Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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

  • mRNA binding Source: EcoCyc
  • rRNA binding Source: EcoCyc
  • structural constituent of ribosome Source: GO_Central
  • tRNA binding Source: UniProtKB-HAMAP

GO - Biological processi

  • negative regulation of translation Source: EcoCyc
  • ribosomal small subunit assembly Source: EcoCyc
  • 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
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10906. rpsG.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • cytosolic small ribosomal subunit Source: EcoCyc
  • 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.

Chemistry

ChEMBLiCHEMBL2363135.
DrugBankiDB00759. Tetracycline.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 17917830S ribosomal protein S7PRO_0000124259Add
BLAST

Proteomic databases

EPDiP02359.
PaxDbiP02359.
PRIDEiP02359.

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[»]
3J9Yelectron microscopy3.90g1-179[»]
3J9Zelectron microscopy3.60SG2-179[»]
3JA1electron microscopy3.60SG2-179[»]
3JBUelectron microscopy3.64G1-156[»]
3JBVelectron microscopy3.32G1-156[»]
3JCDelectron microscopy3.70g1-179[»]
3JCEelectron microscopy3.20g1-179[»]
3JCJelectron microscopy3.70m1-179[»]
3JCNelectron microscopy4.60h1-179[»]
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/DG2-179[»]
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[»]
4WOIX-ray3.00AG/DG1-179[»]
4WWWX-ray3.10QG/XG2-152[»]
4YBBX-ray2.10AG/BG2-152[»]
5AFIelectron microscopy2.90g1-179[»]
5IQRelectron microscopy3.00l1-179[»]
ProteinModelPortaliP02359.
SMRiP02359. Positions 2-152.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02359.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S7P family.Curated

Phylogenomic databases

eggNOGiENOG4108UHY. Bacteria.
COG0049. LUCA.
HOGENOMiHOG000039067.
InParanoidiP02359.
KOiK02992.
OMAiEVHRMAD.
PhylomeDBiP02359.

Family and domain databases

Gene3Di1.10.455.10. 1 hit.
HAMAPiMF_00480_B. Ribosomal_S7_B. 1 hit.
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.
WP_001138045.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76366; AAC76366; b3341.
BAE77950; BAE77950; BAE77950.
GeneIDi947846.
KEGGiecj:JW3303.
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.
WP_001138045.1. NZ_LN832404.1.

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[»]
3J9Yelectron microscopy3.90g1-179[»]
3J9Zelectron microscopy3.60SG2-179[»]
3JA1electron microscopy3.60SG2-179[»]
3JBUelectron microscopy3.64G1-156[»]
3JBVelectron microscopy3.32G1-156[»]
3JCDelectron microscopy3.70g1-179[»]
3JCEelectron microscopy3.20g1-179[»]
3JCJelectron microscopy3.70m1-179[»]
3JCNelectron microscopy4.60h1-179[»]
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/DG2-179[»]
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[»]
4WOIX-ray3.00AG/DG1-179[»]
4WWWX-ray3.10QG/XG2-152[»]
4YBBX-ray2.10AG/BG2-152[»]
5AFIelectron microscopy2.90g1-179[»]
5IQRelectron microscopy3.00l1-179[»]
ProteinModelPortaliP02359.
SMRiP02359. Positions 2-152.
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

EPDiP02359.
PaxDbiP02359.
PRIDEiP02359.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76366; AAC76366; b3341.
BAE77950; BAE77950; BAE77950.
GeneIDi947846.
KEGGiecj:JW3303.
eco:b3341.
PATRICi32122114. VBIEscCol129921_3434.

Organism-specific databases

EchoBASEiEB0899.
EcoGeneiEG10906. rpsG.

Phylogenomic databases

eggNOGiENOG4108UHY. Bacteria.
COG0049. LUCA.
HOGENOMiHOG000039067.
InParanoidiP02359.
KOiK02992.
OMAiEVHRMAD.
PhylomeDBiP02359.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP02359.
PROiP02359.

Family and domain databases

Gene3Di1.10.455.10. 1 hit.
HAMAPiMF_00480_B. Ribosomal_S7_B. 1 hit.
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...

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: September 7, 2016
This is version 184 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

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 one 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.