Reviewed, UniProtKB/Swiss-Prot P23940 (T2BA_BACAM)

Names and origin

Protein names

Recommended name:
    Type-2 restriction enzyme BamHI
      Short name=R.BamHI
    EC=3.1.21.4
Alternative name(s):
    Type II restriction enzyme BamHI
    Endonuclease BamHI

Gene names

Name:

bamHIR

Encoded on

Plasmid

Organism

Bacillus amyloliquefaciens

Taxonomic identifier

1390 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	213 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Recognizes the double-stranded sequence GGATCC and cleaves after G-1.
Catalytic activity	Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.
Cofactor	Binds 2 magnesium ions per subunit.
Subunit structure	Homodimer.

Ontologies

Keywords
Biological process	Restriction system
Ligand	Magnesium Metal-binding
Molecular function	Endonuclease Hydrolase Nuclease
Technical term	3D-structure Direct protein sequencing Plasmid
Gene Ontology (GO)
Biological process	DNA restriction-modification system Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro Type II site-specific deoxyribonuclease activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 213

213

Type-2 restriction enzyme BamHI

PRO_0000077281

Sites

Active site

94

1

Active site

111

1

Active site

113

1

Metal binding

77

1

Magnesium 2

Metal binding

94

1

Magnesium 1

Metal binding

94

1

Magnesium 2

Metal binding

112

1

Magnesium 1; via carbonyl oxygen

Secondary structure

1

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213

Helix Strand Turn

Details...

Beta strand

2 – 8

7

Helix

10 – 16

7

Helix

20 – 34

15

Beta strand

43 – 48

6

Helix

58 – 72

15

Beta strand

94 – 101

8

Beta strand

104 – 112

9

Helix

117 – 132

16

Beta strand

137 – 144

8

Helix

146 – 149

4

Helix

159 – 162

4

Helix

163 – 169

7

Beta strand

174 – 180

7

Beta strand

182 – 185

4

Helix

200 – 211

12

Sequences

	Sequence		Length	Mass (Da)
	P23940-1 [UniParc]. Last modified March 1, 1992. Version 1. Checksum: FFE57F518F37D8D6	FASTA	213	24,570
	10 20 30 40 50 60 MEVEKEFITD EAKELLSKDK LIQQAYNEVK TSICSPIWPA TSKTFTINNT EKNCNGVVPI 70 80 90 100 110 120 KELCYTLLED TYNWYREKPL DILKLEKKKG GPIDVYKEFI ENSELKRVGM EFETGNISSA 130 140 150 160 170 180 HRSMNKLLLG LKHGEIDLAI ILMPIKQLAY YLTDRVTNFE ELEPYFELTE GQPFIFIGFN 190 200 210 AEAYNSNVPL IPKGSDGMSK RSIKKWKDKV ENK

References

[1]	"Characterization of the cloned BamHI restriction modification system: its nucleotide sequence, properties of the methylase, and expression in heterologous hosts." Brooks J.E., Nathan P.D., Landry D., Sznyter L.A., White-Rees P., Ives C.L., Moran L.S., Slatko B.E., Benner J.S. Nucleic Acids Res. 19:841-850(1991) [PubMed: 1901989] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-8 AND 11-14. Strain: 168.
[2]	"Structure of restriction endonuclease BamHI and its relationship to EcoRI." Newman M., Strzelecka T., Dorner L.F., Schildkraut I., Aggarwal A.K. Nature 368:660-664(1994) [PubMed: 8145855] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
[3]	"The role of metals in catalysis by the restriction endonuclease BamHI." Viadiu H., Aggarwal A.K. Nat. Struct. Biol. 5:910-916(1998) [PubMed: 9783752] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X55285 Genomic DNA. Translation: CAA38999.1.

PIR

A38693.
S26844.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BAM	X-ray	1.95	A	1-213	[»]
1BHM	X-ray	2.20	A/B	1-213	[»]
1ESG	X-ray	1.90	A/B	1-213	[»]
2BAM	X-ray	2.00	A/B	1-213	[»]
3BAM	X-ray	1.80	A/B	1-213	[»]

ModBase

Search...

Protein family/group databases

REBASE

185. BamHI.

Enzyme and pathway databases

BRENDA

3.1.21.4. 1130.

Family and domain databases

InterPro

IPR011338. Restrct_endonuc_II_BamHI/BglII.
IPR004194. Restrict_endonuc_II_BamHI.
[Graphical view]

Gene3D

G3DSA:3.40.91.20. Restrct_endonuc_II_BamHI/BglII. 1 hit.

Pfam

PF02923. BamHI. 1 hit.
[Graphical view]

PIRSF

PIRSF009309. Restrict_endonuc_II_BamHI. 1 hit.

ProDom

PD026987. BamHI. 1 hit.
[Graphical view] [Entries sharing at least one domain]

ProtoNet

Search...

Entry information

Entry name

T2BA_BACAM

Accession

Primary (citable) accession number: P23940

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	March 1, 1992
Last modified:	June 16, 2009
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)