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P00648 (RNBR_BACAM) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribonuclease

EC=3.1.27.-
Alternative name(s):
Barnase
RNase Ba
OrganismBacillus amyloliquefaciens (Bacillus velezensis)
Taxonomic identifier1390 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length157 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes phosphodiester bonds in RNA, poly- and oligoribonucleotides resulting in 3'-nucleoside monophosphates via 2',3'-cyclophosphate intermediates.

Subcellular location

Secreted.

Biotechnological use

Introduced by genetic manipulation and expressed in male sterile maize and rape by Plant Genetic Systems and in radicchio rosso by Bejo Zaden. Barnase expressed in transgenic plants will specifically destroy the tissue(s) where it is expressed. After cell transformation, protein expression and plant regeneration, the active nuclease destroys the pollen producing organs thus rendering the plant sterile.

Sequence similarities

Belongs to the ribonuclease N1/T1 family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionEndonuclease
Hydrolase
Nuclease
   Technical term3D-structure
Direct protein sequencing
Genetically modified food
Gene Ontology (GO)
   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: InterPro

endoribonuclease activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3434
Propeptide35 – 4713
PRO_0000030828
Chain48 – 157110Ribonuclease Ref.3
PRO_0000030829

Sites

Active site1201Proton acceptor
Active site1491Proton donor

Experimental info

Mutagenesis1491H → Q: Loss of activity.

Secondary structure

.................... 157
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00648 [UniParc].

Last modified July 1, 1989. Version 2.
Checksum: 42B6669F9B0D7FBA

FASTA15717,473
        10         20         30         40         50         60 
MMKMEGIALK KRLSWISVCL LVLVSAAGML FSTAAKTETS SHKAHTEAQV INTFDGVADY 

        70         80         90        100        110        120 
LQTYHKLPDN YITKSEAQAL GWVASKGNLA DVAPGKSIGG DIFSNREGKL PGKSGRTWRE 

