ID   T2N3_NEILA              Reviewed;         230 AA.
AC   Q51083;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   24-JAN-2024, entry version 67.
DE   RecName: Full=Type II restriction enzyme NlaIII {ECO:0000303|PubMed:12654995};
DE            Short=R.NlaIII;
DE            EC=3.1.21.4;
DE   AltName: Full=Endonuclease NlaIII;
DE   AltName: Full=Type-2 restriction enzyme NlaIII;
GN   Name=nlaIIIR;
OS   Neisseria lactamica.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=486;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 23970 / DSM 4691 / CCUG 5853 / CIP 72.17 / NCTC 10617 /
RC   NCDC A7515;
RX   PubMed=8996109; DOI=10.1016/s0378-1119(96)00561-6;
RA   Morgan R.D., Camp R.R., Wilson G.G., Xu S.-Y.;
RT   "Molecular cloning and expression of NlaIII restriction-modification system
RT   in E. coli.";
RL   Gene 183:215-218(1996).
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'-CATG-3' and cleaves after G-4.
CC       {ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:8996109}.
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; U59398; AAB41400.1; -; Genomic_DNA.
DR   PIR; JC5751; JC5751.
DR   RefSeq; WP_003709319.1; NZ_LR590477.1.
DR   AlphaFoldDB; Q51083; -.
DR   STRING; 486.B2G52_01560; -.
DR   PRO; PR:Q51083; -.
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; IPR007979; NlaIII/ICEA1.
DR   Pfam; PF05315; ICEA; 1.
PE   4: Predicted;
KW   Endonuclease; Hydrolase; Nuclease; Restriction system.
FT   CHAIN           1..230
FT                   /note="Type II restriction enzyme NlaIII"
FT                   /id="PRO_0000077349"
SQ   SEQUENCE   230 AA;  26487 MW;  00C933962C3ADC43 CRC64;
     MKITKTELFL RLAKPNEQGI SRWVKTSEFA GEYKDLKLGN GGSWCRKDSP LARDYIVEFD
     KGLTSGNSID AIRLNGFNQE KHFKQYIRKD IKDALKTRNC VMLGVNGKSE NTKIEIDHKD
     GRKNNHRVSD IKTQKLEDFQ PLCKAANDVK RQICKTCKET NKRWSAKNIS GNPYAFYMGD
     ENYSEELGCV GCYQYDPVEY RKSSVKRIAA EAAKYTSDYI FKKLYEEDNG
//