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P0A7W1 (RS5_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
30S ribosomal protein S5
Gene names
Name:rpsE
Synonyms:spc
Ordered Locus Names:b3303, JW3265
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length167 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

With S4 and S12 plays an important role in translational accuracy. Many suppressors of streptomycin-dependent mutants of protein S12 are found in this protein, some but not all of which decrease translational accuracy (ram, ribosomal ambiguity mutations). Ref.10

Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body. Ref.10

The physical location of this protein suggests it may also play a role in mRNA unwinding by the ribosome, possibly by forming part of a processivity clamp. Ref.10

Subunit structure

Part of the 30S ribosomal subunit. Contacts proteins S4 and S8. With proteins S4 and S5 encircles the mRNA as it enters the ribosome, which may play a role in mRNA helicase processivity. Can be cross-linked to mRNA.

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

Miscellaneous

Altered S5 proteins have been identified in a number of mutants. Some mutations in S5 have been shown to increase translational error frequencies.

Some mutants in this protein can partially suppress an alanyl-tRNA synthetase mutant.

Sequence similarities

Belongs to the ribosomal protein S5P family.

Contains 1 S5 DRBM domain.

Mass spectrometry

Molecular mass is 17514.8 Da from positions 2 - 167. Determined by MALDI. Ref.11

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 16716630S ribosomal protein S5 HAMAP-Rule MF_01307_B
PRO_0000131511

Regions

Domain11 – 7464S5 DRBM

Amino acid modifications

Modified residue21N-acetylalanine Ref.4

Natural variations

Natural variant201R → L in strain: SPCR9; spectinomycin resistant. Not a ram mutation.
Natural variant211V → E in strain: SPCR7; spectinomycin resistant. Not a ram mutation.
Natural variant221S → P in strain: SPCR13 and SPCR15; spectinomycin resistant. Not a ram mutation.
Natural variant1041G → R in strain: N-660; suppresses S12 streptomycin dependence.
Natural variant1121R → G in strain: NEA-314; neamycin resistant.
Natural variant1121R → L in strain: N-421 and D-1023; suppresses S12 streptomycin-dependence.
Natural variant1121R → S in strain: NEA-319; neamycin resistant.
Natural variant1511E → S in strain: B.
Natural variant162 – 1676EEILGK → G in strain: 0-1; suppresses an alanyl-tRNA synthetase mutation. Blocks ribosome assembly below 25 degrees Celsius.

Experimental info

Mutagenesis20 – 2910RVSKTVKGGR → AVSKTVKGGA: No effect on mRNA unwinding ability of the ribosome.

Secondary structure

.................................... 167
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A7W1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 0B7EA2CB34018CAB

FASTA16717,603
        10         20         30         40         50         60 
MAHIEKQAGE LQEKLIAVNR VSKTVKGGRI FSFTALTVVG DGNGRVGFGY GKAREVPAAI 

        70         80         90        100        110        120 
QKAMEKARRN MINVALNNGT LQHPVKGVHT GSRVFMQPAS EGTGIIAGGA MRAVLEVAGV 

