UniProtKB - P02359 (RS7_ECOLI)
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- BLAST>sp|P02359|RS7_ECOLI 30S ribosomal protein S7 OS=Escherichia coli (strain K12) OX=83333 GN=rpsG PE=1 SV=3 MPRRRVIGQRKILPDPKFGSELLAKFVNILMVDGKKSTAESIVYSALETLAQRSGKSELE AFEVALENVRPTVEVKSRRVGGSTYQVPVEVRPVRRNALAMRWIVEAARKRGDKSMALRL ANELSDAAENKGTAVKKREDVHRMAEANKAFAHYRWLSLRSFSHQAGASSKQPALGYLN
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30S ribosomal protein S7
rpsG
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.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. - Ref.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. - Ref.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.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.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.
Miscellaneous
<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
- Ref.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. - Ref.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. - Ref.19"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.
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- mRNA binding Source: CAFA <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- rRNA binding Source: EcoCyc <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- structural constituent of ribosome Source: CAFA <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- tRNA binding Source: UniProtKB-KW
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- negative regulation of translation Source: CAFA <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- ribosomal small subunit assembly Source: CAFA <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- translation Source: InterPro
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Ribonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding, tRNA-binding |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | EcoCyc:EG10906-MONOMER MetaCyc:EG10906-MONOMER |
Protein family/group databases
MoonProt database of moonlighting proteins More...MoonProti | P02359 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: 30S ribosomal protein S7Alternative name(s): Small ribosomal subunit protein uS71 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
|
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:rpsG Ordered Locus Names:b3341, JW3303 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Escherichia coli (strain K12) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 83333 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
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Organism-specific databases
Escherichia coli strain K12 genome database More...EcoGenei | EG10906 rpsG |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti
- cytosol Source: EcoCyc <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- cytosolic small ribosomal subunit Source: CAFA <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- membrane Source: UniProtKBInferred from high throughput direct assayi
<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 2 – 18 | Missing : Defective in ribosome assembly; accumulates to abnormally high levels on polysomes; significantly decreases affinity for its own mRNA. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 17 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 36 | K → A or E: Defective in ribosome assembly. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 116 | M → G: Significantly decreases affinity for its own mRNA. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Chemistry databases
Drug and drug target database More...DrugBanki | DB00759 Tetracycline |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methioninei | Removed1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| |||
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000124259 | 2 – 179 | 30S ribosomal protein S7Add BLAST | 178 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P02359 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P02359 |
PRoteomics IDEntifications database More...PRIDEi | P02359 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
2 Publications<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
- Ref.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. - Ref.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.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.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, SUBUNIT. - Ref.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, SUBUNIT. - Ref.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. - Ref.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, SUBUNIT. - Ref.20"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, SUBUNIT. - Ref.21"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), SUBUNIT. - Ref.22"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, SUBUNIT. - Ref.23"Mechanistic insights into the alternative translation termination by ArfA and RF2."
Ma C., Kurita D., Li N., Chen Y., Himeno H., Gao N.
Nature 541:550-553(2017) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) OF 70S RIBOSOME IN COMPLEX WITH ARFA AND RF2, SUBUNIT. - Ref.24"Structural basis for ArfA-RF2-mediated translation termination on mRNAs lacking stop codons."
Huter P., Mueller C., Beckert B., Arenz S., Berninghausen O., Beckmann R., Wilson D.N.
Nature 541:546-549(2017) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.1 ANGSTROMS) OF 70S RIBOSOME IN COMPLEX WITH ARFA AND RF2, SUBUNIT. - Ref.25"Translational termination without a stop codon."
James N.R., Brown A., Gordiyenko Y., Ramakrishnan V.
Science 354:1437-1440(2016) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (2.97 ANGSTROMS) OF 70S RIBOSOME IN COMPLEX WITH ARFA AND RF2, SUBUNIT. - Ref.26"Structural basis of co-translational quality control by ArfA and RF2 bound to ribosome."
