ID   T2K1_KLEPN              Reviewed;         218 AA.
AC   P25237;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Type II restriction enzyme KpnI {ECO:0000303|PubMed:12654995};
DE            Short=R.KpnI {ECO:0000303|PubMed:1754388};
DE            EC=3.1.21.4;
DE   AltName: Full=Endonuclease KpnI;
DE   AltName: Full=Type-2 restriction enzyme KpnI;
GN   Name=kpnIR {ECO:0000303|PubMed:1754388};
OS   Klebsiella pneumoniae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-12.
RC   STRAIN=OK8;
RX   PubMed=1754388; DOI=10.1093/nar/19.23.6505;
RA   Chatterjee D.K., Hammond A.W., Blakesley R.W., Adams S.M., Gerard G.F.;
RT   "Genetic organization of the KpnI restriction-modification system.";
RL   Nucleic Acids Res. 19:6505-6509(1991).
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'-GGTACC-3' and cleaves after C-5.
CC       {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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M76435; AAA25089.1; -; Genomic_DNA.
DR   EMBL; X61796; CAA43897.1; -; Genomic_DNA.
DR   PIR; S34431; S34431.
DR   RefSeq; WP_004176755.1; NZ_ULCW01000003.1.
DR   AlphaFoldDB; P25237; -.
DR   REBASE; 1180; KpnI.
DR   REBASE; 152761; Rsp541ORF2003P.
DR   REBASE; 152769; Rsp941ORF2000P.
DR   PATRIC; fig|573.1567.peg.2312; -.
DR   BRENDA; 3.1.21.4; 2814.
DR   PRO; PR:P25237; -.
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.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Endonuclease; Hydrolase; Nuclease;
KW   Restriction system.
FT   CHAIN           1..218
FT                   /note="Type II restriction enzyme KpnI"
FT                   /id="PRO_0000077327"
SQ   SEQUENCE   218 AA;  25112 MW;  857240D500E26C50 CRC64;
     MDVFDKVYSD DNNSYDQKTV SQRIEALFLN NLGKVVTRQQ IIRAATDPKT GKQPENWHQR
     LSELRTDKGY TILSWRDMKV LAPQEYIMPH ATRRPKAAKR VLPTKETWEQ VLDRANYSCE
     WQEDGQHCGL VEGDIDPIGG GTVKLTPDHM TPHSIDPATD VNDPKMWQAL CGRHQVMKKN
     YWDSNNGKIN VIGILQSVNE KQKNDALEFL LNYYGLKR