ID   T2S9_STAAU              Reviewed;         261 AA.
AC   P23736;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Type II restriction enzyme Sau96I {ECO:0000303|PubMed:12654995};
DE            Short=R.Sau96I;
DE            EC=3.1.21.4;
DE   AltName: Full=Endonuclease Sau96I;
DE   AltName: Full=Type-2 restriction enzyme Sau96I;
GN   Name=sau96IR {ECO:0000303|PubMed:2204026};
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBUNIT.
RC   STRAIN=PS96;
RX   PubMed=2204026; DOI=10.1093/nar/18.16.4659;
RA   Szilak L., Venetianer P., Kiss A.;
RT   "Cloning and nucleotide sequence of the genes coding for the Sau96I
RT   restriction and modification enzymes.";
RL   Nucleic Acids Res. 18:4659-4664(1990).
RN   [2]
RP   NOMENCLATURE, AND SUBTYPE.
RX   PubMed=12654995; DOI=10.1093/nar/gkg274;
RA   Roberts R.J., Belfort M., Bestor T., Bhagwat A.S., Bickle T.A.,
RA   Bitinaite J., Blumenthal R.M., Degtyarev S.K., Dryden D.T., Dybvig K.,
RA   Firman K., Gromova E.S., Gumport R.I., Halford S.E., Hattman S.,
RA   Heitman J., Hornby D.P., Janulaitis A., Jeltsch A., Josephsen J., Kiss A.,
RA   Klaenhammer T.R., Kobayashi I., Kong H., Krueger D.H., Lacks S.,
RA   Marinus M.G., Miyahara M., Morgan R.D., Murray N.E., Nagaraja V.,
RA   Piekarowicz A., Pingoud A., Raleigh E., Rao D.N., Reich N., Repin V.E.,
RA   Selker E.U., Shaw P.C., Stein D.C., Stoddard B.L., Szybalski W.,
RA   Trautner T.A., Van Etten J.L., Vitor J.M., Wilson G.G., Xu S.Y.;
RT   "A nomenclature for restriction enzymes, DNA methyltransferases, homing
RT   endonucleases and their genes.";
RL   Nucleic Acids Res. 31:1805-1812(2003).
CC   -!- FUNCTION: A P subtype restriction enzyme that recognizes the double-
CC       stranded sequence 5'-GGNCC-3' and cleaves after G-1.
CC       {ECO:0000269|PubMed:2204026, ECO:0000303|PubMed:12654995}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage of DNA to give specific double-
CC         stranded fragments with terminal 5'-phosphates.; EC=3.1.21.4;
CC   -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:2204026}.
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DR   EMBL; X53096; CAA37259.1; -; Genomic_DNA.
DR   PIR; S12706; S12706.
DR   RefSeq; WP_000182778.1; NZ_WKGE01000019.1.
DR   AlphaFoldDB; P23736; -.
DR   REBASE; 1607; Sau96I.
DR   PATRIC; fig|1280.3540.peg.2443; -.
DR   BRENDA; 3.1.21.4; 3352.
DR   PRO; PR:P23736; -.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0009036; F:type II site-specific deoxyribonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   InterPro; IPR019057; Restrct_endonuc_II_Eco47II.
DR   Pfam; PF09553; RE_Eco47II; 1.
PE   1: Evidence at protein level;
KW   Endonuclease; Hydrolase; Nuclease; Restriction system.
FT   CHAIN           1..261
FT                   /note="Type II restriction enzyme Sau96I"
FT                   /id="PRO_0000077359"
SQ   SEQUENCE   261 AA;  30486 MW;  75338416FCD54677 CRC64;
     MTNKYLSFIT DEDLFECIEF LYTEYEKALE GIDFDKFFKN RIDTFKMTFD MGINNLSEQD
     WLAAELQRQV EKTITNHVGT FHEKLIGKIE GYTNYPVGYD YDVAKDDNTL FAEIKNKHNT
     LTGTHTKSLF QKICGYAEKY PDAICYYVRI IDTKSRNDIW EFRSGSIDEN TREKPRFSHP
     RVRIASGDQF YKIVTGEEDA FKQLAYNIPI ALDDWIETKR AKKGSSLGLF AELYQQAKAN
     NRTLSEEIIS INYPKSNYIS F