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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}.
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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
 
 
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