       130        140        150 
ADINYTSGFR NSDRILYSSD WLIYKTTDHY QTFTKIR 

« Hide

References

[1]"Cloning, sequencing and transcription of an inactivated copy of Bacillus amyloliquefaciens extracellular ribonuclease (barnase)."
Paddon C.J., Hartley R.W.
Gene 40:231-239(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Barnase and barstar. Expression of its cloned inhibitor permits expression of a cloned ribonuclease."
Hartley R.W.
J. Mol. Biol. 202:913-915(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 48-157.
[3]"Amino-acid sequence of extracellular ribonuclease (barnase) of Bacillus amyloliquefaciens."
Hartley R.W., Barker E.A.
Nature New Biol. 235:15-16(1972) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 48-157.
[4]"Determination of the three-dimensional solution structure of barnase using nuclear magnetic resonance spectroscopy."
Bycroft M., Ludvigsen S., Fersht A.R., Poulsen F.M.
Biochemistry 30:8697-8701(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[5]"An N-terminal fragment of barnase has residual helical structure similar to that in a refolding intermediate."
Sancho J., Neira J.L., Fersht A.R.
J. Mol. Biol. 224:749-758(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 48-83.
[6]"Three-dimensional structure of binase in solution."
Reibarkh M.Y.A., Nolde D.E., Vasilieva L.I., Bocharov E.V., Shulga A.A., Kirpichnikov M.P., Arseniev A.S.
FEBS Lett. 431:250-254(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 48-157.
[7]"Crystal structure of a barnase-d(GpC) complex at 1.9-A resolution."
Baudet S., Janin J.
J. Mol. Biol. 219:123-132(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[8]"Recognition between a bacterial ribonuclease, barnase, and its natural inhibitor, barstar."
Guillet V., Lapthorn A., Hartley R.W., Mauguen Y.
Structure 1:165-177(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF COMPLEX WITH BARNASE.
[9]"A structural double-mutant cycle: estimating the strength of a buried salt bridge in barnase."
Vaughan C.K., Harryson P., Buckle A.M., Fersht A.R.
Acta Crystallogr. D 58:591-600(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[10]"Barnase and barstar: two small proteins to fold and fit together."
Hartley R.W.
Trends Biochem. Sci. 14:450-454(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M14442 Genomic DNA. Translation: AAA86441.1.
X12871 Genomic DNA. Translation: CAA31365.1.
PIRNRBSN. A24038.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A2PX-ray1.50A/B/C48-157[»]
1B20X-ray1.70A/B/C48-157[»]
1B21X-ray2.00A/B/C48-157[»]
1B27X-ray2.10A/B/C48-157[»]
1B2SX-ray1.82A/B/C48-157[»]
1B2UX-ray2.10A/B/C48-157[»]
1B2XX-ray1.80A/B/C48-157[»]
1B2ZX-ray2.03A/B/C48-157[»]
1B3SX-ray2.39A/B/C48-157[»]
1BANX-ray2.20A/B/C48-157[»]
1BAOX-ray2.20A/B/C48-157[»]
1BGSX-ray2.60A/B/C48-157[»]
1BNEX-ray2.10A/B/C48-157[»]
1BNFX-ray2.00A/B/C48-157[»]
1BNGX-ray2.10A/B/C48-157[»]
1BNIX-ray2.10A/B/C48-157[»]
1BNJX-ray2.10A/B/C48-157[»]
1BNRNMR-A48-157[»]
1BNSX-ray2.05A/B/C48-157[»]
1BRGX-ray2.20A/B/C50-157[»]
1BRHX-ray2.00A/B/C48-157[»]
1BRIX-ray1.90A/B/C48-157[»]
1BRJX-ray2.00A/B/C48-157[»]
1BRKX-ray2.00A/B/C48-157[»]
1BRNX-ray1.76L/M48-157[»]
1BRSX-ray2.00A/B/C48-157[»]
1BSAX-ray2.00A/B/C48-157[»]
1BSBX-ray2.00A/B/C48-157[»]
1BSCX-ray2.00A/B/C48-157[»]
1BSDX-ray2.30A/B/C48-157[»]
1BSEX-ray2.00A/B/C48-157[»]
1FW7NMR-A48-157[»]
1RNBX-ray1.90A48-157[»]
1X1UX-ray2.30A/B/C48-157[»]
1X1WX-ray2.10A/B/C48-157[»]
1X1XX-ray2.30A/B/C48-157[»]
1X1YX-ray1.90A/B/C50-157[»]
1YVSX-ray2.20A48-157[»]
2C4BX-ray1.30A/B49-157[»]
2F4YX-ray2.15A/B/C50-157[»]
2F56X-ray1.96A/B/C50-157[»]
2F5MX-ray1.95A/B/C50-157[»]
2F5WX-ray2.00A/B/C50-157[»]
2KF3NMR-A48-157[»]
2KF4NMR-A48-157[»]
2KF5NMR-A48-157[»]
2KF6NMR-A48-157[»]
2ZA4X-ray1.58A/C48-157[»]
3DA7X-ray2.25A/B/E/G48-157[»]
3KCHX-ray1.94A/B/C48-157[»]
3Q3FX-ray2.17A48-157[»]
ProteinModelPortalP00648.
SMRP00648. Positions 48-157.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-544N.
IntActP00648. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.10.450.30. 1 hit.
InterProIPR001887. Barnase.
IPR000026. Gua-sp_ribonuclease_N1/T1.
IPR016191. Ribonuclease/ribotoxin.
[Graphical view]
PfamPF00545. Ribonuclease. 1 hit.
[Graphical view]
PIRSFPIRSF001013. Barnase. 1 hit.
PRINTSPR00117. BARNASE.
SUPFAMSSF53933. SSF53933. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP00648.

Entry information

Entry nameRNBR_BACAM
AccessionPrimary (citable) accession number: P00648
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 1, 1989
Last modified: April 16, 2014
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references