       130        140        150        160 
HNVLAKAYGS TNPINVVRAT IDGLENMNSP EMVAAKRGKS VEEILGK 

« Hide

References

« Hide 'large scale' references
[1]"The spc ribosomal protein operon of Escherichia coli: sequence and cotranscription of the ribosomal protein genes and a protein export gene."
Cerretti D.P., Dean D., Davis G.R., Bedwell D.M., Nomura M.
Nucleic Acids Res. 11:2599-2616(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"The primary structure of protein S5 from the small subunit of the Escherichia coli ribosome."
Wittmann-Liebold B., Greuer B.
FEBS Lett. 95:91-98(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-167, ACETYLATION AT ALA-2, VARIANTS, MUTANTS.
Strain: B and K.
[5]"Localization of the amino-acid exchange in protein S5 from an Escherichia coli mutant resistant to spectinomycin."
DeWilde M., Wittmann-Liebold B.
Mol. Gen. Genet. 127:273-276(1973) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 15-23, VARIANT SPECTINOMYCIN RESISTANT.
Strain: B.
[6]"Requirement of proteins S5 and S9 from 30S subunits for the ribosome-dependent GTPase activity of elongation factor G."
Marsh R.C., Parmeggiani A.
Proc. Natl. Acad. Sci. U.S.A. 70:151-155(1973) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN FORMATION OF THE EF-G/RIBOSOME COMPLEX.
Strain: B/2.
[7]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[8]"Ribosomal RNA and protein mutants resistant to spectinomycin."
Bilgin N., Richter A.A., Ehrenberg M., Dahlberg A.E., Kurland C.G.
EMBO J. 9:735-739(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS.
Strain: O17.
[9]"The path of mRNA through the Escherichia coli ribosome; site-directed cross-linking of mRNA analogues carrying a photo-reactive label at various points 3' to the decoding site."
Rinke-Appel J., Juenke N., Stade K., Brimacombe R.
EMBO J. 10:2195-2202(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: CROSS-LINKING TO MRNA.
[10]"mRNA helicase activity of the ribosome."
Takyar S., Hickerson R.P., Noller H.F.
Cell 120:49-58(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ROLE IN MRNA HELICASE ACTIVITY, MUTAGENESIS.
Strain: MRE-600.
[11]"Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry."
Arnold R.J., Reilly J.P.
Anal. Biochem. 269:105-112(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: MASS SPECTROMETRY.
Strain: K12 / ATCC 25404 / DSM 5698 / NCIMB 11290.
[12]"All-atom homology model of the Escherichia coli 30S ribosomal subunit."
Tung C.-S., Joseph S., Sanbonmatsu K.Y.
Nat. Struct. Biol. 9:750-755(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING.
[13]"Study of the structural dynamics of the E. coli 70S ribosome using real-space refinement."
Gao H., Sengupta J., Valle M., Korostelev A., Eswar N., Stagg S.M., Van Roey P., Agrawal R.K., Harvey S.C., Sali A., Chapman M.S., Frank J.
Cell 113:789-801(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS).
Strain: MRE-600.
[14]"Structures of the bacterial ribosome at 3.5 A resolution."
Schuwirth B.S., Borovinskaya M.A., Hau C.W., Zhang W., Vila-Sanjurjo A., Holton J.M., Cate J.H.D.
Science 310:827-834(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
Strain: MRE-600.
[15]"Limitations of translational accuracy."
Kurland C.G., Hughes D., Ehrenberg M.
(In) Neidhardt F.C., Curtiss R. III, Ingraham J.L., Lin E.C.C., Low K.B. Magasanik B., Reznikoff W.S., Riley M., Schaechter M., Umbarger H.E. (eds.); Escherichia coli and Salmonella: Cellular and molecular biology (2nd ed.), pp.979-1004, American Society for Microbiology Press, Washington D.C. (1996)
Cited for: REVIEW ON TRANSLATIONAL ACCURACY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X01563 Genomic DNA. Translation: CAA25722.1.
U18997 Genomic DNA. Translation: AAA58100.1.
U00096 Genomic DNA. Translation: AAC76328.1.
AP009048 Genomic DNA. Translation: BAE77988.1.
PIRR3EC5. B65123.
RefSeqNP_417762.1. NC_000913.3.
YP_492129.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EG0electron microscopy11.50B1-148[»]
