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P02359 (RS7_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 165. 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 S7
Gene names
Name:rpsG
Ordered Locus Names:b3341, JW3303
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length179 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.11

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. Ref.11

Subunit structure

Part of the 30S ribosomal subunit. Contacts proteins S9 and S11 By similarity. Cross-links to IF3 and the P and E site tRNAs. Ref.11 Ref.18

Miscellaneous

The strain K12 sequence is shown.

Has been predicted to contact the N-terminal domain of IF-3 based on footprint studies (Ref.18); exactly how IF-3 interacts with the 30S subunit is controversial.

Sequence similarities

Belongs to the ribosomal protein S7P family.

Mass spectrometry

Molecular mass is 19888.7 Da from positions 2 - 179. Determined by MALDI. Ref.17

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 17917830S ribosomal protein S7 HAMAP-Rule MF_00480_B
PRO_0000124259

Natural variations

Natural variant157 – 17923Missing in strain: B and L44.

Experimental info

Mutagenesis2 – 1817Missing: Defective in ribosome assembly; accumulates to abnormally high levels on polysomes; significantly decreases affinity for its own mRNA. Ref.15 Ref.16
Mutagenesis361K → A or E: Defective in ribosome assembly. Ref.15 Ref.16
Mutagenesis1161M → G: Significantly decreases affinity for its own mRNA. Ref.15 Ref.16
Sequence conflict921Missing AA sequence Ref.3

Secondary structure

........................... 179
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02359 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 8627DB380C4A9C0D

FASTA17920,019
        10         20         30         40         50         60 
MPRRRVIGQR KILPDPKFGS ELLAKFVNIL MVDGKKSTAE SIVYSALETL AQRSGKSELE 

        70         80         90        100        110        120 
AFEVALENVR PTVEVKSRRV GGSTYQVPVE VRPVRRNALA MRWIVEAARK RGDKSMALRL 

