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P00648

- RNBR_BACAM

UniProt

P00648 - RNBR_BACAM

Protein

Ribonuclease

Gene
N/A
Organism
Bacillus amyloliquefaciens (Bacillus velezensis)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei120 – 1201Proton acceptor
    Active sitei149 – 1491Proton donor

    GO - Molecular functioni

    1. endoribonuclease activity Source: InterPro
    2. RNA binding Source: InterPro

    Keywords - Molecular functioni

    Endonuclease, Hydrolase, Nuclease

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribonuclease (EC:3.1.27.-)
    Alternative name(s):
    Barnase
    RNase Ba
    OrganismiBacillus amyloliquefaciens (Bacillus velezensis)
    Taxonomic identifieri1390 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Biotechnological usei

    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.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi149 – 1491H → Q: Loss of activity.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3434Add
    BLAST
    Propeptidei35 – 47131 PublicationPRO_0000030828Add
    BLAST
    Chaini48 – 157110Ribonuclease1 PublicationPRO_0000030829Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    DIPiDIP-544N.
    IntActiP00648. 1 interaction.

    Structurei

    Secondary structure

    1
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi54 – 6411
    Helixi74 – 796
    Helixi84 – 863
    Helixi89 – 924
    Beta strandi97 – 1037
    Beta strandi118 – 1225
    Beta strandi127 – 1293
    Beta strandi134 – 1385
    Beta strandi143 – 1486
    Beta strandi154 – 1574

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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/C48-157[»]
    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/G48-113[»]
    3KCHX-ray1.94A/B/C48-157[»]
    3Q3FX-ray2.17A48-157[»]
    ProteinModelPortaliP00648.
    SMRiP00648. Positions 48-157.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00648.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribonuclease N1/T1 family.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.10.450.30. 1 hit.
    InterProiIPR001887. Barnase.
    IPR000026. Gua-sp_ribonuclease_N1/T1.
    IPR016191. Ribonuclease/ribotoxin.
    [Graphical view]
    PfamiPF00545. Ribonuclease. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001013. Barnase. 1 hit.
    PRINTSiPR00117. BARNASE.
    SUPFAMiSSF53933. SSF53933. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P00648-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMKMEGIALK KRLSWISVCL LVLVSAAGML FSTAAKTETS SHKAHTEAQV    50
    INTFDGVADY LQTYHKLPDN YITKSEAQAL GWVASKGNLA DVAPGKSIGG 100
    DIFSNREGKL PGKSGRTWRE ADINYTSGFR NSDRILYSSD WLIYKTTDHY 150
    QTFTKIR 157
    Length:157
    Mass (Da):17,473
    Last modified:July 1, 1989 - v2
    Checksum:i42B6669F9B0D7FBA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14442 Genomic DNA. Translation: AAA86441.1.
    X12871 Genomic DNA. Translation: CAA31365.1.
    PIRiA24038. NRBSN.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14442 Genomic DNA. Translation: AAA86441.1 .
    X12871 Genomic DNA. Translation: CAA31365.1 .
    PIRi A24038. NRBSN.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 48-157 [» ]
    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 48-113 [» ]
    3KCH X-ray 1.94 A/B/C 48-157 [» ]
    3Q3F X-ray 2.17 A 48-157 [» ]
    ProteinModelPortali P00648.
    SMRi P00648. Positions 48-157.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-544N.
    IntActi P00648. 1 interaction.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P00648.

    Family and domain databases

    Gene3Di 3.10.450.30. 1 hit.
    InterProi IPR001887. Barnase.
    IPR000026. Gua-sp_ribonuclease_N1/T1.
    IPR016191. Ribonuclease/ribotoxin.
    [Graphical view ]
    Pfami PF00545. Ribonuclease. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001013. Barnase. 1 hit.
    PRINTSi PR00117. BARNASE.
    SUPFAMi SSF53933. SSF53933. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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. 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.

    Entry informationi

    Entry nameiRNBR_BACAM
    AccessioniPrimary (citable) accession number: P00648
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 106 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing, Genetically modified food

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3