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P0A7V3 (RS3_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 100. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
30S ribosomal protein S3
Gene names
Name:rpsC
Ordered Locus Names:b3314, JW3276
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length233 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation By similarity. Ref.7

Plays a role in mRNA unwinding by the ribosome, possibly by forming part of a processivity clamp. Ref.7

Subunit structure

Part of the 30S ribosomal subunit. Forms a tight complex with proteins S10 and S14 By similarity. With proteins S4 and S5 encircles the mRNA as it enters the ribosome, which may play a role in mRNA helicase processivity. Some nascent polypeptide chains are able to cross-link to this protein in situ.

Sequence similarities

Belongs to the ribosomal protein S3P family.

Contains 1 KH type-2 domain.

Mass spectrometry

Molecular mass is 25851.9 Da from positions 2 - 233. Determined by MALDI. Ref.8

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 23323230S ribosomal protein S3 HAMAP-Rule MF_01309_B
PRO_0000130113

Regions

Domain39 – 10769KH type-2

Experimental info

Mutagenesis131 – 1355RRAMK → AAAMA: Decreases mRNA unwinding ability of the ribosome.

Secondary structure

....................................... 233
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A7V3 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 6D0131A285B7AAB3

FASTA23325,983
        10         20         30         40         50         60 
MGQKVHPNGI RLGIVKPWNS TWFANTKEFA DNLDSDFKVR QYLTKELAKA SVSRIVIERP 

        70         80         90        100        110        120 
AKSIRVTIHT ARPGIVIGKK GEDVEKLRKV VADIAGVPAQ INIAEVRKPE LDAKLVADSI 

       130        140        150        160        170        180 
TSQLERRVMF RRAMKRAVQN AMRLGAKGIK VEVSGRLGGA EIARTEWYRE GRVPLHTLRA 

       190        200        210        220        230 
DIDYNTSEAH TTYGVIGVKV WIFKGEILGG MAAVEQPEKP AAQPKKQQRK GRK 

« Hide

References

« Hide 'large scale' references
[1]"Structure of the Escherichia coli S10 ribosomal protein operon."
Zurawski G., Zurawski S.M.
Nucleic Acids Res. 13:4521-4526(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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 S3 from the small ribosomal subunit of Escherichia coli."
Brauer D., Roming R.
FEBS Lett. 106:352-357(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-233.
Strain: K.
[5]"Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by cross-linking studies."
Urlaub H., Kruft V., Bischof O., Mueller E.-C., Wittmann-Liebold B.
EMBO J. 14:4578-4588(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 39-49 AND 87-108, CROSS-LINKING TO RRNA.
Strain: MRE-600.
[6]"Flexibility of the nascent polypeptide chain within the ribosome --contacts from the peptide N-terminus to a specific region of the 30S subunit."
Choi K.M., Atkins J.F., Gesteland R.F., Brimacombe R.
Eur. J. Biochem. 255:409-413(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: CROSS-LINKING TO NASCENT POLYPEPTIDE CHAINS.
[7]"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.
[8]"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.
[9]"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.
[10]"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.
[11]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X02613 Genomic DNA. Translation: CAA26466.1.
U18997 Genomic DNA. Translation: AAA58111.1.
U00096 Genomic DNA. Translation: AAC76339.1.
AP009048 Genomic DNA. Translation: BAE77977.1.
PIRR3EC3. H23129.
RefSeqNP_417773.1. NC_000913.3.
YP_492118.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-C2-207[»]
1P6Gelectron microscopy12.30C2-233[»]
1P87electron microscopy11.50C2-233[»]
1VS5X-ray3.46C1-233[»]
1VS7X-ray3.46C1-233[»]
2AVYX-ray3.46C2-233[»]
2AW7X-ray3.46C2-233[»]
2GY9electron microscopy15.00C2-206[»]
2GYBelectron microscopy15.00C2-206[»]
2I2PX-ray3.22C2-232[»]
2I2UX-ray3.22C2-232[»]
2QALX-ray3.21C2-233[»]
2QANX-ray3.21C2-233[»]
2QB9X-ray3.54C2-233[»]
2QBBX-ray3.54C2-233[»]
2QBDX-ray3.30C2-233[»]
2QBFX-ray3.30C2-233[»]
2QBHX-ray4.00C2-233[»]
2QBJX-ray4.00C2-233[»]
2QOUX-ray3.93C2-233[»]
2QOWX-ray3.93C2-233[»]
2QOYX-ray3.50C2-233[»]
2QP0X-ray3.50C2-233[»]
2VHOX-ray3.74C2-233[»]
2VHPX-ray3.74C2-233[»]
2WWLelectron microscopy5.80C2-207[»]
2YKRelectron microscopy9.80C2-207[»]
2Z4KX-ray4.45C2-233[»]
2Z4MX-ray4.45C2-233[»]
3DF1X-ray3.50C2-232[»]
3DF3X-ray3.50C2-232[»]
3E1Aelectron microscopy-O1-233[»]
3E1Celectron microscopy-O1-233[»]
3FIHelectron microscopy6.70C2-207[»]
3I1MX-ray3.19C1-233[»]
3I1OX-ray3.19C1-233[»]
3I1QX-ray3.81C1-233[»]
3I1SX-ray3.81C1-233[»]
3I1ZX-ray3.71C1-233[»]
3I21X-ray3.71C1-233[»]
3IZVelectron microscopy-G1-233[»]
3IZWelectron microscopy-G1-233[»]
3J00electron microscopy-C2-233[»]
3J0Uelectron microscopy12.10F2-233[»]
3J0Velectron microscopy14.70F2-233[»]
3J0Xelectron microscopy13.50F2-233[»]
3J0Zelectron microscopy11.50F2-233[»]
3J10electron microscopy11.50F2-233[»]
3J13electron microscopy13.10E2-233[»]
3J18electron microscopy8.30C2-207[»]
3J36electron microscopy9.80C2-233[»]
3J4Velectron microscopy12.00C1-207[»]
3J4Welectron microscopy12.00C1-207[»]
3J4Yelectron microscopy17.00C1-207[»]
3J4Zelectron microscopy20.00C1-207[»]
3J53electron microscopy13.00C1-207[»]
3J55electron microscopy15.00C1-207[»]
3J57electron microscopy17.00C1-207[»]
3J59electron microscopy12.00C1-207[»]
3J5Belectron microscopy17.00C1-207[»]
3J5Delectron microscopy17.00C1-207[»]
3J5Felectron microscopy20.00C1-207[»]
3J5Helectron microscopy15.00C1-207[»]
3J5Jelectron microscopy9.00C1-207[»]
3J5Nelectron microscopy6.80C1-233[»]
3J5Telectron microscopy7.60C2-233[»]
3J5Xelectron microscopy7.60C2-233[»]
3KC4electron microscopy-C1-233[»]
3OAQX-ray3.25C2-207[»]
3OARX-ray3.25C2-207[»]
3OFAX-ray3.19C2-207[»]
3OFBX-ray3.19C2-207[»]
3OFOX-ray3.10C2-207[»]
3OFPX-ray3.10C2-207[»]
3OFXX-ray3.29C2-207[»]
3OFYX-ray3.29C2-207[»]
3OR9X-ray3.30C1-233[»]
3ORAX-ray3.30C1-233[»]
3SFSX-ray3.20C1-233[»]
3UOQX-ray3.70C1-233[»]
4A2Ielectron microscopy16.50C2-207[»]
4ADVelectron microscopy13.50C2-233[»]
4GAQX-ray3.30C1-233[»]
4GASX-ray3.30C1-233[»]
4GD1X-ray3.00C2-207[»]
4GD2X-ray3.00C2-207[»]
4KIYX-ray2.90C1-233[»]
4KJ0X-ray2.90C1-233[»]
4KJ2X-ray2.90C1-233[»]
4KJ4X-ray2.90C1-233[»]
4KJ6X-ray2.90C1-233[»]
4KJ8X-ray2.90C1-233[»]
4KJAX-ray2.90C1-233[»]
4KJCX-ray2.90C1-233[»]
ProteinModelPortalP0A7V3.
SMRP0A7V3. Positions 2-233.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid852126. 1 interaction.
DIPDIP-35807N.
IntActP0A7V3. 188 interactions.
MINTMINT-6478122.
STRING511145.b3314.