Zeng F., Chen Y., Remis J., Shekhar M., Phillips J.C., Tajkhorshid E., Jin H.
Nature 541:554-557(2017) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.52 ANGSTROMS) OF 70S RIBOSOME IN COMPLEX WITH ARFA AND RF2, SUBUNIT.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| infC | P0A707 | 4 | EBI-543074,EBI-546262 | |
| rluB | P37765 | 4 | EBI-543074,EBI-561550 | |
| tig | P0A850 | 4 | EBI-543074,EBI-544862 |
Protein-protein interaction databases
Database of interacting proteins More...DIPi | DIP-10783N |
Protein interaction database and analysis system More...IntActi | P02359, 154 interactors |
STRING: functional protein association networks More...STRINGi | 316385.ECDH10B_3516 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 16 – 18 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 21 – 30 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 32 – 34 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 36 – 54 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 19 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 59 – 69 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 72 – 76 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 78 – 80 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 81 – 83 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 87 – 90 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 93 – 109 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 17 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 113 – 115 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 116 – 128 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 133 – 144 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 145 – 147 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 148 – 151 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P02359 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P02359 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P02359 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG4108UHY Bacteria COG0049 LUCA |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000039067 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P02359 |
KEGG Orthology (KO) More...KOi | K02992 |
Identification of Orthologs from Complete Genome Data More...OMAi | TERLMNE |
Database for complete collections of gene phylogenies More...PhylomeDBi | P02359 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.10.455.10, 1 hit |
HAMAP database of protein families More...HAMAPi | MF_00480_B Ribosomal_S7_B, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR000235 Ribosomal_S5/S7 IPR005717 Ribosomal_S7_bac/org-type IPR020606 Ribosomal_S7_CS IPR023798 Ribosomal_S7_dom IPR036823 Ribosomal_S7_dom_sf |
The PANTHER Classification System More...PANTHERi | PTHR11205 PTHR11205, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00177 Ribosomal_S7, 1 hit |
PIRSF; a whole-protein classification database More...PIRSFi | PIRSF002122 RPS7p_RPS7a_RPS5e_RPS7o, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF47973 SSF47973, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR01029 rpsG_bact, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00052 RIBOSOMAL_S7, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
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
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 92 | Missing AA sequence (PubMed:385062).Curated | 1 |