       130        140        150        160        170 
ANELSDAAEN KGTAVKKRED VHRMAEANKA FAHYRWLSLR SFSHQAGASS KQPALGYLN 

« Hide

References

« Hide 'large scale' references
[1]"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.
[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(2006) [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(1979) [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(1980) [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(1992) [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(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 81-173.
Strain: K12 / MG1655 / ATCC 47076.
[7]Weigel C.T.O.
Submitted (MAY-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(1995) [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(1980) [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(1983) [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(1988) [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(1994) [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(1995) [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(1999) [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(2000) [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(2001) [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(1999) [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(2001) [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(2002) [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(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS).
Strain: MRE-600.
[21]"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
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.
PIRR3EC7K. H65127.
RefSeqNP_417800.1. NC_000913.3.
YP_492091.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EG0electron microscopy11.50D1-146[»]
1M5Gmodel-G3-156[»]
1ML5electron microscopy14.00J1-156[»]
1P6Gelectron microscopy12.30G2-179[»]
1P87electron microscopy11.50G2-179[»]
1VS5X-ray3.46G1-179[»]
1VS7X-ray3.46G1-179[»]
2AVYX-ray3.46G2-179[»]
2AW7X-ray3.46G2-179[»]
2GY9electron microscopy15.00G20-156[»]
2GYBelectron microscopy15.00G20-156[»]
2I2PX-ray3.22G2-179[»]
2I2UX-ray3.22G2-179[»]
2QALX-ray3.21G2-179[»]
2QANX-ray3.21G2-179[»]
2QB9X-ray3.54G2-179[»]
2QBBX-ray3.54G2-179[»]
2QBDX-ray3.30G2-179[»]
2QBFX-ray3.30G2-179[»]
2QBHX-ray4.00G2-179[»]
2QBJX-ray4.00G2-179[»]
2QOUX-ray3.93G2-179[»]
2QOWX-ray3.93G2-179[»]
2QOYX-ray3.50G2-179[»]
2QP0X-ray3.50G2-179[»]
2VHOX-ray3.74G2-179[»]
2VHPX-ray3.74G2-179[»]
2WWLelectron microscopy5.80G3-152[»]
2YKRelectron microscopy9.80G2-152[»]
2Z4KX-ray4.45G2-179[»]
2Z4MX-ray4.45G2-179[»]
3DF1X-ray3.50G2-178[»]
3DF3X-ray3.50G2-178[»]
3E1Aelectron microscopy-U1-179[»]
3E1Celectron microscopy-U1-179[»]
3FIHelectron microscopy6.70G3-152[»]
3I1MX-ray3.19G1-179[»]
3I1OX-ray3.19G1-179[»]
3I1QX-ray3.81G1-179[»]
3I1SX-ray3.81G1-179[»]
3I1ZX-ray3.71G1-179[»]
3I21X-ray3.71G1-179[»]
3IZVelectron microscopy-K1-179[»]
3IZWelectron microscopy-K1-179[»]
3J00electron microscopy-G2-179[»]
3J0Uelectron microscopy12.10J2-179[»]
3J0Velectron microscopy14.70J2-179[»]
3J0Xelectron microscopy13.50J2-179[»]
3J0Zelectron microscopy11.50J2-179[»]
3J10electron microscopy11.50J2-179[»]
3J13electron microscopy13.10I2-179[»]
3J18electron microscopy8.30G2-152[»]
3J36electron microscopy9.80G2-179[»]
3J4Velectron microscopy12.00G3-152[»]
3J4Welectron microscopy12.00G3-152[»]
3J4Yelectron microscopy17.00G3-152[»]
3J4Zelectron microscopy20.00G3-152[»]
3J53electron microscopy13.00G3-152[»]
3J55electron microscopy15.00G3-152[»]
3J57electron microscopy17.00G3-152[»]
3J59electron microscopy12.00G3-152[»]
3J5Belectron microscopy17.00G3-152[»]
3J5Delectron microscopy17.00G3-152[»]
3J5Felectron microscopy20.00G3-152[»]
3J5Helectron microscopy15.00G3-152[»]
3J5Jelectron microscopy9.00G3-152[»]
3J5Nelectron microscopy6.80G1-179[»]
3J5Selectron microscopy7.50I2-152[»]
3J5Telectron microscopy7.60G2-179[»]
3J5Xelectron microscopy7.60G2-179[»]
3KC4electron microscopy-G1-179[»]
3OAQX-ray3.25G2-152[»]
3OARX-ray3.25G3-152[»]
3OFAX-ray3.19G2-152[»]
3OFBX-ray3.19G3-152[»]
3OFOX-ray3.10G2-152[»]
3OFPX-ray3.10G3-152[»]
3OFXX-ray3.29G2-152[»]
3OFYX-ray3.29G3-152[»]
3OR9X-ray3.30G1-179[»]
3ORAX-ray3.30G1-179[»]
3SFSX-ray3.20G1-156[»]
3UOQX-ray3.70G1-179[»]
4A2Ielectron microscopy16.50G3-152[»]
4ADVelectron microscopy13.50G2-179[»]
4GAQX-ray3.30G1-179[»]
4GASX-ray3.30G1-179[»]
4GD1X-ray3.00G2-152[»]
4GD2X-ray3.00G2-152[»]
4KIYX-ray2.90G1-179[»]
4KJ0X-ray2.90G1-179[»]
4KJ2X-ray2.90G1-179[»]
4KJ4X-ray2.90G1-179[»]
4KJ6X-ray2.90G1-179[»]
4KJ8X-ray2.90G1-179[»]
4KJAX-ray2.90G1-179[»]
4KJCX-ray2.90G1-179[»]
ProteinModelPortalP02359.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10783N.
IntActP02359. 151 interactions.
MINTMINT-1236482.
STRING511145.b3341.

Chemistry

ChEMBLCHEMBL2363135.

PTM databases

PhosSiteP0810434.

Proteomic databases

PaxDbP02359.
PRIDEP02359.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76366; AAC76366; b3341.
BAE77950; BAE77950; BAE77950.
GeneID12933477.
947846.
KEGGecj:Y75_p3835.
eco:b3341.
PATRIC32122114. VBIEscCol129921_3434.

Organism-specific databases

EchoBASEEB0899.
EcoGeneEG10906. rpsG.

Phylogenomic databases

eggNOGCOG0049.
HOGENOMHOG000039067.
KOK02992.
OMAALGMRWL.
OrthoDBEOG6P5ZKW.
PhylomeDBP02359.

Enzyme and pathway databases

BioCycEcoCyc:EG10906-MONOMER.
ECOL316407:JW3303-MONOMER.

Gene expression databases

GenevestigatorP02359.

Family and domain databases

Gene3D1.10.455.10. 1 hit.
HAMAPMF_00480_B. Ribosomal_S7_B.
InterProIPR000235. Ribosomal_S5/S7.
IPR005717. Ribosomal_S7_bac/org-type.
IPR020606. Ribosomal_S7_CS.
IPR023798. Ribosomal_S7_dom.
[Graphical view]
PANTHERPTHR11205. PTHR11205. 1 hit.
PfamPF00177. Ribosomal_S7. 1 hit.
[Graphical view]
PIRSFPIRSF002122. RPS7p_RPS7a_RPS5e_RPS7o. 1 hit.
SUPFAMSSF47973. SSF47973. 1 hit.
TIGRFAMsTIGR01029. rpsG_bact. 1 hit.
PROSITEPS00052. RIBOSOMAL_S7. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP02359.
PROP02359.

Entry information

Entry nameRS7_ECOLI
AccessionPrimary (citable) accession number: P02359
Secondary accession number(s): Q2M706
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 165 of the entry and version 3 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