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Protein

Barstar

Gene
N/A
Organism
Bacillus amyloliquefaciens (Bacillus velezensis)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Inhibitor of the ribonuclease barnase. Forms a one-to-one non-covalent complex.

Names & Taxonomyi

Protein namesi
Recommended name:
Barstar
Alternative name(s):
Ribonuclease inhibitor
OrganismiBacillus amyloliquefaciens (Bacillus velezensis)
Taxonomic identifieri1390 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved
Chaini2 – 9089BarstarPRO_0000064827Add
BLAST

Interactioni

Protein-protein interaction databases

DIPiDIP-621N.
IntActiP11540. 2 interactions.
MINTiMINT-1539643.
STRINGi326423.RBAM_008490.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 76Combined sources
Helixi8 – 103Combined sources
Helixi14 – 2411Combined sources
Helixi35 – 4410Combined sources
Beta strandi48 – 558Combined sources
Helixi57 – 637Combined sources
Turni64 – 663Combined sources
Helixi67 – 8014Combined sources
Beta strandi85 – 906Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A19X-ray2.76A/B1-90[»]
1AB7NMR-A2-90[»]
1AY7X-ray1.70B2-90[»]
1B27X-ray2.10D/E/F1-90[»]
1B2SX-ray1.82D/E/F1-90[»]
1B2UX-ray2.10D/E/F1-90[»]
1B3SX-ray2.39D/E/F1-90[»]
1BGSX-ray2.60E/F/G2-90[»]
1BRSX-ray2.00D/E/F2-90[»]
1BTANMR-A2-90[»]
1BTBNMR-A2-90[»]
1L1KNMR-A2-21[»]
1X1UX-ray2.30D/E/F2-90[»]
1X1WX-ray2.10D/E/F1-90[»]
1X1XX-ray2.30D/E/F2-90[»]
1X1YX-ray1.90D/E/F1-90[»]
2HXXX-ray2.00A/B2-90[»]
2ZA4X-ray1.58B/D1-90[»]
3DA7X-ray2.25C/D/F/H1-90[»]
ProteinModelPortaliP11540.
SMRiP11540. Positions 2-90.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11540.

Family & Domainsi

Sequence similaritiesi

Belongs to the barstar family.Curated

Phylogenomic databases

eggNOGiCOG2732. LUCA.

Family and domain databases

Gene3Di3.30.370.10. 1 hit.
InterProiIPR000468. Barstar.
[Graphical view]
PfamiPF01337. Barstar. 1 hit.
[Graphical view]
SUPFAMiSSF52038. SSF52038. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P11540-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKAVINGEQ IRSISDLHQT LKKELALPEY YGENLDALWD CLTGWVEYPL
60 70 80 90
VLEWRQFEQS KQLTENGAES VLQVFREAKA EGCDITIILS
Length:90
Mass (Da):10,343
Last modified:January 23, 2007 - v3
Checksum:i3A8E7A2348DEEC98
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15545 Genomic DNA. Translation: CAA33551.1.
PIRiS01373.
RefSeqiWP_013351425.1. NZ_LQYP01000016.1.

Genome annotation databases

GeneIDi9780711.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15545 Genomic DNA. Translation: CAA33551.1.
PIRiS01373.
RefSeqiWP_013351425.1. NZ_LQYP01000016.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A19X-ray2.76A/B1-90[»]
1AB7NMR-A2-90[»]
1AY7X-ray1.70B2-90[»]
1B27X-ray2.10D/E/F1-90[»]
1B2SX-ray1.82D/E/F1-90[»]
1B2UX-ray2.10D/E/F1-90[»]
1B3SX-ray2.39D/E/F1-90[»]
1BGSX-ray2.60E/F/G2-90[»]
1BRSX-ray2.00D/E/F2-90[»]
1BTANMR-A2-90[»]
1BTBNMR-A2-90[»]
1L1KNMR-A2-21[»]
1X1UX-ray2.30D/E/F2-90[»]
1X1WX-ray2.10D/E/F1-90[»]
1X1XX-ray2.30D/E/F2-90[»]
1X1YX-ray1.90D/E/F1-90[»]
2HXXX-ray2.00A/B2-90[»]
2ZA4X-ray1.58B/D1-90[»]
3DA7X-ray2.25C/D/F/H1-90[»]
ProteinModelPortaliP11540.
SMRiP11540. Positions 2-90.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-621N.
IntActiP11540. 2 interactions.
MINTiMINT-1539643.
STRINGi326423.RBAM_008490.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi9780711.

Phylogenomic databases

eggNOGiCOG2732. LUCA.

Miscellaneous databases

EvolutionaryTraceiP11540.

Family and domain databases

Gene3Di3.30.370.10. 1 hit.
InterProiIPR000468. Barstar.
[Graphical view]
PfamiPF01337. Barstar. 1 hit.
[Graphical view]
SUPFAMiSSF52038. SSF52038. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "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].
  2. "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.
  3. "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.
  4. "Recognition of RNase Sa by the inhibitor barstar: structure of the complex at 1.7 A resolution."
    Sevcik J., Urbanikova L., Dauter Z., Wilson K.S.
    Acta Crystallogr. D 54:954-963(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF COMPLEX WITH RNASE SA.
  5. "Assignment of the backbone 1H and 15N NMR resonances and secondary structure characterization of barstar."
    Lubienski M.J., Bycroft M., Jones D.N.M., Fersht A.R.
    FEBS Lett. 332:81-87(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  6. "Three-dimensional solution structure and 13C assignments of barstar using nuclear magnetic resonance spectroscopy."
    Lubienski M.J., Bycroft M., Freund S.M.V., Fersht A.R.
    Biochemistry 33:8866-8877(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiBARS_BACAM
AccessioniPrimary (citable) accession number: P11540
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 97 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

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

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.