<p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.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, SUBUNIT.
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti | 157 – 179 | Missing in strain: B and L44. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 23 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks 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 |
Protein sequence database of the Protein Information Resource More...PIRi | H65127 R3EC7K |
NCBI Reference Sequences More...RefSeqi | NP_417800.1, NC_000913.3 WP_001138045.1, NZ_LN832404.1 |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAC76366; AAC76366; b3341 BAE77950; BAE77950; BAE77950 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 947846 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ecj:JW3303 eco:b3341 |
Pathosystems Resource Integration Center (PATRIC) More...PATRICi | fig|1411691.4.peg.3390 |
<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P02359 | 30S ribosomal protein S7 | 179 | |||
| 30S ribosomal protein S7 | 179 | ||||
| 30S ribosomal protein S7 | 179 | ||||
| 30S ribosomal protein S7 | 156 | ||||
| 30S ribosomal protein S7 | 156 | ||||
| +252 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P02359 | 30S ribosomal protein S7 | 156 | |||
| 30S ribosomal protein S7 | 179 | ||||
| 30S ribosomal protein S7 | 179 | ||||
| 30S ribosomal protein S7 | 179 | ||||
| 30S ribosomal protein S7 | 156 | ||||
| +944 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P02359 | 30S ribosomal protein S7 | 155 | |||
| 30S ribosomal protein S7 | 164 | ||||
| 30S ribosomal protein S7 | 156 | ||||
| 30S ribosomal subunit protein S7 | 156 | ||||
| 30S ribosomal protein S7 | 156 | ||||
| +5219 | |||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks 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 |
Protein sequence database of the Protein Information Resource More...PIRi | H65127 R3EC7K |
NCBI Reference Sequences More...RefSeqi | NP_417800.1, NC_000913.3 WP_001138045.1, NZ_LN832404.1 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1EG0 | electron microscopy | 11.50 | D | 1-146 | [»] | |
| 1M5G | model | - | G | 3-156 | [»] | |
| 1ML5 | electron microscopy | 14.00 | J | 1-156 | [»] | |
| 2YKR | electron microscopy | 9.80 | G | 2-152 | [»] | |
| 3J5S | electron microscopy | 7.50 | I | 2-152 | [»] | |
| 3J9Y | electron microscopy | 3.90 | g | 1-179 | [»] | |
| 3J9Z | electron microscopy | 3.60 | SG | 2-179 | [»] | |
| 3JA1 | electron microscopy | 3.60 | SG | 2-179 | [»] | |
| 3JBU | electron microscopy | 3.64 | G | 1-156 | [»] | |
| 3JBV | electron microscopy | 3.32 | G | 1-156 | [»] | |
| 3JCD | electron microscopy | 3.70 | g | 1-179 | [»] | |
| 3JCE | electron microscopy | 3.20 | g | 1-179 | [»] | |
| 3JCJ | electron microscopy | 3.70 | m | 1-179 | [»] | |
| 3JCN | electron microscopy | 4.60 | h | 1-179 | [»] | |
| 4A2I | electron microscopy | 16.50 | G | 3-152 | [»] | |
| 4ADV | electron microscopy | 13.50 | G | 2-179 | [»] | |
| 4U1U | X-ray | 2.95 | AG/CG | 2-152 | [»] | |
| 4U1V | X-ray | 3.00 | AG/CG | 2-152 | [»] | |
| 4U20 | X-ray | 2.90 | AG/CG | 2-152 | [»] | |
| 4U24 | X-ray | 2.90 | AG/CG | 2-152 | [»] | |
| 4U25 | X-ray | 2.90 | AG/CG | 2-152 | [»] | |
| 4U26 | X-ray | 2.80 | AG/CG | 2-152 | [»] | |
| 4U27 | X-ray | 2.80 | AG/CG | 2-152 | [»] | |
| 4V47 | electron microscopy | 12.30 | BG | 2-179 | [»] | |
| 4V48 | electron microscopy | 11.50 | BG | 2-179 | [»] | |
