YOKF_BACSU
ID YOKF_BACSU Reviewed; 296 AA.
AC O32001;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=SPbeta prophage-derived endonuclease YokF;
DE EC=3.1.-.-;
DE Flags: Precursor;
GN Name=yokF; OrderedLocusNames=BSU21610;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
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 [2]
RP FUNCTION, DNASE ACTIVITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, 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: Catalyzes the hydrolysis of supercoiled double and single
CC strand DNA and RNA. Involved in chromosomal DNA degradation and cell
CC death caused by thermal stress. {ECO:0000269|PubMed:11584000}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:11584000};
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000269|PubMed:11584000};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:11584000};
CC Note=Binds 1 Ca(2+) ion per subunit. Can also use Co(2+) or Mn(2+).
CC {ECO:0000269|PubMed:11584000};
CC -!- ACTIVITY REGULATION: Inhibited by aurintricalboxylic acid but not by
CC Zn(2+), Mn(2+), Hg(2+), 2-mercaptoethanol and sodium citrate. Neither
CC inhibited nor activated by ATP. {ECO:0000269|PubMed:11584000}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0-8.0. {ECO:0000269|PubMed:11584000};
CC Temperature dependence:
CC Optimum temperature is 40-45 degrees Celsius.
CC {ECO:0000269|PubMed:11584000};
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 are more sensitive to
CC mitomycin C, show an increased ability of competence and are not able
CC to metabolize extracellular DNA. {ECO:0000269|PubMed:11584000}.
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DR EMBL; AL009126; CAB14079.1; -; Genomic_DNA.
DR RefSeq; NP_390044.1; NC_000964.3.
DR RefSeq; WP_004399048.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; O32001; -.
DR SMR; O32001; -.
DR STRING; 224308.BSU21610; -.
DR PaxDb; O32001; -.
DR PRIDE; O32001; -.
DR EnsemblBacteria; CAB14079; CAB14079; BSU_21610.
DR GeneID; 939113; -.
DR KEGG; bsu:BSU21610; -.
DR PATRIC; fig|224308.179.peg.2360; -.
DR eggNOG; COG1525; Bacteria.
DR InParanoid; O32001; -.
DR OMA; GYARVAY; -.
DR BioCyc; BSUB:BSU21610-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:0004518; F:nuclease activity; IMP:CACAO.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR Gene3D; 2.40.50.90; -; 1.
DR InterPro; IPR008613; Excalibur_Ca-bd_domain.
DR InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR016071; Staphylococal_nuclease_OB-fold.
DR InterPro; IPR002071; Thermonucl_AS.
DR Pfam; PF05901; Excalibur; 1.
DR Pfam; PF00565; SNase; 1.
DR SMART; SM00894; Excalibur; 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; Copper; Endonuclease; Hydrolase; Lipoprotein;
KW Manganese; Membrane; Metal-binding; Nuclease; Palmitate;
KW Reference proteome; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 20..296
FT /note="SPbeta prophage-derived endonuclease YokF"
FT /id="PRO_0000375918"
FT DOMAIN 66..199
FT /note="TNase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT REGION 20..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 93
FT /evidence="ECO:0000250"
FT ACT_SITE 101
FT /evidence="ECO:0000250"
FT ACT_SITE 144
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT BINDING 98
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT BINDING 99
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 296 AA; 33003 MW; AB11DCD0C89D0C4E CRC64;
MKKVLLGFAA FTLSLSLAAC SSNDSEKVST EKETPQASTD VEKKTEQKES TKEKTADKSK
EKDKKELVDV TLDRAVDGDT IKVTYNGNVD TVRYLLIDTP ETKKPNSCVQ PYGEDASKRN
KELVNSGKLQ LEFDKGDRRD KYGRLLAYVY VDGKSVQETL LKEGLARVAY VYEPNTKYID
QFKKDEQEAK SEKLSIWSKN GYVTDRGFNG CVKEKTTAVK KATTSKPAAT QPTTPKASSE
TSTTTEKEAS SETTGGTETF KNCTELRKKY PNGVPSSHPA YQSKMDRDHD NYACER