Chemistry

ChEMBLCHEMBL2363135.

Proteomic databases

PaxDbP0A7V3.
PRIDEP0A7V3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76339; AAC76339; b3314.
BAE77977; BAE77977; BAE77977.
GeneID12932292.
947814.
KEGGecj:Y75_p3862.
eco:b3314.
PATRIC32122060. VBIEscCol129921_3407.

Organism-specific databases

EchoBASEEB0895.
EcoGeneEG10902. rpsC.

Phylogenomic databases

eggNOGCOG0092.
HOGENOMHOG000210610.
KOK02982.
OMAMGQKTNP.
OrthoDBEOG6K13X3.
PhylomeDBP0A7V3.
ProtClustDBPRK00310.

Enzyme and pathway databases

BioCycEcoCyc:EG10902-MONOMER.
ECOL316407:JW3276-MONOMER.

Gene expression databases

GenevestigatorP0A7V3.

Family and domain databases

Gene3D3.30.1140.32. 1 hit.
3.30.300.20. 1 hit.
HAMAPMF_01309_B. Ribosomal_S3_B.
InterProIPR004087. KH_dom.
IPR015946. KH_dom-like_a/b.
IPR004044. KH_dom_type_2.
IPR009019. KH_prok-type.
IPR005704. Ribosomal_S3_bac.
IPR001351. Ribosomal_S3_C.
IPR018280. Ribosomal_S3_CS.
[Graphical view]
PfamPF07650. KH_2. 1 hit.
PF00189. Ribosomal_S3_C. 1 hit.
[Graphical view]
SMARTSM00322. KH. 1 hit.
[Graphical view]
SUPFAMSSF54814. SSF54814. 1 hit.
SSF54821. SSF54821. 1 hit.
TIGRFAMsTIGR01009. rpsC_bact. 1 hit.
PROSITEPS50823. KH_TYPE_2. 1 hit.
PS00548. RIBOSOMAL_S3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A7V3.
PROP0A7V3.

Entry information

Entry nameRS3_ECOLI
AccessionPrimary (citable) accession number: P0A7V3
Secondary accession number(s): P02352, Q2M6X9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 100 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