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UniProtKB - P02359 (RS7_ECOLI)

Entry version 223 (23 Feb 2022)
Sequence version 3 (23 Jan 2007)
Previous versions | rss
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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

<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>

<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

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 (PubMed:2461734).

Is located at the subunit interface close to the decoding center, where it has been shown to contact mRNA (PubMed:10606263).

Has been shown to contact tRNA in both the P and E sites; it probably blocks exit of the E site tRNA (PubMed:8524654).

3 Publications

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

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 (PubMed:7000779, PubMed:6349681, PubMed:11684020).3 Publications

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionRibonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding, tRNA-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc: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%5Fand%5Ftaxonomy%5Fsection">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 S7
Alternative name(s):
Small ribosomal subunit protein uS71 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

<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>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 keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi2 – 18Missing : Defective in ribosome assembly; accumulates to abnormally high levels on polysomes; significantly decreases affinity for its own mRNA. 1 PublicationAdd BLAST17
Mutagenesisi36K → A or E: Defective in ribosome assembly. 1 Publication1
Mutagenesisi116M → G: Significantly decreases affinity for its own mRNA. 1 Publication1

Chemistry databases

Drug and drug target database

More...DrugBanki		DB09093, Chlortetracycline
DB13092, Meclocycline
DB12455, Omadacycline
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 keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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 methionineiRemoved1 Publication
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001242592 – 17930S ribosomal protein S7Add BLAST178

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Part of the 30S ribosomal subunit (PubMed:385062, PubMed:7556101, PubMed:10094780, PubMed:12809609, PubMed:16272117, PubMed:27934701, PubMed:12244297, PubMed:27906160, PubMed:27906161, PubMed:28077875). Contacts proteins S9 and S11 (By similarity). Cross-links to IF3 and the P and E site tRNAs (PubMed:7000779, PubMed:6349681, PubMed:8524654).

By similarity2 Publications11 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		852157, 1 interactor

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-3802, 30S small ribosomal subunit

Database of interacting proteins

More...DIPi		DIP-10783N

Protein interaction database and analysis system

More...IntActi		P02359, 167 interactors

STRING: functional protein association networks

More...STRINGi		511145.b3341

<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

1179
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P02359

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		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

Belongs to the universal ribosomal protein uS7 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG0049, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_072226_1_1_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P02359

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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i8627DB380C4A9C0D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 conflicti92Missing AA sequence (PubMed:385062).Curated1

<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

Molecular mass is 19888.7 Da. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 varianti157 – 179Missing in strain: B and L44. 1 PublicationAdd BLAST23

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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

