T2PS_PROST
ID T2PS_PROST Reviewed; 326 AA.
AC P00640;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Type II restriction enzyme PstI {ECO:0000303|PubMed:12654995};
DE Short=R.PstI;
DE EC=3.1.21.4;
DE AltName: Full=Endonuclease PstI;
DE AltName: Full=Type-2 restriction enzyme PstI;
GN Name=pstIR;
OS Providencia stuartii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Providencia.
OX NCBI_TaxID=588;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, FUNCTION, AND
RP SUBUNIT.
RC STRAIN=164;
RX PubMed=6330092; DOI=10.1016/s0021-9258(17)42896-1;
RA Walder R.Y., Walder J.A., Donelson J.E.;
RT "The organization and complete nucleotide sequence of the PstI restriction-
RT modification system.";
RL J. Biol. Chem. 259:8015-8026(1984).
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'-CTGCAG-3' and cleaves after A-5.
CC {ECO:0000269|PubMed:6330092, 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:6330092}.
CC -!- SIMILARITY: Belongs to the BsuBI/PstI type II restriction endonuclease
CC family. {ECO:0000305}.
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DR EMBL; K02081; AAA25673.1; -; Genomic_DNA.
DR PIR; A00783; NDOFS.
DR AlphaFoldDB; P00640; -.
DR SMR; P00640; -.
DR BindingDB; P00640; -.
DR ChEMBL; CHEMBL5713; -.
DR BRENDA; 3.1.21.4; 5058.
DR PRO; PR:P00640; -.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion 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; 1.10.10.1820; -; 1.
DR Gene3D; 3.40.1350.80; -; 1.
DR InterPro; IPR041963; BsuBI/PstI_C_sf.
DR InterPro; IPR041454; BsuBI/PstI_N.
DR InterPro; IPR041962; BsuBI/PstI_N_sf.
DR InterPro; IPR009528; Restrct_endonuc_II_BsuBI_C.
DR Pfam; PF06616; BsuBI_PstI_RE; 1.
DR Pfam; PF17728; BsuBI_PstI_RE_N; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Endonuclease; Hydrolase; Magnesium; Nuclease;
KW Restriction system.
FT CHAIN 1..326
FT /note="Type II restriction enzyme PstI"
FT /id="PRO_0000077354"
SQ SEQUENCE 326 AA; 37414 MW; 475841183B414504 CRC64;
MKELKLKEAK EILKALGLPP QQYNDRSGWV LLALANIKPE DSWKEAKAPL LPTVSIMEFI
RTEYGKDYKP NSRETIRRQT LHQFEQARIV DRNRDLPSRA TNSKDNNYSL NQVIIDILHN
YPNGNWKELI QQFLTHVPSL QELYERALAR DRIPIKLLDG TQISLSPGEH NQLHADIVHE
FCPRFVGDMG KILYIGDTAS SRNEGGKLMV LDSEYLKKLG VPPMSHDKLP DVVVYDEKRK
WLFLIEAVTS HGPISPKRWL ELEAALSSCT VGKVYVTAFP TRTEFRKNAA NIAWETEVWI
ADNPDHMVHF NGDRFLGPHD KKPELS
