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P02357 (RS5_GEOSE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
30S ribosomal protein S5

Short name=BS5
Alternative name(s):
BS6
Gene names
Name:rpsE
OrganismGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifier1422 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Protein attributes

Sequence length166 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

With S4 and S12 plays an important role in translational accuracy By similarity. HAMAP-Rule MF_01307_B

Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body By similarity. HAMAP-Rule MF_01307_B

Subunit structure

Part of the 30S ribosomal subunit. Contacts proteins S4 and S8 By similarity.

Domain

The N-terminal domain interacts with the head of the 30S subunit; the C-terminal domain interacts with the body and contacts protein S4. The interaction surface between S4 and S5 is involved in control of translational fidelity. HAMAP-Rule MF_01307_B

Sequence similarities

Belongs to the ribosomal protein S5P family.

Contains 1 S5 DRBM domain.

Ontologies

Keywords
   Biological processAntibiotic resistance
   LigandRNA-binding
rRNA-binding
   Molecular functionRibonucleoprotein
Ribosomal protein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processresponse to antibiotic

Inferred from electronic annotation. Source: UniProtKB-KW

translation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentsmall ribosomal subunit

Inferred from electronic annotation. Source: InterPro

   Molecular_functionrRNA binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

structural constituent of ribosome

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 16616630S ribosomal protein S5 HAMAP-Rule MF_01307_B
PRO_0000131469

Regions

Domain11 – 7464S5 DRBM

Secondary structure

........................ 166
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02357 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 774E82A2ED1D8EC5

FASTA16617,628
        10         20         30         40         50         60 
MRRINPNKLE LEERVVAVNR VAKVVKGGRR LRFSALVVVG DKNGHVGFGT GKAQEVPEAI 

        70         80         90        100        110        120 
RKAIEDAKKN LIEVPIVGTT IPHEVIGHFG AGEIILKPAS EGTGVIAGGP ARAVLELAGI 

       130        140        150        160 
SDILSKSIGS NTPINMVRAT FDGLKQLKRA EDVAKLRGKT VEELLG 

« Hide

References

[1]"Proteins of the Bacillus stearothermophilus ribosome. The amino acid sequences of proteins S5 and L30."
Kimura M.
J. Biol. Chem. 259:1051-1055(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Strain: ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924.
[2]"Cloning, sequencing, and overexpression of genes for ribosomal proteins from Bacillus stearothermophilus."
Ramakrishnan V., Gerchman S.E.
J. Biol. Chem. 266:880-885(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Procaryotic ribosomal proteins: N-terminal sequence homologies and structural correspondence of 30 S ribosomal proteins from Escherichia coli and Bacillus stearothermophilus."
Yaguchi M., Matheson A.T., Visentin L.P.
FEBS Lett. 46:296-300(1974) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-15.
Strain: DSM 13240 / CIP 106956 / 10.
[4]"Isolation and characterization of Bacillus stearothermophilus 30S and 50S ribosomal protein mutations."
Schnier J., Gewitz H.S., Behrens S.E., Lee A., Ginther C., Leighton T.
J. Bacteriol. 172:7306-7309(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: ISOLATION OF STREPTOMYCIN INDEPENDENT STRAINS.
Strain: 799.
[5]"The structure of ribosomal protein S5 reveals sites of interaction with 16S rRNA."
Ramakrishnan V., White S.W.
Nature 358:768-771(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
[6]"Ribosomal proteins S5 and L6: high-resolution crystal structures and roles in protein synthesis and antibiotic resistance."
Davies C., Bussiere D.E., Golden B.L., Porter S.J., Ramakrishnan V., White S.W.
J. Mol. Biol. 279:873-888(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M57621 Genomic DNA. Translation: AAA22699.1.
PIRR3BS5F. A02708.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DV4X-ray4.50E4-148[»]
1PKPX-ray2.80A1-150[»]
ProteinModelPortalP02357.
SMRP02357. Positions 4-148.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-112114.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.30.160.20. 1 hit.
3.30.230.10. 1 hit.
HAMAPMF_01307_B. Ribosomal_S5_B.
InterProIPR014720. dsRNA-bd_dom.
IPR000851. Ribosomal_S5.
IPR005712. Ribosomal_S5_bac-type.
IPR005324. Ribosomal_S5_C.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR013810. Ribosomal_S5_N.
IPR018192. Ribosomal_S5_N_CS.
[Graphical view]
PANTHERPTHR13718. PTHR13718. 1 hit.
PfamPF00333. Ribosomal_S5. 1 hit.
PF03719. Ribosomal_S5_C. 1 hit.
[Graphical view]
SUPFAMSSF54211. SSF54211. 1 hit.
TIGRFAMsTIGR01021. rpsE_bact. 1 hit.
PROSITEPS00585. RIBOSOMAL_S5. 1 hit.
PS50881. S5_DSRBD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP02357.

Entry information

Entry nameRS5_GEOSE
AccessionPrimary (citable) accession number: P02357
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: February 19, 2014
This is version 97 of the entry and version 1 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

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references