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

<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:
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:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EG0electron microscopy11.50D1-146[»]
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-ray3.20AG1-156[»]
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[»]
5H5Uelectron microscopy3.00n2-179[»]
5IQRelectron microscopy3.00l1-179[»]
5IT8X-ray3.12AG/BG2-152[»]
5J5BX-ray2.80AG/BG2-152[»]
5J7LX-ray3.00AG/BG2-152[»]
5J88X-ray3.32AG/BG2-152[»]
5J8AX-ray3.10AG/BG2-152[»]
5J91X-ray2.96AG/BG2-152[»]
5JC9X-ray3.03AG/BG2-152[»]
5JTEelectron microscopy3.60AG1-179[»]
5JU8electron microscopy3.60AG1-179[»]
5KCRelectron microscopy3.601g1-179[»]
5KCSelectron microscopy3.901g1-179[»]
5KPSelectron microscopy3.90121-179[»]
5KPVelectron microscopy4.10111-179[»]
5KPWelectron microscopy3.90111-179[»]
5KPXelectron microscopy3.90111-179[»]
5L3Pelectron microscopy3.70g1-179[»]
5LZAelectron microscopy3.60g2-152[»]
5LZBelectron microscopy5.30g2-152[»]
5LZCelectron microscopy4.80g2-152[»]
5LZDelectron microscopy3.40g2-152[»]
5LZEelectron microscopy3.50g2-152[»]
5LZFelectron microscopy4.60g2-152[»]
5MDVelectron microscopy2.97l1-179[»]
5MDWelectron microscopy3.06l1-179[»]
5MDYelectron microscopy3.35l1-179[»]
5MDZelectron microscopy3.10l1-179[»]
5ME0electron microscopy13.50G1-156[»]
5ME1electron microscopy13.50G1-156[»]
5MGPelectron microscopy3.10g2-152[»]
5MY1electron microscopy7.60G2-179[»]
5NO2electron microscopy5.16G2-131[»]
5NO3electron microscopy5.16G2-131[»]
5NO4electron microscopy5.16G2-131[»]
5NP6electron microscopy3.60J2-152[»]
5NWYelectron microscopy2.9361-156[»]
5O2Relectron microscopy3.40g2-152[»]
5U4Ielectron microscopy3.50g1-179[»]
5U9Felectron microscopy3.20G1-156[»]
5U9Gelectron microscopy3.20G1-156[»]
5UYKelectron microscopy3.90G2-152[»]
5UYLelectron microscopy3.60G2-152[»]
5UYMelectron microscopy3.20G2-152[»]
5UYNelectron microscopy4.00G2-152[»]
5UYPelectron microscopy3.90G2-152[»]
5UYQelectron microscopy3.80G2-152[»]
5UZ4electron microscopy5.80G1-179[»]
5WDTelectron microscopy3.00g2-152[»]
5WE4electron microscopy3.10g2-152[»]
5WE6electron microscopy3.40g2-152[»]
5WFKelectron microscopy3.40g2-152[»]
6BU8electron microscopy3.50G2-152[»]
6BY1X-ray3.94AG/BG1-179[»]
6C4Ielectron microscopy3.24g1-179[»]
6ENFelectron microscopy3.20g2-152[»]
6ENJelectron microscopy3.70g2-152[»]
6ENUelectron microscopy3.10g2-152[»]
6GWTelectron microscopy3.80g2-152[»]
6GXMelectron microscopy3.80g2-152[»]
6GXNelectron microscopy3.90g2-152[»]
6GXOelectron microscopy3.90g2-152[»]
6GXPelectron microscopy4.40g2-152[»]
6H4Nelectron microscopy3.00g2-162[»]
6H58electron microscopy7.90g/gg2-162[»]
6HRMelectron microscopy2.96l2-152[»]
6I7VX-ray2.90AG/BG2-152[»]
6O9Jelectron microscopy3.90g3-152[»]
6O9Kelectron microscopy4.00g2-152[»]
6OFXelectron microscopy3.30L2-152[»]
6OG7electron microscopy3.30L2-152[»]
6OREelectron microscopy2.90l2-152[»]
6ORLelectron microscopy3.50l2-152[»]
6OSTelectron microscopy4.20l2-152[»]
6OT3electron microscopy3.90l2-152[»]
6OUOelectron microscopy3.70l2-152[»]
6Q97electron microscopy3.90l2-152[»]
6Q98electron microscopy4.30l1-179[»]
6Q9Aelectron microscopy3.70l2-153[»]
6SZSelectron microscopy3.06g1-179[»]
6TBVelectron microscopy2.70S0711-179[»]
6TC3electron microscopy2.70S0711-179[»]
6VWLelectron microscopy3.10f1-179[»]
6VWMelectron microscopy3.40f1-179[»]
6VWNelectron microscopy3.40f1-179[»]
6W7Melectron microscopy3.80G1-179[»]
6WD6electron microscopy3.70L2-152[»]
6WDBelectron microscopy4.00L2-152[»]
6WDCelectron microscopy4.20L2-152[»]
6WDDelectron microscopy3.20L2-152[»]
6WDEelectron microscopy3.00L2-152[»]
6WDFelectron microscopy3.30L2-152[»]
6WDGelectron microscopy3.30L2-152[»]
6WDHelectron microscopy4.30L2-152[»]
6WDIelectron microscopy4.00L2-152[»]
6WDJelectron microscopy3.70L2-152[»]
6WDKelectron microscopy3.60L2-152[»]
6WDLelectron microscopy3.70L2-152[»]
6WDMelectron microscopy3.60L2-152[»]
6WNVelectron microscopy3.50L2-152[»]
6WNWelectron microscopy3.20L2-152[»]
6XE0electron microscopy6.80F2-152[»]
6XZAelectron microscopy2.66G12-152[»]
6XZBelectron microscopy2.54G12-152[»]
6Y69electron microscopy2.86g2-156[»]
6ZTJelectron microscopy3.40AG1-156[»]
6ZTLelectron microscopy3.50AG1-156[»]
6ZTMelectron microscopy3.30AG1-156[»]
6ZTNelectron microscopy3.90AG1-156[»]
6ZTOelectron microscopy3.00AG1-156[»]
6ZTPelectron microscopy3.00AG1-156[»]
6ZU1electron microscopy3.00AG1-156[»]
7ABZelectron microscopy3.21l2-152[»]
7AC7electron microscopy3.08l2-152[»]
7ACJelectron microscopy3.20l2-152[»]
7ACRelectron microscopy3.44l2-152[»]
7B5Kelectron microscopy2.90g2-152[»]
7D6Zelectron microscopy3.40n1-179[»]
7D80electron microscopy4.10H1-179[»]
7JSSelectron microscopy3.70L2-152[»]
7JSWelectron microscopy3.80L2-152[»]
7JSZelectron microscopy3.70L2-152[»]
7JT1electron microscopy3.30L2-152[»]
7JT2electron microscopy3.50L2-152[»]
7JT3electron microscopy3.70L2-152[»]
7K50electron microscopy3.40L2-152[»]
7K51electron microscopy3.50L2-152[»]
7K52electron microscopy3.40L2-152[»]
7K53electron microscopy3.20L2-152[»]
7K54electron microscopy3.20L2-152[»]
7K55electron microscopy3.30L2-152[»]
7LV0electron microscopy3.20L2-152[»]
7N1Pelectron microscopy2.33SG1-179[»]
7N2Celectron microscopy2.72SG1-179[»]
7N2Uelectron microscopy2.53SG1-179[»]
7N2Velectron microscopy2.54SG1-179[»]
7N30electron microscopy2.66SG1-179[»]
7N31electron microscopy2.69SG1-179[»]
7NSOelectron microscopy2.90g2-152[»]
7NSPelectron microscopy3.50g2-152[»]
7NSQelectron microscopy3.10g2-152[»]
7O19electron microscopy2.90AG1-179[»]
7O1Aelectron microscopy2.40AG1-179[»]
7O1Celectron microscopy2.60AG1-179[»]
7OE0electron microscopy2.69G2-179[»]
7OIZelectron microscopy2.90G1-179[»]
7OJ0electron microscopy3.50G1-179[»]
7P3Kelectron microscopy2.90G1-179[»]
7PJSelectron microscopy2.35g1-179[»]
7PJTelectron microscopy6.00g1-179[»]
7PJVelectron microscopy3.10g1-179[»]
7PJWelectron microscopy4.00g1-179[»]
7PJXelectron microscopy6.50g1-179[»]
7PJYelectron microscopy3.10g1-179[»]
7PJZelectron microscopy6.00g1-179[»]
SMRiP02359
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi852157, 1 interactor
ComplexPortaliCPX-3802, 30S small ribosomal subunit
DIPiDIP-10783N
IntActiP02359, 167 interactors
STRINGi511145.b3341