| 4V4H | X-ray | 3.46 | AG/CG | 1-179 | [»] | |
| 4V4Q | X-ray | 3.46 | AG/CG | 2-179 | [»] | |
| 4V4V | electron microscopy | 15.00 | AG | 20-156 | [»] | |
| 4V4W | electron microscopy | 15.00 | AG | 20-156 | [»] | |
| 4V50 | X-ray | 3.22 | AG/CG | 2-179 | [»] | |
| 4V52 | X-ray | 3.21 | AG/CG | 2-179 | [»] | |
| 4V53 | X-ray | 3.54 | AG/CG | 2-179 | [»] | |
| 4V54 | X-ray | 3.30 | AG/CG | 2-179 | [»] | |
| 4V55 | X-ray | 4.00 | AG/CG | 2-179 | [»] | |
| 4V56 | X-ray | 3.93 | AG/CG | 2-179 | [»] | |
| 4V57 | X-ray | 3.50 | AG/CG | 2-179 | [»] | |
| 4V5B | X-ray | 3.74 | BG/DG | 2-179 | [»] | |
| 4V5H | electron microscopy | 5.80 | AG | 3-152 | [»] | |
| 4V5Y | X-ray | 4.45 | AG/CG | 2-179 | [»] | |
| 4V64 | X-ray | 3.50 | AG/CG | 2-179 | [»] | |
| 4V65 | electron microscopy | 9.00 | AU | 1-179 | [»] | |
| 4V66 | electron microscopy | 9.00 | AU | 1-179 | [»] | |
| 4V69 | electron microscopy | 6.70 | AG | 3-152 | [»] | |
| 4V6C | X-ray | 3.19 | AG/CG | 1-179 | [»] | |
| 4V6D | X-ray | 3.81 | AG/CG | 1-179 | [»] | |
| 4V6E | X-ray | 3.71 | AG/CG | 1-179 | [»] | |
| 4V6K | electron microscopy | 8.25 | BK | 1-179 | [»] | |
| 4V6L | electron microscopy | 13.20 | AK | 1-179 | [»] | |
| 4V6M | electron microscopy | 7.10 | AG | 2-179 | [»] | |
| 4V6N | electron microscopy | 12.10 | BJ | 2-179 | [»] | |
| 4V6O | electron microscopy | 14.70 | AJ | 2-179 | [»] | |
| 4V6P | electron microscopy | 13.50 | AJ | 2-179 | [»] | |
| 4V6Q | electron microscopy | 11.50 | AJ | 2-179 | [»] | |
| 4V6R | electron microscopy | 11.50 | AJ | 2-179 | [»] | |
| 4V6S | electron microscopy | 13.10 | BI | 2-179 | [»] | |
| 4V6T | electron microscopy | 8.30 | AG | 2-152 | [»] | |
| 4V6V | electron microscopy | 9.80 | AG | 2-179 | [»] | |
| 4V6Y | electron microscopy | 12.00 | AG | 3-152 | [»] | |
| 4V6Z | electron microscopy | 12.00 | AG | 3-152 | [»] | |
| 4V70 | electron microscopy | 17.00 | AG | 3-152 | [»] | |
| 4V71 | electron microscopy | 20.00 | AG | 3-152 | [»] | |
| 4V72 | electron microscopy | 13.00 | AG | 3-152 | [»] | |
| 4V73 | electron microscopy | 15.00 | AG | 3-152 | [»] | |
| 4V74 | electron microscopy | 17.00 | AG | 3-152 | [»] | |
| 4V75 | electron microscopy | 12.00 | AG | 3-152 | [»] | |
| 4V76 | electron microscopy | 17.00 | AG | 3-152 | [»] | |
| 4V77 | electron microscopy | 17.00 | AG | 3-152 | [»] | |
| 4V78 | electron microscopy | 20.00 | AG | 3-152 | [»] | |
| 4V79 | electron microscopy | 15.00 | AG | 3-152 | [»] | |
| 4V7A | electron microscopy | 9.00 | AG | 3-152 | [»] | |
| 4V7B | electron microscopy | 6.80 | AG | 1-179 | [»] | |
| 4V7C | electron microscopy | 7.60 | AG | 2-179 | [»] | |
| 4V7D | electron microscopy | 7.60 | BG | 2-179 | [»] | |
| 4V7I | electron microscopy | 9.60 | BG | 1-179 | [»] | |
| 4V7S | X-ray | 3.25 | AG | 2-152 | [»] | |
| CG | 3-152 | [»] | ||||
| 4V7T | X-ray | 3.19 | AG | 2-152 | [»] | |
| CG | 3-152 | [»] | ||||
| 4V7U | X-ray | 3.10 | AG/CG | 2-152 | [»] | |
| 4V7V | X-ray | 3.29 | AG | 2-152 | [»] | |
| CG | 3-152 | [»] | ||||
| 4V85 | X-ray | 3.20 | G | 1-156 | [»] | |
| 4V89 | X-ray | 3.70 | AG | 1-179 | [»] | |
| 4V9C | X-ray | 3.30 | AG/CG | 1-179 | [»] | |
| 4V9D | X-ray | 3.00 | AG/BG | 2-152 | [»] | |
| 4V9O | X-ray | 2.90 | BG/DG/FG/HG | 1-179 | [»] | |
| 4V9P | X-ray | 2.90 | BG/DG/FG/HG | 1-179 | [»] | |
| 4WF1 | X-ray | 3.09 | AG/CG | 2-152 | [»] | |
| 4WOI | X-ray | 3.00 | AG/DG | 1-179 | [»] | |
