 99
FT /evidence="ECO:0000250"
FT ACT_SITE 142
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT BINDING 96
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT BINDING 97
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT LIPID 20
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 20
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 211 AA; 23684 MW; C7F96B2B68CAD671 CRC64;
MKKILISMIA IVLSITLAAC GSNHAAKNHS DSNGTEQVSQ DTHSNEYNQT EQKAGTPHSK
NQKKLVNVTL DRAIDGDTIK VIYNGKKDTV RYLLVDTPET KKPNSCVQPY GEDASKRNKE
LVNSGKLQLE FDKGDRRDKY GRLLAYVYVD GKSVQETLLK EGLARVAYVY EPNTKYIDQF
RLDEQEAKSD KLSIWSKSGY VTNRGFNGCV K