T2BA_BACAM
ID T2BA_BACAM Reviewed; 213 AA.
AC P23940;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Type II restriction enzyme BamHI {ECO:0000303|PubMed:12654995};
DE Short=R.BamHI {ECO:0000303|PubMed:1901989};
DE EC=3.1.21.4 {ECO:0000269|PubMed:1177312, ECO:0000269|PubMed:834250};
DE AltName: Full=Endonuclease BamHI;
DE AltName: Full=Type-2 restriction enzyme BamHI;
GN Name=bamHIR {ECO:0000303|PubMed:1901989};
OS Bacillus amyloliquefaciens (Bacillus velezensis).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus amyloliquefaciens group.
OX NCBI_TaxID=1390;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-14, AND FUNCTION.
RC STRAIN=ATCC 49763 / H;
RX PubMed=1901989; DOI=10.1093/nar/19.4.841;
RA Brooks J.E., Nathan P.D., Landry D., Sznyter L.A., White-Rees P.,
RA Ives C.L., Moran L.S., Slatko B.E., Benner J.S.;
RT "Characterization of the cloned BamHI restriction modification system: its
RT nucleotide sequence, properties of the methylase, and expression in
RT heterologous hosts.";
RL Nucleic Acids Res. 19:841-850(1991).
RN [2]
RP FUNCTION AS AN ENDONUCLEASE, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 49763 / H / RUB500;
RX PubMed=1177312; DOI=10.1016/s0022-2836(75)80028-3;
RA Wilson G.A., Young F.E.;
RT "Isolation of a sequence-specific endonuclease (BamI) from Bacillus
RT amyloliquefaciens H.";
RL J. Mol. Biol. 97:123-125(1975).
RN [3]
RP FUNCTION, SUBSTRATE SPECIFICITY, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 49763 / H;
RX PubMed=834250; DOI=10.1038/265082a0;
RA Roberts R.J., Wilson G.A., Young F.E.;
RT "Recognition sequence of specific endonuclease BamH.I from Bacillus
RT amyloliquefaciens H.";
RL Nature 265:82-84(1977).
RN [4]
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).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
RX PubMed=8145855; DOI=10.1038/368660a0;
RA Newman M., Strzelecka T., Dorner L.F., Schildkraut I., Aggarwal A.K.;
RT "Structure of restriction endonuclease BamHI and its relationship to
RT EcoRI.";
RL Nature 368:660-664(1994).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=9783752; DOI=10.1038/2352;
RA Viadiu H., Aggarwal A.K.;
RT "The role of metals in catalysis by the restriction endonuclease BamHI.";
RL Nat. Struct. Biol. 5:910-916(1998).
CC -!- FUNCTION: A P subtype restriction enzyme that recognizes the double-
CC stranded sequence 5'-GGATCC-3' and cleaves after G-1.
CC {ECO:0000269|PubMed:834250, ECO:0000303|PubMed:12654995,
CC ECO:0000305|PubMed:1177312, ECO:0000305|PubMed:1901989}.
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:1177312, ECO:0000269|PubMed:834250};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Note=Binds 2 magnesium ions per subunit.;
CC -!- SUBUNIT: Homodimer.
CC -!- MISCELLANEOUS: The protein sequnce was determined following expression
CC in E.coli. {ECO:0000269|PubMed:1901989}.
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DR EMBL; X55285; CAA38999.1; -; Genomic_DNA.
DR PIR; A38693; A38693.
DR PIR; S26844; S26844.
DR RefSeq; WP_013353547.1; NZ_VRTX01000001.1.
DR PDB; 1BAM; X-ray; 1.95 A; A=1-213.
DR PDB; 1BHM; X-ray; 2.20 A; A/B=1-213.
DR PDB; 1ESG; X-ray; 1.90 A; A/B=1-213.
DR PDB; 2BAM; X-ray; 2.00 A; A/B=1-213.
DR PDB; 3BAM; X-ray; 1.80 A; A/B=1-213.
DR PDBsum; 1BAM; -.
DR PDBsum; 1BHM; -.
DR PDBsum; 1ESG; -.
DR PDBsum; 2BAM; -.
DR PDBsum; 3BAM; -.
DR AlphaFoldDB; P23940; -.
DR SMR; P23940; -.
DR BindingDB; P23940; -.
DR ChEMBL; CHEMBL5928; -.
DR REBASE; 185; BamHI.
DR REBASE; 203435; Bam1267ORF3424P.
DR OMA; FALEWET; -.
DR BRENDA; 3.1.21.4; 630.
DR EvolutionaryTrace; P23940; -.
DR PRO; PR:P23940; -.
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; 3.40.91.20; -; 1.
DR InterPro; IPR011338; BamHI/BglII/BstY.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR004194; Restrct_endonuc_II_BamHI.
DR Pfam; PF02923; BamHI; 1.
DR PIRSF; PIRSF009309; Restrict_endonuc_II_BamHI; 1.
DR SUPFAM; SSF52980; SSF52980; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Endonuclease; Hydrolase;
KW Magnesium; Metal-binding; Nuclease; Restriction system.
FT CHAIN 1..213
FT /note="Type II restriction enzyme BamHI"
FT /id="PRO_0000077281"
FT ACT_SITE 94
FT ACT_SITE 111
FT ACT_SITE 113
FT BINDING 77
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT BINDING 94
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 94
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT BINDING 112
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:3BAM"
FT HELIX 10..18
FT /evidence="ECO:0007829|PDB:3BAM"
FT HELIX 20..34
FT /evidence="ECO:0007829|PDB:3BAM"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:3BAM"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:3BAM"
FT HELIX 62..70
FT /evidence="ECO:0007829|PDB:3BAM"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:3BAM"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:3BAM"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:1ESG"
FT STRAND 93..101
FT /evidence="ECO:0007829|PDB:3BAM"
FT STRAND 104..112
FT /evidence="ECO:0007829|PDB:3BAM"
FT HELIX 117..132
FT /evidence="ECO:0007829|PDB:3BAM"
FT STRAND 137..144
FT /evidence="ECO:0007829|PDB:3BAM"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:3BAM"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:3BAM"
FT HELIX 163..169
FT /evidence="ECO:0007829|PDB:3BAM"
FT STRAND 174..180
FT /evidence="ECO:0007829|PDB:3BAM"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:3BAM"
FT HELIX 200..205
FT /evidence="ECO:0007829|PDB:1ESG"
SQ SEQUENCE 213 AA; 24570 MW; FFE57F518F37D8D6 CRC64;
MEVEKEFITD EAKELLSKDK LIQQAYNEVK TSICSPIWPA TSKTFTINNT EKNCNGVVPI
KELCYTLLED TYNWYREKPL DILKLEKKKG GPIDVYKEFI ENSELKRVGM EFETGNISSA
HRSMNKLLLG LKHGEIDLAI ILMPIKQLAY YLTDRVTNFE ELEPYFELTE GQPFIFIGFN
AEAYNSNVPL IPKGSDGMSK RSIKKWKDKV ENK