| 4WWW | X-ray | 3.10 | QG/XG | 2-152 | [»] | |
| 4YBB | X-ray | 2.10 | AG/BG | 2-152 | [»] | |
| 5AFI | electron microscopy | 2.90 | g | 1-179 | [»] | |
| 5H5U | electron microscopy | 3.00 | n | 2-179 | [»] | |
| 5IQR | electron microscopy | 3.00 | l | 1-179 | [»] | |
| 5IT8 | X-ray | 3.12 | AG/BG | 2-152 | [»] | |
| 5J5B | X-ray | 2.80 | AG/BG | 2-152 | [»] | |
| 5J7L | X-ray | 3.00 | AG/BG | 2-152 | [»] | |
| 5J88 | X-ray | 3.32 | AG/BG | 2-152 | [»] | |
| 5J8A | X-ray | 3.10 | AG/BG | 2-152 | [»] | |
| 5J91 | X-ray | 2.96 | AG/BG | 2-152 | [»] | |
| 5JC9 | X-ray | 3.03 | AG/BG | 2-152 | [»] | |
| 5JTE | electron microscopy | 3.60 | AG | 1-179 | [»] | |
| 5JU8 | electron microscopy | 3.60 | AG | 1-179 | [»] | |
| 5KCR | electron microscopy | 3.60 | 1g | 1-179 | [»] | |
| 5KCS | electron microscopy | 3.90 | 1g | 1-179 | [»] | |
| 5KPS | electron microscopy | 3.90 | 12 | 1-179 | [»] | |
| 5KPV | electron microscopy | 4.10 | 11 | 1-179 | [»] | |
| 5KPW | electron microscopy | 3.90 | 11 | 1-179 | [»] | |
| 5KPX | electron microscopy | 3.90 | 11 | 1-179 | [»] | |
| 5L3P | electron microscopy | 3.70 | g | 1-179 | [»] | |
| 5LZA | electron microscopy | 3.60 | g | 2-152 | [»] | |
| 5LZB | electron microscopy | 5.30 | g | 2-152 | [»] | |
| 5LZC | electron microscopy | 4.80 | g | 2-152 | [»] | |
| 5LZD | electron microscopy | 3.40 | g | 2-152 | [»] | |
| 5LZE | electron microscopy | 3.50 | g | 2-152 | [»] | |
| 5LZF | electron microscopy | 4.60 | g | 2-152 | [»] | |
| 5MDV | electron microscopy | 2.97 | l | 1-179 | [»] | |
| 5MDW | electron microscopy | 3.06 | l | 1-179 | [»] | |
| 5MDY | electron microscopy | 3.35 | l | 1-179 | [»] | |
| 5MDZ | electron microscopy | 3.10 | l | 1-179 | [»] | |
| 5ME0 | electron microscopy | 13.50 | G | 1-156 | [»] | |
| 5ME1 | electron microscopy | 13.50 | G | 1-156 | [»] | |
| 5MGP | electron microscopy | 3.10 | g | 2-152 | [»] | |
| 5MY1 | electron microscopy | 7.60 | G | 2-179 | [»] | |
| 5NO2 | electron microscopy | 5.16 | G | 2-131 | [»] | |
| 5NO3 | electron microscopy | 5.16 | G | 2-131 | [»] | |
| 5NO4 | electron microscopy | 5.16 | G | 2-131 | [»] | |
| 5NP6 | electron microscopy | 3.60 | J | 2-152 | [»] | |
| 5NWY | electron microscopy | 2.93 | 6 | 1-156 | [»] | |
| 5O2R | electron microscopy | 3.40 | g | 2-152 | [»] | |
| 5U4I | electron microscopy | 3.50 | g | 1-179 | [»] | |
| 5U9F | electron microscopy | 3.20 | G | 1-156 | [»] | |
| 5U9G | electron microscopy | 3.20 | G | 1-156 | [»] | |
| 5UYK | electron microscopy | 3.90 | G | 2-152 | [»] | |
| 5UYL | electron microscopy | 3.60 | G | 2-152 | [»] | |
| 5UYM | electron microscopy | 3.20 | G | 2-152 | [»] | |
| 5UYN | electron microscopy | 4.00 | G | 2-152 | [»] | |
| 5UYP | electron microscopy | 3.90 | G | 2-152 | [»] | |
| 5UYQ | electron microscopy | 3.80 | G | 2-152 | [»] | |
| 5UZ4 | electron microscopy | 5.80 | G | 1-179 | [»] | |
| 5WDT | electron microscopy | 3.00 | g | 2-152 | [»] | |
| 5WE4 | electron microscopy | 3.10 | g | 2-152 | [»] | |
| 5WE6 | electron microscopy | 3.40 | g | 2-152 | [»] | |
| 5WFK | electron microscopy | 3.40 | g | 2-152 | [»] | |
| 6BU8 | electron microscopy | 3.50 | G | 2-152 | [»] | |
| 6C4I | electron microscopy | 3.24 | g | 1-179 | [»] | |
| 6ENF | electron microscopy | 3.20 | g | 2-152 | [»] | |
| 6ENJ | electron microscopy | 3.70 | g | 2-152 | [»] | |