Chemistry databases

DrugBankiDB09093, Chlortetracycline
DB13092, Meclocycline
DB12455, Omadacycline
DB00759, Tetracycline

Protein family/group databases

MoonProtiP02359

Proteomic databases

jPOSTiP02359
PaxDbiP02359
PRIDEiP02359

Genome annotation databases

EnsemblBacteriaiAAC76366; AAC76366; b3341
BAE77950; BAE77950; BAE77950
GeneIDi947846
KEGGiecj:JW3303
eco:b3341
PATRICifig|1411691.4.peg.3390

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...EchoBASEi		EB0899

Phylogenomic databases

eggNOGiCOG0049, Bacteria
HOGENOMiCLU_072226_1_1_6
InParanoidiP02359
PhylomeDBiP02359

Enzyme and pathway databases

BioCyciEcoCyc:EG10906-MONOMER

Miscellaneous databases

EvolutionaryTraceiP02359

Protein Ontology

More...PROi		PR:P02359

Family and domain databases

Gene3Di1.10.455.10, 1 hit
HAMAPiMF_00480_B, Ribosomal_S7_B, 1 hit
InterProiView 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
PANTHERiPTHR11205, PTHR11205, 1 hit
PfamiView protein in Pfam
PF00177, Ribosomal_S7, 1 hit
PIRSFiPIRSF002122, RPS7p_RPS7a_RPS5e_RPS7o, 1 hit
SUPFAMiSSF47973, SSF47973, 1 hit
TIGRFAMsiTIGR01029, rpsG_bact, 1 hit
PROSITEiView protein in PROSITE
PS00052, RIBOSOMAL_S7, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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 nameiRS7_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>AccessioniPrimary (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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: February 23, 2022
This is version 223 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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic 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

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. Ribosomal proteins
    Ribosomal proteins families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
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