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Protein

30S ribosomal protein S11

Gene

rpsK

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

  • small ribosomal subunit rRNA binding Source: EcoliWiki
  • structural constituent of ribosome Source: EcoliWiki

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10910-MONOMER.
ECOL316407:JW3259-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S11
Gene namesi
Name:rpsK
Ordered Locus Names:b3297, JW3259
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10910. rpsK.

Subcellular locationi

GO - Cellular componenti

  • cytosolic small ribosomal subunit Source: EcoliWiki
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 12912830S ribosomal protein S11PRO_0000123144Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-methylalanine1 Publication

Keywords - PTMi

Methylation

Proteomic databases

PaxDbiP0A7R9.
PRIDEiP0A7R9.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi852104. 1 interaction.
DIPiDIP-47838N.
IntActiP0A7R9. 14 interactions.
MINTiMINT-1232137.
STRINGi511145.b3297.

Structurei

Secondary structure

1
129
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi17 – 2610Combined sources
Beta strandi29 – 3810Combined sources
Beta strandi43 – 464Combined sources
Helixi47 – 504Combined sources
Helixi55 – 573Combined sources
Helixi60 – 7415Combined sources
Helixi75 – 773Combined sources
Beta strandi81 – 9010Combined sources
Turni91 – 944Combined sources
Helixi95 – 10410Combined sources
Beta strandi106 – 1127Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-K13-129[»]
2YKRelectron microscopy9.80K13-129[»]
3J9Yelectron microscopy3.90k1-129[»]
4A2Ielectron microscopy16.50K13-129[»]
4ADVelectron microscopy13.50K2-129[»]
4U1UX-ray2.95AK/CK13-129[»]
4U1VX-ray3.00AK/CK13-129[»]
4U20X-ray2.90AK/CK13-129[»]
4U24X-ray2.90AK/CK13-129[»]
4U25X-ray2.90AK/CK13-129[»]
4U26X-ray2.80AK/CK13-129[»]
4U27X-ray2.80AK/CK13-129[»]
4V47electron microscopy12.30BK2-129[»]
4V48electron microscopy11.50BK2-129[»]
4V4HX-ray3.46AK/CK1-129[»]
4V4QX-ray3.46AK/CK2-129[»]
4V4Velectron microscopy15.00AK13-128[»]
4V4Welectron microscopy15.00AK13-128[»]
4V50X-ray3.22AK/CK2-129[»]
4V52X-ray3.21AK/CK2-129[»]
4V53X-ray3.54AK/CK2-129[»]
4V54X-ray3.30AK/CK2-129[»]
4V55X-ray4.00AK/CK2-129[»]
4V56X-ray3.93AK/CK2-129[»]
4V57X-ray3.50AK/CK2-129[»]
4V5BX-ray3.74BK/DK2-129[»]
4V5Helectron microscopy5.80AK13-129[»]
4V5YX-ray4.45AK/CK2-129[»]
4V64X-ray3.50AK/CK2-129[»]
4V65electron microscopy9.00AC1-129[»]
4V66electron microscopy9.00AC1-129[»]
4V69electron microscopy6.70AK13-129[»]
4V6CX-ray3.19AK/CK1-129[»]
4V6DX-ray3.81AK/CK1-129[»]
4V6EX-ray3.71AK/CK1-129[»]
4V6Kelectron microscopy8.25BO1-129[»]
4V6Lelectron microscopy13.20AO1-129[»]
4V6Melectron microscopy7.10AK2-129[»]
4V6Nelectron microscopy12.10BN2-129[»]
4V6Oelectron microscopy14.70AN2-129[»]
4V6Pelectron microscopy13.50AN2-129[»]
4V6Qelectron microscopy11.50AN2-129[»]
4V6Relectron microscopy11.50AN2-129[»]
4V6Selectron microscopy13.10BM2-129[»]
4V6Telectron microscopy8.30AK13-129[»]
4V6Velectron microscopy9.80AK2-129[»]
4V6Yelectron microscopy12.00AK13-129[»]
4V6Zelectron microscopy12.00AK13-129[»]
4V70electron microscopy17.00AK13-129[»]
4V71electron microscopy20.00AK13-129[»]
4V72electron microscopy13.00AK13-129[»]
4V73electron microscopy15.00AK13-129[»]
4V74electron microscopy17.00AK13-129[»]
4V75electron microscopy12.00AK13-129[»]
4V76electron microscopy17.00AK13-129[»]
4V77electron microscopy17.00AK13-129[»]
4V78electron microscopy20.00AK13-129[»]
4V79electron microscopy15.00AK13-129[»]
4V7Aelectron microscopy9.00AK13-129[»]
4V7Belectron microscopy6.80AK1-129[»]
4V7Celectron microscopy7.60AK2-129[»]
4V7Delectron microscopy7.60BK2-129[»]
4V7Ielectron microscopy9.60BK1-129[»]
4V7SX-ray3.25AK/CK13-129[»]
4V7TX-ray3.19AK/CK13-129[»]
4V7UX-ray3.10AK/CK13-129[»]
4V7VX-ray3.29AK/CK13-129[»]
4V85X-ray3.20AK1-129[»]
4V89X-ray3.70AK1-129[»]
4V9CX-ray3.30AK/CK1-129[»]
4V9DX-ray3.00AK/BK13-129[»]
4V9OX-ray2.90BK/DK/FK/HK1-129[»]
4V9PX-ray2.90BK/DK/FK/HK1-129[»]
4WF1X-ray3.09AK/CK13-129[»]
4WWWX-ray3.10QK/XK13-129[»]
4YBBX-ray2.10AK/BK13-129[»]
5AFIelectron microscopy2.90k1-129[»]
ProteinModelPortaliP0A7R9.
SMRiP0A7R9. Positions 13-129.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7R9.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S11P family.Curated

Phylogenomic databases

eggNOGiCOG0100.
HOGENOMiHOG000111598.
InParanoidiP0A7R9.
KOiK02948.
OMAiNTPYASQ.
OrthoDBiEOG6ZSPF3.
PhylomeDBiP0A7R9.

Family and domain databases

Gene3Di3.30.420.80. 1 hit.
HAMAPiMF_01310. Ribosomal_S11.
InterProiIPR001971. Ribosomal_S11.
IPR019981. Ribosomal_S11_bac-type.
IPR018102. Ribosomal_S11_CS.
[Graphical view]
PANTHERiPTHR11759. PTHR11759. 1 hit.
PfamiPF00411. Ribosomal_S11. 1 hit.
[Graphical view]
PIRSFiPIRSF002131. Ribosomal_S11. 1 hit.
TIGRFAMsiTIGR03632. uS11_bact. 1 hit.
PROSITEiPS00054. RIBOSOMAL_S11. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0A7R9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKAPIRARK RVRKQVSDGV AHIHASFNNT IVTITDRQGN ALGWATAGGS
60 70 80 90 100
GFRGSRKSTP FAAQVAAERC ADAVKEYGIK NLEVMVKGPG PGRESTIRAL
110 120
NAAGFRITNI TDVTPIPHNG CRPPKKRRV
Length:129
Mass (Da):13,845
Last modified:January 23, 2007 - v2
Checksum:i0C759DDA60E89C0C
GO

Mass spectrometryi

Molecular mass is 13727.7 Da from positions 2 - 129. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02543 Genomic DNA. Translation: CAA26393.1.
U18997 Genomic DNA. Translation: AAA58095.1.
U00096 Genomic DNA. Translation: AAC76322.1.
AP009048 Genomic DNA. Translation: BAE77994.1.
PIRiB23807. R3EC11.
RefSeqiNP_417756.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC76322; AAC76322; b3297.
BAE77994; BAE77994; BAE77994.
GeneIDi947792.
KEGGiecj:Y75_p3879.
eco:b3297.
PATRICi32122026. VBIEscCol129921_3390.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02543 Genomic DNA. Translation: CAA26393.1.
U18997 Genomic DNA. Translation: AAA58095.1.
U00096 Genomic DNA. Translation: AAC76322.1.
AP009048 Genomic DNA. Translation: BAE77994.1.
PIRiB23807. R3EC11.
RefSeqiNP_417756.1. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-K13-129[»]
2YKRelectron microscopy9.80K13-129[»]
3J9Yelectron microscopy3.90k1-129[»]
4A2Ielectron microscopy16.50K13-129[»]
4ADVelectron microscopy13.50K2-129[»]
4U1UX-ray2.95AK/CK13-129[»]
4U1VX-ray3.00AK/CK13-129[»]
4U20X-ray2.90AK/CK13-129[»]
4U24X-ray2.90AK/CK13-129[»]
4U25X-ray2.90AK/CK13-129[»]
4U26X-ray2.80AK/CK13-129[»]
4U27X-ray2.80AK/CK13-129[»]
4V47electron microscopy12.30BK2-129[»]
4V48electron microscopy11.50BK2-129[»]
4V4HX-ray3.46AK/CK1-129[»]
4V4QX-ray3.46AK/CK2-129[»]
4V4Velectron microscopy15.00AK13-128[»]
4V4Welectron microscopy15.00AK13-128[»]
4V50X-ray3.22AK/CK2-129[»]
4V52X-ray3.21AK/CK2-129[»]
4V53X-ray3.54AK/CK2-129[»]
4V54X-ray3.30AK/CK2-129[»]
4V55X-ray4.00AK/CK2-129[»]
4V56X-ray3.93AK/CK2-129[»]
4V57X-ray3.50AK/CK2-129[»]
4V5BX-ray3.74BK/DK2-129[»]
4V5Helectron microscopy5.80AK13-129[»]
4V5YX-ray4.45AK/CK2-129[»]
4V64X-ray3.50AK/CK2-129[»]
4V65electron microscopy9.00AC1-129[»]
4V66electron microscopy9.00AC1-129[»]
4V69electron microscopy6.70AK13-129[»]
4V6CX-ray3.19AK/CK1-129[»]
4V6DX-ray3.81AK/CK1-129[»]
4V6EX-ray3.71AK/CK1-129[»]
4V6Kelectron microscopy8.25BO1-129[»]
4V6Lelectron microscopy13.20AO1-129[»]
4V6Melectron microscopy7.10AK2-129[»]
4V6Nelectron microscopy12.10BN2-129[»]
4V6Oelectron microscopy14.70AN2-129[»]
4V6Pelectron microscopy13.50AN2-129[»]
4V6Qelectron microscopy11.50AN2-129[»]
4V6Relectron microscopy11.50AN2-129[»]
4V6Selectron microscopy13.10BM2-129[»]
4V6Telectron microscopy8.30AK13-129[»]
4V6Velectron microscopy9.80AK2-129[»]
4V6Yelectron microscopy12.00AK13-129[»]
4V6Zelectron microscopy12.00AK13-129[»]
4V70electron microscopy17.00AK13-129[»]
4V71electron microscopy20.00AK13-129[»]
4V72electron microscopy13.00AK13-129[»]
4V73electron microscopy15.00AK13-129[»]
4V74electron microscopy17.00AK13-129[»]
4V75electron microscopy12.00AK13-129[»]
4V76electron microscopy17.00AK13-129[»]
4V77electron microscopy17.00AK13-129[»]
4V78electron microscopy20.00AK13-129[»]
4V79electron microscopy15.00AK13-129[»]
4V7Aelectron microscopy9.00AK13-129[»]
4V7Belectron microscopy6.80AK1-129[»]
4V7Celectron microscopy7.60AK2-129[»]
4V7Delectron microscopy7.60BK2-129[»]
4V7Ielectron microscopy9.60BK1-129[»]
4V7SX-ray3.25AK/CK13-129[»]
4V7TX-ray3.19AK/CK13-129[»]
4V7UX-ray3.10AK/CK13-129[»]
4V7VX-ray3.29AK/CK13-129[»]
4V85X-ray3.20AK1-129[»]
4V89X-ray3.70AK1-129[»]
4V9CX-ray3.30AK/CK1-129[»]
4V9DX-ray3.00AK/BK13-129[»]
4V9OX-ray2.90BK/DK/FK/HK1-129[»]
4V9PX-ray2.90BK/DK/FK/HK1-129[»]
4WF1X-ray3.09AK/CK13-129[»]
4WWWX-ray3.10QK/XK13-129[»]
4YBBX-ray2.10AK/BK13-129[»]
5AFIelectron microscopy2.90k1-129[»]
ProteinModelPortaliP0A7R9.
SMRiP0A7R9. Positions 13-129.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi852104. 1 interaction.
DIPiDIP-47838N.
IntActiP0A7R9. 14 interactions.
MINTiMINT-1232137.
STRINGi511145.b3297.

Chemistry

ChEMBLiCHEMBL2363135.

Proteomic databases

PaxDbiP0A7R9.
PRIDEiP0A7R9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76322; AAC76322; b3297.
BAE77994; BAE77994; BAE77994.
GeneIDi947792.
KEGGiecj:Y75_p3879.
eco:b3297.
PATRICi32122026. VBIEscCol129921_3390.

Organism-specific databases

EchoBASEiEB0903.
EcoGeneiEG10910. rpsK.

Phylogenomic databases

eggNOGiCOG0100.
HOGENOMiHOG000111598.
InParanoidiP0A7R9.
KOiK02948.
OMAiNTPYASQ.
OrthoDBiEOG6ZSPF3.
PhylomeDBiP0A7R9.

Enzyme and pathway databases

BioCyciEcoCyc:EG10910-MONOMER.
ECOL316407:JW3259-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A7R9.
PROiP0A7R9.

Family and domain databases

Gene3Di3.30.420.80. 1 hit.
HAMAPiMF_01310. Ribosomal_S11.
InterProiIPR001971. Ribosomal_S11.
IPR019981. Ribosomal_S11_bac-type.
IPR018102. Ribosomal_S11_CS.
[Graphical view]
PANTHERiPTHR11759. PTHR11759. 1 hit.
PfamiPF00411. Ribosomal_S11. 1 hit.
[Graphical view]
PIRSFiPIRSF002131. Ribosomal_S11. 1 hit.
TIGRFAMsiTIGR03632. uS11_bact. 1 hit.
PROSITEiPS00054. RIBOSOMAL_S11. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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, METHYLATION AT ALA-2.
    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. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.

Entry informationi

Entry nameiRS11_ECOLI
AccessioniPrimary (citable) accession number: P0A7R9
Secondary accession number(s): P02366, Q2M6W2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Has been predicted to contact the N-terminal domain of IF-3 based on footprint studies; exactly how IF-3 interacts with the 30S subunit is controversial.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Ribosomal proteins
    Ribosomal proteins families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.