| 6ENU | electron microscopy | 3.10 | g | 2-152 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P02359 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P02359 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
Database of interacting proteins More...DIPi | DIP-10783N |
Protein interaction database and analysis system More...IntActi | P02359, 154 interactors |
STRING: functional protein association networks More...STRINGi | 316385.ECDH10B_3516 |
Chemistry databases
Drug and drug target database More...DrugBanki | DB00759 Tetracycline |
Protein family/group databases
MoonProt database of moonlighting proteins More...MoonProti | P02359 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P02359 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P02359 |
PRoteomics IDEntifications database More...PRIDEi | P02359 |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAC76366; AAC76366; b3341 BAE77950; BAE77950; BAE77950 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 947846 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ecj:JW3303 eco:b3341 |
Pathosystems Resource Integration Center (PATRIC) More...PATRICi | fig|1411691.4.peg.3390 |
Organism-specific databases
EchoBASE - an integrated post-genomic database for E. coli More...EchoBASEi | EB0899 |
Escherichia coli strain K12 genome database More...EcoGenei | EG10906 rpsG |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG4108UHY Bacteria COG0049 LUCA |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000039067 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P02359 |
KEGG Orthology (KO) More...KOi | K02992 |
Identification of Orthologs from Complete Genome Data More...OMAi | TERLMNE |
Database for complete collections of gene phylogenies More...PhylomeDBi | P02359 |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | EcoCyc:EG10906-MONOMER MetaCyc:EG10906-MONOMER |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P02359 |
Protein Ontology More...PROi | PR:P02359 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.10.455.10, 1 hit |
HAMAP database of protein families More...HAMAPi | MF_00480_B Ribosomal_S7_B, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR000235 Ribosomal_S5/S7 IPR005717 Ribosomal_S7_bac/org-type IPR020606 Ribosomal_S7_CS IPR023798 Ribosomal_S7_dom IPR036823 Ribosomal_S7_dom_sf |
The PANTHER Classification System More...PANTHERi | PTHR11205 PTHR11205, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00177 Ribosomal_S7, 1 hit |
PIRSF; a whole-protein classification database More...PIRSFi | PIRSF002122 RPS7p_RPS7a_RPS5e_RPS7o, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF47973 SSF47973, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR01029 rpsG_bact, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00052 RIBOSOMAL_S7, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | RS7_ECOLI | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P02359Primary (citable) accession number: P02359 Secondary accession number(s): Q2M706 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
| Last sequence update: | January 23, 2007 | |
| Last modified: | June 20, 2018 | |
| This is version 200 of the entry and version 3 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Prokaryotic Protein Annotation Program | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - Ribosomal proteins
Ribosomal proteins families and list of entries - SIMILARITY comments
Index of protein domains and families
