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P0A7R9 (RS11_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. 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 S11
Gene names
Name:rpsK
Ordered Locus Names:b3297, JW3259
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length129 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome By similarity. HAMAP-Rule MF_01310

Subunit structure

Part of the 30S ribosomal subunit. Interacts with proteins S7 and S18 By similarity. Cross-links to IF-3. Ref.10

Miscellaneous

Has been predicted to contact the N-terminal domain of IF-3 based on footprint studies (Ref.10); exactly how IF-3 interacts with the 30S subunit is controversial.

Sequence similarities

Belongs to the ribosomal protein S11P family.

Mass spectrometry

Molecular mass is 13727.7 Da from positions 2 - 129. Determined by MALDI. Ref.9

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 12912830S ribosomal protein S11 HAMAP-Rule MF_01310
PRO_0000123144

Amino acid modifications

Modified residue21N-methylalanine HAMAP-Rule MF_01310

Secondary structure

....................... 129
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A7R9 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 0C759DDA60E89C0C

FASTA12913,845
        10         20         30         40         50         60 
MAKAPIRARK RVRKQVSDGV AHIHASFNNT IVTITDRQGN ALGWATAGGS GFRGSRKSTP 

        70         80         90        100        110        120 
FAAQVAAERC ADAVKEYGIK NLEVMVKGPG PGRESTIRAL NAAGFRITNI TDVTPIPHNG 


CRPPKKRRV 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the alpha ribosomal protein operon of Escherichia coli."
Bedwell D.M., Davis G.R., Gosink M., Post L.E., Nomura M., Kestler H., Zengel J.M., Lindahl L.
Nucleic Acids Res. 13:3891-3903(1985) [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]"Primary structure of protein S11 from Escherichia coli ribosomes."
Kamp R., Wittmann-Liebold B.
FEBS Lett. 121:117-122(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-129.
Strain: K.
[5]"Photochemical cross-linking of initiation factor-3 to Escherichia coli 30 S ribosomal subunits."
MacKeen L.A., Kahan L., Wahba A.J., Schwartz I.
J. Biol. Chem. 255:10526-10531(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: CROSS-LINKING TO IF-3.
Strain: B.
[6]"IF-3 crosslinking to Escherichia coli ribosomal 30 S subunits by three different light-dependent procedures: identification of 30 S proteins crosslinked to IF-3 -- utilization of a new two-stage crosslinking reagent, p-nitrobenzylmaleimide."
Cooperman B.S., Expert-Bezancon A., Kahan L., Dondon J., Grunberg-Manago M.
Arch. Biochem. Biophys. 208:554-562(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: CROSS-LINKING TO IF-3.
[7]"Direct cross-links between initiation factors 1, 2, and 3 and ribosomal proteins promoted by 2-iminothiolane."
Boileau G., Butler P., Hershey J.W.B., Traut R.R.
Biochemistry 22:3162-3170(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: CROSS-LINKING TO IF-3.
Strain: MRE-600.
[8]"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.
[9]"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.
[10]"Interaction of translation initiation factor 3 with the 30S ribosomal subunit."
Dallas A., Noller H.F.
Mol. Cell 8:855-864(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: MODELING OF IF-3/30S SUBUNIT INTERACTION.
[11]"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.
[12]"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.
[13]"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
X02543 Genomic DNA. Translation: CAA26393.1.
U18997 Genomic DNA. Translation: AAA58095.1.
U00096 Genomic DNA. Translation: AAC76322.1.
AP009048 Genomic DNA. Translation: BAE77994.1.
PIRR3EC11. B23807.
RefSeqNP_417756.1. NC_000913.3.
YP_492135.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-K13-129[»]
1P6Gelectron microscopy12.30K2-129[»]
1P87electron microscopy11.50K2-129[»]
1VS5X-ray3.46K1-129[»]
1VS7X-ray3.46K1-129[»]
2AVYX-ray3.46K2-129[»]
2AW7X-ray3.46K2-129[»]
2GY9electron microscopy15.00K13-127[»]
2GYBelectron microscopy15.00K13-127[»]
2I2PX-ray3.22K2-128[»]
2I2UX-ray3.22K2-128[»]
2QALX-ray3.21K2-129[»]
2QANX-ray3.21K2-129[»]
2QB9X-ray3.54K2-129[»]
2QBBX-ray3.54K2-129[»]
2QBDX-ray3.30K2-129[»]
2QBFX-ray3.30K2-129[»]
2QBHX-ray4.00K2-129[»]
2QBJX-ray4.00K2-129[»]
2QOUX-ray3.93K2-129[»]
2QOWX-ray3.93K2-129[»]
2QOYX-ray3.50K2-129[»]
2QP0X-ray3.50K2-129[»]
2VHOX-ray3.74K2-129[»]
2VHPX-ray3.74K2-129[»]
2WWLelectron microscopy5.80K13-129[»]
2YKRelectron microscopy9.80K13-129[»]
2Z4KX-ray4.45K2-129[»]
2Z4MX-ray4.45K2-129[»]
3DF1X-ray3.50K2-128[»]
3DF3X-ray3.50K2-128[»]
3E1Aelectron microscopy-C1-129[»]
3E1Celectron microscopy-C1-129[»]
3FIHelectron microscopy6.70K13-129[»]
3I1MX-ray3.19K1-129[»]
3I1OX-ray3.19K1-129[»]
3I1QX-ray3.81K1-129[»]
3I1SX-ray3.81K1-129[»]
3I1ZX-ray3.71K1-129[»]
3I21X-ray3.71K1-129[»]
3IZVelectron microscopy-O1-129[»]
3IZWelectron microscopy-O1-129[»]
3J00electron microscopy-K2-129[»]
3J0Uelectron microscopy12.10N2-129[»]
3J0Velectron microscopy14.70N2-129[»]
3J0Xelectron microscopy13.50N2-129[»]
3J0Zelectron microscopy11.50N2-129[»]
3J10electron microscopy11.50N2-129[»]
3J13electron microscopy13.10M2-129[»]
3J18electron microscopy8.30K13-129[»]
3J36electron microscopy9.80K2-129[»]
3J4Velectron microscopy12.00K13-129[»]
3J4Welectron microscopy12.00K13-129[»]
3J4Yelectron microscopy17.00K13-129[»]
3J4Zelectron microscopy20.00K13-129[»]
3J53electron microscopy13.00K13-129[»]
3J55electron microscopy15.00K13-129[»]
3J57electron microscopy17.00K13-129[»]
3J59electron microscopy12.00K13-129[»]
3J5Belectron microscopy17.00K13-129[»]
3J5Delectron microscopy17.00K13-129[»]
3J5Felectron microscopy20.00K13-129[»]
3J5Helectron microscopy15.00K13-129[»]
3J5Jelectron microscopy9.00K13-129[»]
3J5Nelectron microscopy6.80K1-129[»]
3J5Telectron microscopy7.60K2-129[»]
3J5Xelectron microscopy7.60K2-129[»]
3KC4electron microscopy-K1-129[»]
3OAQX-ray3.25K13-129[»]
3OARX-ray3.25K13-129[»]
3OFAX-ray3.19K13-129[»]
3OFBX-ray3.19K13-129[»]
3OFOX-ray3.10K13-129[»]
3OFPX-ray3.10K13-129[»]
3OFXX-ray3.29K13-129[»]
3OFYX-ray3.29K13-129[»]
3OR9X-ray3.30K1-129[»]
3ORAX-ray3.30K1-129[»]
3SFSX-ray3.20K1-129[»]
3UOQX-ray3.70K1-129[»]
4A2Ielectron microscopy16.50K13-129[»]
4ADVelectron microscopy13.50K2-129[»]
4GAQX-ray3.30K1-129[»]
4GASX-ray3.30K1-129[»]
4GD1X-ray3.00K13-129[»]
4GD2X-ray3.00K13-129[»]
4KIYX-ray2.90K1-129[»]
4KJ0X-ray2.90K1-129[»]
4KJ2X-ray2.90K1-129[»]
4KJ4X-ray2.90K1-129[»]
4KJ6X-ray2.90K1-129[»]
4KJ8X-ray2.90K1-129[»]
4KJAX-ray2.90K1-129[»]
4KJCX-ray2.90K1-129[»]
ProteinModelPortalP0A7R9.
SMRP0A7R9. Positions 2-129.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid852104. 1 interaction.
DIPDIP-47838N.
IntActP0A7R9. 13 interactions.
MINTMINT-1232137.
STRING511145.b3297.

