T2D1_STRPN
ID T2D1_STRPN Reviewed; 254 AA.
AC P0A459; P09356;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Type II methyl-directed restriction enzyme DpnI {ECO:0000303|PubMed:12654995};
DE Short=R.DpnI;
DE EC=3.1.21.4 {ECO:0000269|PubMed:2844782};
DE AltName: Full=Endonuclease DpnI;
DE AltName: Full=Type-2 restriction enzyme DpnI;
GN Name=dpnC {ECO:0000303|PubMed:2844782}; OrderedLocusNames=SP_1850;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3019562; DOI=10.1016/0092-8674(86)90698-7;
RA Lacks S.A., Mannarelli B.M., Springhorn S.S., Greenberg B.;
RT "Genetic basis of the complementary DpnI and DpnII restriction systems of
RT S. pneumoniae: an intercellular cassette mechanism.";
RL Cell 46:993-1000(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, FUNCTION, AND
RP CATALYTIC ACTIVITY.
RX PubMed=2844782; DOI=10.1016/s0021-9258(18)68093-7;
RA de la Campa A.G., Springhorn S.S., Kale P., Lacks S.A.;
RT "Proteins encoded by the DpnI restriction gene cassette. Hyperproduction
RT and characterization of the DpnI endonuclease.";
RL J. Biol. Chem. 263:14696-14702(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
RN [4]
RP NOMENCLATURE, AND SUBTYPES.
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 M and P subtype restriction enzyme that recognizes the
CC double-stranded, methylated sequence 5'-G(Me)ATC-3' and cleaves after
CC A-2. {ECO:0000269|PubMed:2844782, 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 Evidence={ECO:0000269|PubMed:2844782};
CC -!- SIMILARITY: Belongs to the DpnI type II restriction endonuclease
CC family. {ECO:0000305}.
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DR EMBL; M14340; AAA88577.2; -; Genomic_DNA.
DR EMBL; AE005672; AAK75922.1; -; Genomic_DNA.
DR PIR; A31975; A31975.
DR PIR; A95216; A95216.
DR RefSeq; WP_000418960.1; NZ_AKVY01000001.1.
DR PDB; 4KYW; X-ray; 2.35 A; A=1-254.
DR PDBsum; 4KYW; -.
DR AlphaFoldDB; P0A459; -.
DR SMR; P0A459; -.
DR STRING; 170187.SP_1850; -.
DR REBASE; 5187; SpnORF1850P.
DR REBASE; 776; DpnI.
DR EnsemblBacteria; AAK75922; AAK75922; SP_1850.
DR GeneID; 60234182; -.
DR KEGG; spn:SP_1850; -.
DR eggNOG; ENOG502Z8N2; Bacteria.
DR OMA; HHIMCSI; -.
DR BioCyc; SPNE170187:G1FZB-1880-MON; -.
DR PRO; PR:P0A459; -.
DR Proteomes; UP000000585; Chromosome.
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; 3.40.210.30; -; 1.
DR InterPro; IPR010324; DRP.
DR InterPro; IPR041368; DRP_C.
DR InterPro; IPR043025; DRP_PD-(D/E)XK_dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF06044; DpnI; 1.
DR Pfam; PF17726; DpnI_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Endonuclease; Hydrolase; Nuclease;
KW Restriction system.
FT CHAIN 1..254
FT /note="Type II methyl-directed restriction enzyme DpnI"
FT /id="PRO_0000077300"
FT HELIX 7..10
FT /evidence="ECO:0007829|PDB:4KYW"
FT HELIX 16..31
FT /evidence="ECO:0007829|PDB:4KYW"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:4KYW"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:4KYW"
FT STRAND 62..70
FT /evidence="ECO:0007829|PDB:4KYW"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:4KYW"
FT HELIX 81..87
FT /evidence="ECO:0007829|PDB:4KYW"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:4KYW"
FT STRAND 105..113
FT /evidence="ECO:0007829|PDB:4KYW"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:4KYW"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:4KYW"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:4KYW"
FT TURN 134..137
FT /evidence="ECO:0007829|PDB:4KYW"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:4KYW"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:4KYW"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:4KYW"
FT HELIX 165..175
FT /evidence="ECO:0007829|PDB:4KYW"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:4KYW"
FT HELIX 188..198
FT /evidence="ECO:0007829|PDB:4KYW"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:4KYW"
FT HELIX 206..209
FT /evidence="ECO:0007829|PDB:4KYW"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:4KYW"
FT HELIX 213..219
FT /evidence="ECO:0007829|PDB:4KYW"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:4KYW"
FT HELIX 226..239
FT /evidence="ECO:0007829|PDB:4KYW"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:4KYW"
FT STRAND 247..253
FT /evidence="ECO:0007829|PDB:4KYW"
SQ SEQUENCE 254 AA; 29785 MW; 7FFFFE14BB3EFEDB CRC64;
MELHFNLELV ETYKSNSQKA RILTEDWVYR QSYCPNCGNN PLNHFENNRP VADFYCNHCS
EEFELKSKKG NFSSTINDGA YATMMKRVQA DNNPNFFFLT YTKNFEVNNF LVLPKQFVTP
KSIIQRKPLA PTARRAGWIG CNIDLSQVPS KGRIFLVQDG QVRDPEKVTK EFKQGLFLRK
SSLSSRGWTI EILNCIDKIE GSEFTLEDMY RFESDLKNIF VKNNHIKEKI RQQLQILRDK
EIIEFKGRGK YRKL
