ID   T2N4_NEILA              Reviewed;         243 AA.
AC   P50183;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=Type II restriction enzyme NlaIV {ECO:0000303|PubMed:12654995};
DE            Short=R.NlaIV {ECO:0000303|PubMed:8190068};
DE            EC=3.1.21.4;
DE   AltName: Full=Endonuclease NlaIV;
DE   AltName: Full=Type-2 restriction enzyme NlaIV;
GN   Name=nlaIVR;
OS   Neisseria lactamica.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=486;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 23970 / DSM 4691 / CCUG 5853 / CIP 72.17 / NCTC 10617 /
RC   NCDC A7515;
RX   PubMed=8190068; DOI=10.1007/bf00283872;
RA   Lau P.C.K., Forghani F., Labbe D., Bergeron H., Brousseau R., Holtke H.J.;
RT   "The NlaIV restriction and modification genes of Neisseria lactamica are
RT   flanked by leucine biosynthesis genes.";
RL   Mol. Gen. Genet. 243:24-31(1994).
RN   [2]
RP   ERRATUM OF PUBMED:8190068.
RA   Lau P.C.K., Forghani F., Labbe D., Bergeron H., Brousseau R., Holtke H.J.;
RL   Mol. Gen. Genet. 244:167-167(1994).
RN   [3]
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'-GGNNCC-3' and cleaves after N-3.
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;
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DR   EMBL; U06074; AAA53238.1; -; Genomic_DNA.
DR   PIR; S43887; S43887.
DR   RefSeq; WP_003708504.1; NZ_QQML01000002.1.
DR   PDB; 6QM2; X-ray; 2.80 A; A=1-243.
DR   PDBsum; 6QM2; -.
DR   AlphaFoldDB; P50183; -.
DR   SMR; P50183; -.
DR   STRING; 486.B2G52_08330; -.
DR   REBASE; 1342; NlaIV.
DR   PRO; PR:P50183; -.
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; IPR019064; Restrct_endonuc_II_NlaIV.
DR   Pfam; PF09564; RE_NgoBV; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Endonuclease; Hydrolase; Nuclease; Restriction system.
FT   CHAIN           1..243
FT                   /note="Type II restriction enzyme NlaIV"
FT                   /id="PRO_0000077350"
FT   HELIX           6..15
FT                   /evidence="ECO:0007829|PDB:6QM2"
FT   TURN            19..21
FT                   /evidence="ECO:0007829|PDB:6QM2"
FT   STRAND          26..30
FT                   /evidence="ECO:0007829|PDB:6QM2"
FT   STRAND          33..37
FT                   /evidence="ECO:0007829|PDB:6QM2"
FT   HELIX           42..57
FT                   /evidence="ECO:0007829|PDB:6QM2"
FT   STRAND          68..71
FT                   /evidence="ECO:0007829|PDB:6QM2"
FT   STRAND          73..76
FT                   /evidence="ECO:0007829|PDB:6QM2"
FT   STRAND          83..92
FT                   /evidence="ECO:0007829|PDB:6QM2"
FT   HELIX           104..113
FT                   /evidence="ECO:0007829|PDB:6QM2"
FT   HELIX           115..119
FT                   /evidence="ECO:0007829|PDB:6QM2"
FT   STRAND          121..129
FT                   /evidence="ECO:0007829|PDB:6QM2"
FT   STRAND          135..144
FT                   /evidence="ECO:0007829|PDB:6QM2"
FT   HELIX           145..148
FT                   /evidence="ECO:0007829|PDB:6QM2"
FT   STRAND          153..157
FT                   /evidence="ECO:0007829|PDB:6QM2"
FT   STRAND          159..162
FT                   /evidence="ECO:0007829|PDB:6QM2"
FT   STRAND          165..169
FT                   /evidence="ECO:0007829|PDB:6QM2"
FT   HELIX           188..201
FT                   /evidence="ECO:0007829|PDB:6QM2"
FT   TURN            203..205
FT                   /evidence="ECO:0007829|PDB:6QM2"
FT   HELIX           206..208
FT                   /evidence="ECO:0007829|PDB:6QM2"
FT   STRAND          209..211
FT                   /evidence="ECO:0007829|PDB:6QM2"
FT   HELIX           212..224
FT                   /evidence="ECO:0007829|PDB:6QM2"
FT   HELIX           233..236
FT                   /evidence="ECO:0007829|PDB:6QM2"
FT   HELIX           237..239
FT                   /evidence="ECO:0007829|PDB:6QM2"
SQ   SEQUENCE   243 AA;  28826 MW;  3068E972D6736A49 CRC64;
     MIKLTAQQIF DKLLDEEKIL SANGQIRFFL GDVDIIVKQK DVVGNIIQEW LGGWLRKREI
     EFDVSTNTQM PPDFFLNKKD RSRELLEVKA FNRNASPGFD IADFKMYSDE IIHKPYMLDV
     DYLIFGYDMD DNGNVTIKDL WLKKVWQITR SMDGWAINLQ VKKGVVHKIR PGVWYSINKK
     NMPMFECLED FVSAIEETVY QNPATRHNAS LWKRKFEEAY KKHYNRSISI PRWHEIAHKY
     KKK
//