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Protein

Type-2 restriction enzyme BamHI

Gene

bamHIR

Organism
Bacillus amyloliquefaciens (Bacillus velezensis)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Recognizes the double-stranded sequence GGATCC and cleaves after G-1.1 Publication

Catalytic activityi

Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.2 Publications

Cofactori

Mg2+Note: Binds 2 magnesium ions per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi77Magnesium 21
Active sitei941
Metal bindingi94Magnesium 11
Metal bindingi94Magnesium 21
Active sitei1111
Metal bindingi112Magnesium 1; via carbonyl oxygen1
Active sitei1131

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

Restriction system

Keywords - Ligandi

Magnesium, Metal-binding

Protein family/group databases

REBASEi185. BamHI.

Names & Taxonomyi

Protein namesi
Recommended name:
Type-2 restriction enzyme BamHI (EC:3.1.21.42 Publications)
Short name:
R.BamHI
Alternative name(s):
Endonuclease BamHI
Type II restriction enzyme BamHI
Gene namesi
Name:bamHIR
OrganismiBacillus amyloliquefaciens (Bacillus velezensis)
Taxonomic identifieri1390 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL5928.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000772811 – 213Type-2 restriction enzyme BamHIAdd BLAST213

Interactioni

Subunit structurei

Homodimer.

Chemistry databases

BindingDBiP23940.

Structurei

Secondary structure

1213
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 8Combined sources7
Helixi10 – 18Combined sources9
Helixi20 – 34Combined sources15
Beta strandi43 – 48Combined sources6
Helixi58 – 61Combined sources4
Helixi62 – 70Combined sources9
Beta strandi75 – 78Combined sources4
Helixi81 – 84Combined sources4
Beta strandi87 – 89Combined sources3
Beta strandi93 – 101Combined sources9
Beta strandi104 – 112Combined sources9
Helixi117 – 132Combined sources16
Beta strandi137 – 144Combined sources8
Helixi146 – 149Combined sources4
Helixi159 – 162Combined sources4
Helixi163 – 169Combined sources7
Beta strandi174 – 180Combined sources7
Beta strandi182 – 185Combined sources4
Helixi200 – 205Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BAMX-ray1.95A1-213[»]
1BHMX-ray2.20A/B1-213[»]
1ESGX-ray1.90A/B1-213[»]
2BAMX-ray2.00A/B1-213[»]
3BAMX-ray1.80A/B1-213[»]
ProteinModelPortaliP23940.
SMRiP23940.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23940.

Family & Domainsi

Family and domain databases

Gene3Di3.40.91.20. 1 hit.
InterProiIPR011338. BamHI/BglII/BstY.
IPR011335. Restrct_endonuc-II-like.
IPR004194. Restrct_endonuc_II_BamHI.
[Graphical view]
PfamiPF02923. BamHI. 1 hit.
[Graphical view]
PIRSFiPIRSF009309. Restrict_endonuc_II_BamHI. 1 hit.
SUPFAMiSSF52980. SSF52980. 1 hit.

Sequencei

Sequence statusi: Complete.

P23940-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEVEKEFITD EAKELLSKDK LIQQAYNEVK TSICSPIWPA TSKTFTINNT
60 70 80 90 100
EKNCNGVVPI KELCYTLLED TYNWYREKPL DILKLEKKKG GPIDVYKEFI
110 120 130 140 150
ENSELKRVGM EFETGNISSA HRSMNKLLLG LKHGEIDLAI ILMPIKQLAY
160 170 180 190 200
YLTDRVTNFE ELEPYFELTE GQPFIFIGFN AEAYNSNVPL IPKGSDGMSK
210
RSIKKWKDKV ENK
Length:213
Mass (Da):24,570
Last modified:March 1, 1992 - v1
Checksum:iFFE57F518F37D8D6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55285 Genomic DNA. Translation: CAA38999.1.
PIRiA38693.
S26844.
RefSeqiWP_013353547.1. NZ_LYUG01000003.1.

Genome annotation databases

GeneIDi9779203.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55285 Genomic DNA. Translation: CAA38999.1.
PIRiA38693.
S26844.
RefSeqiWP_013353547.1. NZ_LYUG01000003.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BAMX-ray1.95A1-213[»]
1BHMX-ray2.20A/B1-213[»]
1ESGX-ray1.90A/B1-213[»]
2BAMX-ray2.00A/B1-213[»]
3BAMX-ray1.80A/B1-213[»]
ProteinModelPortaliP23940.
SMRiP23940.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiP23940.
ChEMBLiCHEMBL5928.

Protein family/group databases

REBASEi185. BamHI.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi9779203.

Miscellaneous databases

EvolutionaryTraceiP23940.
PROiP23940.

Family and domain databases

Gene3Di3.40.91.20. 1 hit.
InterProiIPR011338. BamHI/BglII/BstY.
IPR011335. Restrct_endonuc-II-like.
IPR004194. Restrct_endonuc_II_BamHI.
[Graphical view]
PfamiPF02923. BamHI. 1 hit.
[Graphical view]
PIRSFiPIRSF009309. Restrict_endonuc_II_BamHI. 1 hit.
SUPFAMiSSF52980. SSF52980. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiT2BA_BACAM
AccessioniPrimary (citable) accession number: P23940
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: November 2, 2016
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Restriction enzymes and methylases
    Classification of restriction enzymes and methylases and list of entries

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.