Chemistry

ChEMBLCHEMBL2363135.

Proteomic databases

PaxDbP0A7R9.
PRIDEP0A7R9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76322; AAC76322; b3297.
BAE77994; BAE77994; BAE77994.
GeneID12934439.
947792.
KEGGecj:Y75_p3879.
eco:b3297.
PATRIC32122026. VBIEscCol129921_3390.

Organism-specific databases

EchoBASEEB0903.
EcoGeneEG10910. rpsK.

Phylogenomic databases

eggNOGCOG0100.
HOGENOMHOG000111598.
KOK02948.
OMAVAHIQST.
OrthoDBEOG6ZSPF3.
PhylomeDBP0A7R9.
ProtClustDBPRK05309.

Enzyme and pathway databases

BioCycEcoCyc:EG10910-MONOMER.
ECOL316407:JW3259-MONOMER.

Gene expression databases

GenevestigatorP0A7R9.

Family and domain databases

Gene3D3.30.420.80. 1 hit.
HAMAPMF_01310. Ribosomal_S11.
InterProIPR001971. Ribosomal_S11.
IPR019981. Ribosomal_S11_bac-type.
IPR018102. Ribosomal_S11_CS.
[Graphical view]
PANTHERPTHR11759. PTHR11759. 1 hit.
PfamPF00411. Ribosomal_S11. 1 hit.
[Graphical view]
PIRSFPIRSF002131. Ribosomal_S11. 1 hit.
TIGRFAMsTIGR03632. bact_S11. 1 hit.
PROSITEPS00054. RIBOSOMAL_S11. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A7R9.
PROP0A7R9.

Entry information

Entry nameRS11_ECOLI
AccessionPrimary (citable) accession number: P0A7R9
Secondary accession number(s): P02366, Q2M6W2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 95 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