ID   T2S1_STRSA              Reviewed;         602 AA.
AC   P29346;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Type II restriction enzyme StsI {ECO:0000303|PubMed:12654995};
DE            Short=R.StsI;
DE            EC=3.1.21.4;
DE   AltName: Full=Endonuclease StsI;
DE   AltName: Full=Type-2 restriction enzyme StsI;
GN   Name=stsIR;
OS   Streptococcus sanguinis.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-22, AND FUNCTION.
RC   STRAIN=54;
RX   PubMed=1387204; DOI=10.1093/nar/20.16.4167;
RA   Kita K., Suisha M., Kotani H., Yanase H., Kato N.;
RT   "Cloning and sequence analysis of the StsI restriction-modification gene:
RT   presence of homology to FokI restriction-modification enzymes.";
RL   Nucleic Acids Res. 20:4167-4172(1992).
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: An S subtype restriction enzyme that recognizes the double-
CC       stranded sequences 5'-GGATG-3' and 3'-CATCC-5' and cleaves respectively
CC       15 bases after G-1 and 14 bases before C-1.
CC       {ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:1387204}.
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;
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DR   EMBL; D11101; BAA01875.1; -; Genomic_DNA.
DR   PIR; S35495; S35495.
DR   AlphaFoldDB; P29346; -.
DR   SMR; P29346; -.
DR   REBASE; 1784; StsI.
DR   PRO; PR:P29346; -.
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   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.90.241.10; -; 1.
DR   InterPro; IPR015334; FokI_cleavage_dom.
DR   InterPro; IPR004234; FokI_D1.
DR   InterPro; IPR004233; FokI_D2.
DR   InterPro; IPR044945; FokI_dom_1_2.
DR   InterPro; IPR011335; Restrct_endonuc-II-like.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF09254; Endonuc-FokI_C; 1.
DR   Pfam; PF02980; FokI_C; 1.
DR   Pfam; PF02981; FokI_N; 1.
DR   SUPFAM; SSF46785; SSF46785; 3.
DR   SUPFAM; SSF52980; SSF52980; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Endonuclease; Hydrolase; Nuclease;
KW   Restriction system.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1387204"
FT   CHAIN           2..602
FT                   /note="Type II restriction enzyme StsI"
FT                   /id="PRO_0000077368"
SQ   SEQUENCE   602 AA;  68392 MW;  8FFCC465145F5B99 CRC64;
     MTISINEYSD LNNLAFGLGQ DVSQDLKELV KVASIFMPDS KIHKWLIDTR LEEVVTDLNL
     RYELKSVITN TPISVTWKQL TGTRTKREAN SLVQAVFPGQ CSRLAIVDWA AKNYVSVAVA
     FGLLKFHRAD KTFTISEIGI QAVKLYDSEE LAELDKFLYE RLLEYPYAAW LIRLLGNQPS
     KQFSKFDLGE HFGFIDELGF ETAPIEIFLN GLAQAEIDGD KTAAQKIKSN FESTSDKYMR
     WLAGVLVTAG LATSTTKKVT HTYKNRKFEL TLGTVYQITA KGLTALKEVN GKSRYPRSRK
     RVMWEFLATK DKEAIAKKTS RSLMLKHLTE KKNPIQAEVI ATLINTDYPT LEITPEEVID
     DCIGLNRIGI EILIDGDKLT LNDKLFDFEI PVQKDVVLEK SDIEKFKNQL RTELTNIDHS
     YLKGIDIASK KKTSNVENTE FEAISTKIFT DELGFSGKHL GGSNKPDGLL WDDDCAIILD
     SKAYSEGFPL TASHTDAMGR YLRQFTERKE EIKPTWWDIA PEHLDNTYFA YVSGSFSGNY
     KEQLQKFRQD TNHLGGALEF VKLLLLANNY KTQKMSKKEV KKSILDYNIS YEEYAPLLAE
     IE