Ribonuclease precursor - Bacillus amyloliquefaciens

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P00648 (RNBR_BACAM) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 101. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names	Recommended name: Ribonuclease EC=3.1.27.- Alternative name(s): Barnase RNase Ba
Organism	Bacillus amyloliquefaciens (Bacillus velezensis)
Taxonomic identifier	1390 [NCBI]
Taxonomic lineage	cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group

Protein attributes

Sequence length	157 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Secreted
Domain	Signal
Molecular function	Endonuclease Hydrolase Nuclease
Technical term	3D-structure Direct protein sequencing Genetically modified food
Gene Ontology (GO)
Biological_process	nucleic acid phosphodiester bond hydrolysis Inferred from electronic annotation. Source: GOC
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	RNA binding Inferred from electronic annotation. Source: InterPro endoribonuclease activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 34

Propeptide

35 – 47

PRO_0000030828

Chain

48 – 157

110

Ribonuclease Ref.3

PRO_0000030829

Sites

Active site

120

Proton acceptor

Active site

149

Proton donor

Experimental info

Mutagenesis

149

H → Q: Loss of activity.

Secondary structure

157

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P00648 [UniParc].

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

FASTA

157

17,473

        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.

PIR

NRBSN. A24038.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A2P	X-ray	1.50	A/B/C	48-157	[»]
1B20	X-ray	1.70	A/B/C	48-157	[»]
1B21	X-ray	2.00	A/B/C	48-157	[»]
1B27	X-ray	2.10	A/B/C	48-157	[»]
1B2S	X-ray	1.82	A/B/C	48-157	[»]
1B2U	X-ray	2.10	A/B/C	48-157	[»]
1B2X	X-ray	1.80	A/B/C	48-157	[»]
1B2Z	X-ray	2.03	A/B/C	48-157	[»]
1B3S	X-ray	2.39	A/B/C	48-157	[»]
1BAN	X-ray	2.20	A/B/C	48-157	[»]
1BAO	X-ray	2.20	A/B/C	48-157	[»]
1BGS	X-ray	2.60	A/B/C	48-157	[»]
1BNE	X-ray	2.10	A/B/C	48-157	[»]
1BNF	X-ray	2.00	A/B/C	48-157	[»]
1BNG	X-ray	2.10	A/B/C	48-157	[»]
1BNI	X-ray	2.10	A/B/C	48-157	[»]
1BNJ	X-ray	2.10	A/B/C	48-157	[»]
1BNR	NMR	-	A	48-157	[»]
1BNS	X-ray	2.05	A/B/C	48-157	[»]
1BRG	X-ray	2.20	A/B/C	50-157	[»]
1BRH	X-ray	2.00	A/B/C	48-157	[»]
1BRI	X-ray	1.90	A/B/C	48-157	[»]
1BRJ	X-ray	2.00	A/B/C	48-157	[»]
1BRK	X-ray	2.00	A/B/C	48-157	[»]
1BRN	X-ray	1.76	L/M	48-157	[»]
1BRS	X-ray	2.00	A/B/C	48-157	[»]
1BSA	X-ray	2.00	A/B/C	48-157	[»]
1BSB	X-ray	2.00	A/B/C	48-157	[»]
1BSC	X-ray	2.00	A/B/C	48-157	[»]
1BSD	X-ray	2.30	A/B/C	48-157	[»]
1BSE	X-ray	2.00	A/B/C	48-157	[»]
1FW7	NMR	-	A	48-157	[»]
1RNB	X-ray	1.90	A	48-157	[»]
1X1U	X-ray	2.30	A/B/C	48-157	[»]
1X1W	X-ray	2.10	A/B/C	48-157	[»]
1X1X	X-ray	2.30	A/B/C	48-157	[»]
1X1Y	X-ray	1.90	A/B/C	50-157	[»]
1YVS	X-ray	2.20	A	48-157	[»]
2C4B	X-ray	1.30	A/B	49-157	[»]
2F4Y	X-ray	2.15	A/B/C	50-157	[»]
2F56	X-ray	1.96	A/B/C	50-157	[»]
2F5M	X-ray	1.95	A/B/C	50-157	[»]
2F5W	X-ray	2.00	A/B/C	50-157	[»]
2KF3	NMR	-	A	48-157	[»]
2KF4	NMR	-	A	48-157	[»]
2KF5	NMR	-	A	48-157	[»]
2KF6	NMR	-	A	48-157	[»]
2ZA4	X-ray	1.58	A/C	48-157	[»]
3DA7	X-ray	2.25	A/B/E/G	48-157	[»]
3KCH	X-ray	1.94	A/B/C	48-157	[»]
3Q3F	X-ray	2.17	A	48-157	[»]

ProteinModelPortal

P00648.

SMR

P00648. Positions 48-157.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-544N.

IntAct

P00648. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

3.10.450.30. 1 hit.

InterPro

IPR001887. Barnase.
IPR000026. Gua-sp_ribonuclease_N1/T1.
IPR016191. Ribonuclease/ribotoxin.
[Graphical view]

Pfam

PF00545. Ribonuclease. 1 hit.
[Graphical view]

PIRSF

PIRSF001013. Barnase. 1 hit.

PRINTS

PR00117. BARNASE.

SUPFAM

SSF53933. Ribonuclease/ribotoxin. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P00648.

Entry information

Entry name

RNBR_BACAM

Accession

Primary (citable) accession number: P00648

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 1, 1989
Last modified:	April 3, 2013
This is version 101 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Family and domain databases

Other

Entry information

Relevant documents