1M5Gmodel-E10-159[»]
1P6Gelectron microscopy12.30E2-167[»]
1P87electron microscopy11.50E2-167[»]
1VS5X-ray3.46E1-167[»]
1VS7X-ray3.46E1-167[»]
2AVYX-ray3.46E2-167[»]
2AW7X-ray3.46E2-167[»]
2GY9electron microscopy15.00E10-157[»]
2GYBelectron microscopy15.00E10-157[»]
2I2PX-ray3.22E2-167[»]
2I2UX-ray3.22E2-167[»]
2QALX-ray3.21E2-167[»]
2QANX-ray3.21E2-167[»]
2QB9X-ray3.54E2-167[»]
2QBBX-ray3.54E2-167[»]
2QBDX-ray3.30E2-167[»]
2QBFX-ray3.30E2-167[»]
2QBHX-ray4.00E2-167[»]
2QBJX-ray4.00E2-167[»]
2QOUX-ray3.93E2-167[»]
2QOWX-ray3.93E2-167[»]
2QOYX-ray3.50E2-167[»]
2QP0X-ray3.50E2-167[»]
2VHOX-ray3.74E2-167[»]
2VHPX-ray3.74E2-167[»]
2WWLelectron microscopy5.80E10-159[»]
2YKRelectron microscopy9.80E10-159[»]
2Z4KX-ray4.45E2-167[»]
2Z4MX-ray4.45E2-167[»]
3DF1X-ray3.50E2-167[»]
3DF3X-ray3.50E2-166[»]
3E1Aelectron microscopy-S1-159[»]
3E1Celectron microscopy-S1-159[»]
3FIHelectron microscopy6.70E10-159[»]
3I1MX-ray3.19E1-167[»]
3I1OX-ray3.19E1-167[»]
3I1QX-ray3.81E1-167[»]
3I1SX-ray3.81E1-167[»]
3I1ZX-ray3.71E1-167[»]
3I21X-ray3.71E1-167[»]
3IZVelectron microscopy-I1-167[»]
3IZWelectron microscopy-I1-167[»]
3J00electron microscopy-E2-167[»]
3J0Uelectron microscopy12.10H2-167[»]
3J0Velectron microscopy14.70H2-167[»]
3J0Xelectron microscopy13.50H2-167[»]
3J0Zelectron microscopy11.50H2-167[»]
3J10electron microscopy11.50H2-167[»]
3J13electron microscopy13.10G2-167[»]
3J18electron microscopy8.30E10-159[»]
3J36electron microscopy9.80E2-167[»]
3J4Velectron microscopy12.00E10-159[»]
3J4Welectron microscopy12.00E10-159[»]
3J4Yelectron microscopy17.00E10-159[»]
3J4Zelectron microscopy20.00E10-159[»]
3J53electron microscopy13.00E10-159[»]
3J55electron microscopy15.00E10-159[»]
3J57electron microscopy17.00E10-159[»]
3J59electron microscopy12.00E10-159[»]
3J5Belectron microscopy17.00E10-159[»]
3J5Delectron microscopy17.00E10-159[»]
3J5Felectron microscopy20.00E10-159[»]
3J5Helectron microscopy15.00E10-159[»]
3J5Jelectron microscopy9.00E10-159[»]
3J5Nelectron microscopy6.80E1-167[»]
3J5Telectron microscopy7.60E2-167[»]
3J5Xelectron microscopy7.60E2-167[»]
3KC4electron microscopy-E1-167[»]
3OAQX-ray3.25E10-159[»]
3OARX-ray3.25E10-159[»]
3OFAX-ray3.19E10-159[»]
3OFBX-ray3.19E10-159[»]
3OFOX-ray3.10E10-159[»]
3OFPX-ray3.10E10-159[»]
3OFXX-ray3.29E10-159[»]
3OFYX-ray3.29E10-159[»]
3OR9X-ray3.30E1-167[»]
3ORAX-ray3.30E1-167[»]
3SFSX-ray3.20E1-167[»]
3UOQX-ray3.70E1-167[»]
4A2Ielectron microscopy16.50E10-159[»]
4ADVelectron microscopy13.50E2-167[»]
4GAQX-ray3.30E1-167[»]
4GASX-ray3.30E1-167[»]
4GD1X-ray3.00E10-159[»]
4GD2X-ray3.00E10-159[»]
4KIYX-ray2.90E1-167[»]
4KJ0X-ray2.90E1-167[»]
4KJ2X-ray2.90E1-167[»]
4KJ4X-ray2.90E1-167[»]
4KJ6X-ray2.90E1-167[»]
4KJ8X-ray2.90E1-167[»]
4KJAX-ray2.90E1-167[»]
4KJCX-ray2.90E1-167[»]
ProteinModelPortalP0A7W1.
SMRP0A7W1. Positions 10-159.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10781N.
IntActP0A7W1. 190 interactions.
MINTMINT-6478202.
STRING511145.b3303.

Chemistry

ChEMBLCHEMBL2363135.

Proteomic databases

PaxDbP0A7W1.
PRIDEP0A7W1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76328; AAC76328; b3303.
BAE77988; BAE77988; BAE77988.
GeneID12934414.
947795.
KEGGecj:Y75_p3873.
eco:b3303.
PATRIC32122038. VBIEscCol129921_3396.

Organism-specific databases

EchoBASEEB0897.
EcoGeneEG10904. rpsE.

Phylogenomic databases

eggNOGCOG0098.
HOGENOMHOG000072595.
KOK02988.
OMAPAHEGTG.
OrthoDBEOG6FJNM5.
PhylomeDBP0A7W1.

Enzyme and pathway databases

BioCycEcoCyc:EG10904-MONOMER.
ECOL316407:JW3265-MONOMER.

Gene expression databases

GenevestigatorP0A7W1.

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

EvolutionaryTraceP0A7W1.
PROP0A7W1.

Entry information

Entry nameRS5_ECOLI
AccessionPrimary (citable) accession number: P0A7W1
Secondary accession number(s): O54299, P02356, Q2M6W8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 106 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

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene