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Protein

30S ribosomal protein S7

Gene

rpsG

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

Functioni

One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, where it has been shown to contact mRNA. Has been shown to contact tRNA in both the P and E sites; it probably blocks exit of the E site tRNA.1 Publication
Protein S7 is also a translational repressor protein; it regulates the expression of the str operon members to different degrees by binding to its mRNA.1 Publication

GO - Molecular functioni

  1. mRNA binding Source: EcoCyc
  2. rRNA binding Source: EcoCyc
  3. structural constituent of ribosome Source: InterPro
  4. tRNA binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. negative regulation of translation Source: EcoCyc
  2. ribosomal small subunit assembly Source: EcoCyc
  3. translation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding, tRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10906-MONOMER.
ECOL316407:JW3303-MONOMER.

Protein family/group databases

MoonProtiP02359.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S7
Gene namesi
Name:rpsG
Ordered Locus Names:b3341, JW3303
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10906. rpsG.

Subcellular locationi

GO - Cellular componenti

  1. cytosolic small ribosomal subunit Source: EcoCyc
  2. membrane Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2 – 1817Missing : Defective in ribosome assembly; accumulates to abnormally high levels on polysomes; significantly decreases affinity for its own mRNA. Add
BLAST
Mutagenesisi36 – 361K → A or E: Defective in ribosome assembly.
Mutagenesisi116 – 1161M → G: Significantly decreases affinity for its own mRNA.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 17917830S ribosomal protein S7PRO_0000124259Add
BLAST

Proteomic databases

PaxDbiP02359.
PRIDEiP02359.

Expressioni

Gene expression databases

GenevestigatoriP02359.

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit. Contacts proteins S9 and S11 (By similarity). Cross-links to IF3 and the P and E site tRNAs.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
infCP0A7073EBI-543074,EBI-546262
rluBP377653EBI-543074,EBI-561550
tigP0A8503EBI-543074,EBI-544862

Protein-protein interaction databases

DIPiDIP-10783N.
IntActiP02359. 151 interactions.
MINTiMINT-1236482.
STRINGi511145.b3341.

Structurei

Secondary structure

1
179
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni16 – 183Combined sources
Helixi21 – 3010Combined sources
Helixi32 – 343Combined sources
Helixi36 – 5419Combined sources
Helixi59 – 6911Combined sources
Beta strandi72 – 765Combined sources
Beta strandi78 – 803Combined sources
Beta strandi81 – 833Combined sources
Beta strandi87 – 904Combined sources
Helixi93 – 10917Combined sources
Beta strandi113 – 1153Combined sources
Helixi116 – 12813Combined sources
Helixi133 – 14412Combined sources
Turni145 – 1473Combined sources
Helixi148 – 1514Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EG0electron microscopy11.50D1-146[»]
1M5Gmodel-G3-156[»]
1ML5electron microscopy14.00J1-156[»]
2YKRelectron microscopy9.80G2-152[»]
3J5Selectron microscopy7.50I2-152[»]
4A2Ielectron microscopy16.50G3-152[»]
4ADVelectron microscopy13.50G2-179[»]
4U1UX-ray2.95AG/CG2-152[»]
4U1VX-ray3.00AG/CG2-152[»]
4U20X-ray2.90AG/CG2-152[»]
4U24X-ray2.90AG/CG2-152[»]
4U25X-ray2.90AG/CG2-152[»]
4U26X-ray2.80AG/CG2-152[»]
4U27X-ray2.80AG/CG2-152[»]
4V47electron microscopy12.30BG2-179[»]
4V48electron microscopy11.50BG2-179[»]
4V4HX-ray3.46AG/CG1-179[»]
4V4QX-ray3.46AG/CG2-179[»]
4V4Velectron microscopy15.00AG20-156[»]
4V4Welectron microscopy15.00AG20-156[»]
4V50X-ray3.22AG/CG2-179[»]
4V52X-ray3.21AG/CG2-179[»]
4V53X-ray3.54AG/CG2-179[»]
4V54X-ray3.30AG/CG2-179[»]
4V55X-ray4.00AG/CG2-179[»]
4V56X-ray3.93AG/CG2-179[»]
4V57X-ray3.50AG/CG2-179[»]
4V5BX-ray3.74BG/DG2-156[»]
4V5Helectron microscopy5.80AG3-152[»]
4V5YX-ray4.45AG/CG2-179[»]
4V64X-ray3.50AG/CG2-179[»]
4V65electron microscopy9.00AU1-179[»]
4V66electron microscopy9.00AU1-179[»]
4V69electron microscopy6.70AG3-152[»]
4V6CX-ray3.19AG/CG1-179[»]
4V6DX-ray3.81AG/CG1-179[»]
4V6EX-ray3.71AG/CG1-179[»]
4V6Kelectron microscopy8.25BK1-179[»]
4V6Lelectron microscopy13.20AK1-179[»]
4V6Melectron microscopy7.10AG2-179[»]
4V6Nelectron microscopy12.10BJ2-179[»]
4V6Oelectron microscopy14.70AJ2-179[»]
4V6Pelectron microscopy13.50AJ2-179[»]
4V6Qelectron microscopy11.50AJ2-179[»]
4V6Relectron microscopy11.50AJ2-179[»]
4V6Selectron microscopy13.10BI2-179[»]
4V6Telectron microscopy8.30AG2-152[»]
4V6Velectron microscopy9.80AG2-179[»]
4V6Yelectron microscopy12.00AG3-152[»]
4V6Zelectron microscopy12.00AG3-152[»]
4V70electron microscopy17.00AG3-152[»]
4V71electron microscopy20.00AG3-152[»]
4V72electron microscopy13.00AG3-152[»]
4V73electron microscopy15.00AG3-152[»]
4V74electron microscopy17.00AG3-152[»]
4V75electron microscopy12.00AG3-152[»]
4V76electron microscopy17.00AG3-152[»]
4V77electron microscopy17.00AG3-152[»]
4V78electron microscopy20.00AG3-152[»]
4V79electron microscopy15.00AG3-152[»]
4V7Aelectron microscopy9.00AG3-152[»]
4V7Belectron microscopy6.80AG1-179[»]
4V7Celectron microscopy7.60AG2-179[»]
4V7Delectron microscopy7.60BG2-179[»]
4V7Ielectron microscopy9.60BG1-179[»]
4V7SX-ray3.25AG2-152[»]
CG3-152[»]
4V7TX-ray3.19AG2-152[»]
CG3-152[»]
4V7UX-ray3.10AG/CG2-152[»]
4V7VX-ray3.29AG2-152[»]
CG3-152[»]
4V85X-ray3.20G1-156[»]
4V89X-ray3.70AG1-179[»]
4V9CX-ray3.30AG/CG1-179[»]
4V9DX-ray3.00AG/BG2-152[»]
4V9OX-ray2.90BG/DG/FG/HG1-179[»]
4V9PX-ray2.90BG/DG/FG/HG1-179[»]
4WF1X-ray3.09AG/CG2-152[»]
4WWWX-ray3.10QG/XG2-152[»]
ProteinModelPortaliP02359.
SMRiP02359. Positions 2-179.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02359.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S7P family.Curated

Phylogenomic databases

eggNOGiCOG0049.
HOGENOMiHOG000039067.
InParanoidiP02359.
KOiK02992.
OMAiEVHRMAD.
OrthoDBiEOG6P5ZKW.
PhylomeDBiP02359.

Family and domain databases

Gene3Di1.10.455.10. 1 hit.
HAMAPiMF_00480_B. Ribosomal_S7_B.
InterProiIPR000235. Ribosomal_S5/S7.
IPR005717. Ribosomal_S7_bac/org-type.
IPR020606. Ribosomal_S7_CS.
IPR023798. Ribosomal_S7_dom.
[Graphical view]
PANTHERiPTHR11205. PTHR11205. 1 hit.
PfamiPF00177. Ribosomal_S7. 1 hit.
[Graphical view]
PIRSFiPIRSF002122. RPS7p_RPS7a_RPS5e_RPS7o. 1 hit.
SUPFAMiSSF47973. SSF47973. 1 hit.
TIGRFAMsiTIGR01029. rpsG_bact. 1 hit.
PROSITEiPS00052. RIBOSOMAL_S7. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P02359-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPRRRVIGQR KILPDPKFGS ELLAKFVNIL MVDGKKSTAE SIVYSALETL
60 70 80 90 100
AQRSGKSELE AFEVALENVR PTVEVKSRRV GGSTYQVPVE VRPVRRNALA
110 120 130 140 150
MRWIVEAARK RGDKSMALRL ANELSDAAEN KGTAVKKRED VHRMAEANKA
160 170
FAHYRWLSLR SFSHQAGASS KQPALGYLN
Length:179
Mass (Da):20,019
Last modified:January 23, 2007 - v3
Checksum:i8627DB380C4A9C0D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti92 – 921Missing AA sequence (PubMed:385062).Curated

Mass spectrometryi

Molecular mass is 19888.7 Da from positions 2 - 179. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti157 – 17923Missing in strain: B and L44.
Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18997 Genomic DNA. Translation: AAA58138.1.
U00096 Genomic DNA. Translation: AAC76366.1.
AP009048 Genomic DNA. Translation: BAE77950.1.
V00355 Genomic DNA. Translation: CAA23649.1.
J01689 Genomic DNA. Translation: AAA50990.1.
X64592 Genomic DNA. Translation: CAA45881.1.
X65735 Genomic DNA. Translation: CAA46644.1.
J01688 Genomic DNA. Translation: AAA50989.1.
PIRiH65127. R3EC7K.
RefSeqiNP_417800.1. NC_000913.3.
YP_492091.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76366; AAC76366; b3341.
BAE77950; BAE77950; BAE77950.
GeneIDi12933477.
947846.
KEGGiecj:Y75_p3835.
eco:b3341.
PATRICi32122114. VBIEscCol129921_3434.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18997 Genomic DNA. Translation: AAA58138.1.
U00096 Genomic DNA. Translation: AAC76366.1.
AP009048 Genomic DNA. Translation: BAE77950.1.
V00355 Genomic DNA. Translation: CAA23649.1.
J01689 Genomic DNA. Translation: AAA50990.1.
X64592 Genomic DNA. Translation: CAA45881.1.
X65735 Genomic DNA. Translation: CAA46644.1.
J01688 Genomic DNA. Translation: AAA50989.1.
PIRiH65127. R3EC7K.
RefSeqiNP_417800.1. NC_000913.3.
YP_492091.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EG0electron microscopy11.50D1-146[»]
1M5Gmodel-G3-156[»]
1ML5electron microscopy14.00J1-156[»]
2YKRelectron microscopy9.80G2-152[»]
3J5Selectron microscopy7.50I2-152[»]
4A2Ielectron microscopy16.50G3-152[»]
4ADVelectron microscopy13.50G2-179[»]
4U1UX-ray2.95AG/CG2-152[»]
4U1VX-ray3.00AG/CG2-152[»]
4U20X-ray2.90AG/CG2-152[»]
4U24X-ray2.90AG/CG2-152[»]
4U25X-ray2.90AG/CG2-152[»]
4U26X-ray2.80AG/CG2-152[»]
4U27X-ray2.80AG/CG2-152[»]
4V47electron microscopy12.30BG2-179[»]
4V48electron microscopy11.50BG2-179[»]
4V4HX-ray3.46AG/CG1-179[»]
4V4QX-ray3.46AG/CG2-179[»]
4V4Velectron microscopy15.00AG20-156[»]
4V4Welectron microscopy15.00AG20-156[»]
4V50X-ray3.22AG/CG2-179[»]
4V52X-ray3.21AG/CG2-179[»]
4V53X-ray3.54AG/CG2-179[»]
4V54X-ray3.30AG/CG2-179[»]
4V55X-ray4.00AG/CG2-179[»]
4V56X-ray3.93AG/CG2-179[»]
4V57X-ray3.50AG/CG2-179[»]
4V5BX-ray3.74BG/DG2-156[»]
4V5Helectron microscopy5.80AG3-152[»]
4V5YX-ray4.45AG/CG2-179[»]
4V64X-ray3.50AG/CG2-179[»]
4V65electron microscopy9.00AU1-179[»]
4V66electron microscopy9.00AU1-179[»]
4V69electron microscopy6.70AG3-152[»]
4V6CX-ray3.19AG/CG1-179[»]
4V6DX-ray3.81AG/CG1-179[»]
4V6EX-ray3.71AG/CG1-179[»]
4V6Kelectron microscopy8.25BK1-179[»]
4V6Lelectron microscopy13.20AK1-179[»]
4V6Melectron microscopy7.10AG2-179[»]
4V6Nelectron microscopy12.10BJ2-179[»]
4V6Oelectron microscopy14.70AJ2-179[»]
4V6Pelectron microscopy13.50AJ2-179[»]
4V6Qelectron microscopy11.50AJ2-179[»]
4V6Relectron microscopy11.50AJ2-179[»]
4V6Selectron microscopy13.10BI2-179[»]
4V6Telectron microscopy8.30AG2-152[»]
4V6Velectron microscopy9.80AG2-179[»]
4V6Yelectron microscopy12.00AG3-152[»]
4V6Zelectron microscopy12.00AG3-152[»]
4V70electron microscopy17.00AG3-152[»]
4V71electron microscopy20.00AG3-152[»]
4V72electron microscopy13.00AG3-152[»]
4V73electron microscopy15.00AG3-152[»]
4V74electron microscopy17.00AG3-152[»]
4V75electron microscopy12.00AG3-152[»]
4V76electron microscopy17.00AG3-152[»]
4V77electron microscopy17.00AG3-152[»]
4V78electron microscopy20.00AG3-152[»]
4V79electron microscopy15.00AG3-152[»]
4V7Aelectron microscopy9.00AG3-152[»]
4V7Belectron microscopy6.80AG1-179[»]
4V7Celectron microscopy7.60AG2-179[»]
4V7Delectron microscopy7.60BG2-179[»]
4V7Ielectron microscopy9.60BG1-179[»]
4V7SX-ray3.25AG2-152[»]
CG3-152[»]
4V7TX-ray3.19AG2-152[»]
CG3-152[»]
4V7UX-ray3.10AG/CG2-152[»]
4V7VX-ray3.29AG2-152[»]
CG3-152[»]
4V85X-ray3.20G1-156[»]
4V89X-ray3.70AG1-179[»]
4V9CX-ray3.30AG/CG1-179[»]
4V9DX-ray3.00AG/BG2-152[»]
4V9OX-ray2.90BG/DG/FG/HG1-179[»]
4V9PX-ray2.90BG/DG/FG/HG1-179[»]
4WF1X-ray3.09AG/CG2-152[»]
4WWWX-ray3.10QG/XG2-152[»]
ProteinModelPortaliP02359.
SMRiP02359. Positions 2-179.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-10783N.
IntActiP02359. 151 interactions.
MINTiMINT-1236482.
STRINGi511145.b3341.

Chemistry

ChEMBLiCHEMBL2363135.
DrugBankiDB00759. Tetracycline.

Protein family/group databases

MoonProtiP02359.

Proteomic databases

PaxDbiP02359.
PRIDEiP02359.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76366; AAC76366; b3341.
BAE77950; BAE77950; BAE77950.
GeneIDi12933477.
947846.
KEGGiecj:Y75_p3835.
eco:b3341.
PATRICi32122114. VBIEscCol129921_3434.

Organism-specific databases

EchoBASEiEB0899.
EcoGeneiEG10906. rpsG.

Phylogenomic databases

eggNOGiCOG0049.
HOGENOMiHOG000039067.
InParanoidiP02359.
KOiK02992.
OMAiEVHRMAD.
OrthoDBiEOG6P5ZKW.
PhylomeDBiP02359.

Enzyme and pathway databases

BioCyciEcoCyc:EG10906-MONOMER.
ECOL316407:JW3303-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP02359.
PROiP02359.

Gene expression databases

GenevestigatoriP02359.

Family and domain databases

Gene3Di1.10.455.10. 1 hit.
HAMAPiMF_00480_B. Ribosomal_S7_B.
InterProiIPR000235. Ribosomal_S5/S7.
IPR005717. Ribosomal_S7_bac/org-type.
IPR020606. Ribosomal_S7_CS.
IPR023798. Ribosomal_S7_dom.
[Graphical view]
PANTHERiPTHR11205. PTHR11205. 1 hit.
PfamiPF00177. Ribosomal_S7. 1 hit.
[Graphical view]
PIRSFiPIRSF002122. RPS7p_RPS7a_RPS5e_RPS7o. 1 hit.
SUPFAMiSSF47973. SSF47973. 1 hit.
TIGRFAMsiTIGR01029. rpsG_bact. 1 hit.
PROSITEiPS00052. RIBOSOMAL_S7. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  2. "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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. "The primary structure of ribosomal protein S7 from E. coli strains K and B."
    Reinbolt J., Tritsch D., Wittmann-Liebold B.
    Biochimie 61:501-522(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-179.
    Strain: B and K.
  4. "DNA sequences from the str operon of Escherichia coli."
    Post L.E., Nomura M.
    J. Biol. Chem. 255:4660-4666(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-81 AND 148-179.
    Strain: K12.
  5. "Mutant sequences in the rpsL gene of Escherichia coli B/r: mechanistic implications for spontaneous and ultraviolet light mutagenesis."
    Timms A.R., Steingrimsdottir H., Lehmann A.R., Bridges B.A.
    Mol. Gen. Genet. 232:89-96(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-81.
    Strain: B/R.
  6. "Comparison of the complete sequence of the str operon in Salmonella typhimurium and Escherichia coli."
    Johanson U., Hughes D.
    Gene 120:93-98(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 81-173.
    Strain: K12 / MG1655 / ATCC 47076.
  7. Weigel C.T.O.
    Submitted (APR-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 147-156.
    Strain: L44.
  8. "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(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 111-131, CROSS-LINKING TO RRNA.
    Strain: MRE-600.
  9. "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(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: CROSS-LINKING TO IF3.
    Strain: B.
  10. "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(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: CROSS-LINKING TO IF3.
    Strain: MRE-600.
  11. "Assembly of the 30S subunit from Escherichia coli ribosomes occurs via two assembly domains which are initiated by S4 and S7."
    Nowotny V., Nierhaus K.H.
    Biochemistry 27:7051-7055(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: ROLE IN SUBUNIT ASSEMBLY.
    Strain: K12 / D10.
  12. "Post-transcriptional regulation of the str operon in Escherichia coli. Ribosomal protein S7 inhibits coupled translation of S7 but not its independent translation."
    Saito K., Mattheakis L.C., Nomura M.
    J. Mol. Biol. 235:111-124(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: MECHANISM OF TRANSLATION REGULATION.
    Strain: K12.
  13. "The ribosomal neighbourhood of the central fold of tRNA: cross-links from position 47 of tRNA located at the A, P or E site."
    Osswald M., Doering T., Brimacombe R.
    Nucleic Acids Res. 23:4635-4641(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: CROSS-LINKING TO THE TRNA CENTRAL FOLD.
    Strain: MRE-600.
  14. "The cross-link from the upstream region of mRNA to ribosomal protein S7 is located in the C-terminal peptide: experimental verification of a prediction from modeling studies."
    Greuer B., Thiede B., Brimacombe R.
    RNA 5:1521-1525(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CROSS-LINKING TO MRNA.
    Strain: B and K.
  15. "Tagging ribosomal protein S7 allows rapid identification of mutants defective in assembly and function of 30S subunits."
    Fredrick K., Dunny G.M., Noller H.F.
    J. Mol. Biol. 298:379-394(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CONSERVED SURFACE RESIDUES.
    Strain: K.
  16. "Ribosomal protein S7 from Escherichia coli uses the same determinants to bind 16S ribosomal RNA and its messenger RNA."
    Robert F., Brakier-Gingras L.
    Nucleic Acids Res. 29:677-682(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CONSERVED RESIDUES.
    Strain: K12.
  17. "Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry."
    Arnold R.J., Reilly J.P.
    Anal. Biochem. 269:105-112(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY.
    Strain: K12 / ATCC 25404 / DSM 5698 / NCIMB 11290.
  18. "Interaction of translation initiation factor 3 with the 30S ribosomal subunit."
    Dallas A., Noller H.F.
    Mol. Cell 8:855-864(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: MODELING OF IF-3/30S SUBUNIT INTERACTION.
  19. "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(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING.
  20. "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(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS).
    Strain: MRE-600.
  21. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.

Entry informationi

Entry nameiRS7_ECOLI
AccessioniPrimary (citable) accession number: P02359
Secondary accession number(s): Q2M706
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 171 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The strain K12 sequence is shown.
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.