Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
The new UniProt website is here! Take me to UniProt BETA

UniProtKB - P02358 (RS6_ECOLI)

Entry version 219 (25 May 2022)
Sequence version 1 (21 Jul 1986)
Previous versions | rss
Add a publicationFeedback
Protein

30S ribosomal protein S6

Gene

rpsF

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

Binds together with S18 to 16S ribosomal RNA.

<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

  • cytoplasmic translation Source: ComplexPortal
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

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:EG10905-MONOMER

<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 S6
Alternative name(s):
Small ribosomal subunit protein bS61 Publication
Cleaved into the following 2 chains:
30S ribosomal protein S6, fully modified isoform
30S ribosomal protein S6, non-modified isoform
<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:rpsF
Ordered Locus Names:b4200, JW4158
<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 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 '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_00000306401 – 13530S ribosomal protein S6, fully modified isoform1 PublicationAdd BLAST135
ChainiPRO_00000306411 – 13130S ribosomal protein S6, non-modified isoformAdd BLAST131

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei93N6-acetyllysine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

5 different forms of the protein, varying only in the number of C-terminal glutamate residues, were isolated. The sequence shown is form S6-6, which is the longest. The first two Glu are encoded by the rpsF gene, the other Glu are added post-translationally by the RimK enzyme.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P02358

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P02358

PRoteomics IDEntifications database

More...PRIDEi		P02358

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...SWISS-2DPAGEi		P02358

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P02358

<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:328274, PubMed:10094780, PubMed:12809609, PubMed:16272117, PubMed:27934701, PubMed:12244297, PubMed:27906160, PubMed:27906161, PubMed:28077875).

Interacts weakly with L2 in one of the 3.5 A resolved structures (PubMed:16272117).

9 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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		4259641, 276 interactors
853015, 1 interactor

ComplexPortal: manually curated resource of macromolecular complexes

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

Database of interacting proteins

More...DIPi		DIP-10782N

Protein interaction database and analysis system

More...IntActi		P02358, 80 interactors

STRING: functional protein association networks

More...STRINGi		511145.b4200

<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

1135
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P02358

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

More...SMRi		P02358

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		P02358

<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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni98 – 135DisorderedSequence analysisAdd BLAST38

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi100 – 120Basic and acidic residuesSequence analysisAdd BLAST21
Compositional biasi121 – 135Acidic residuesSequence analysisAdd BLAST15

<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 bacterial ribosomal protein bS6 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG0360, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_113441_6_1_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P02358

Database for complete collections of gene phylogenies

More...PhylomeDBi		P02358

Family and domain databases

Conserved Domains Database

More...CDDi		cd00473, bS6, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.30.70.60, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_00360, Ribosomal_S6, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR000529, Ribosomal_S6
IPR020815, Ribosomal_S6_CS
IPR020814, Ribosomal_S6_plastid/chlpt
IPR035980, Ribosomal_S6_sf
IPR014717, Transl_elong_EF1B/ribosomal_S6

The PANTHER Classification System

More...PANTHERi		PTHR21011, PTHR21011, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01250, Ribosomal_S6, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF54995, SSF54995, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00166, S6, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS01048, RIBOSOMAL_S6, 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.

P02358-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRHYEIVFMV HPDQSEQVPG MIERYTAAIT GAEGKIHRLE DWGRRQLAYP 
        60         70         80         90        100
INKLHKAHYV LMNVEAPQEV IDELETTFRF NDAVIRSMVM RTKHAVTEAS 
       110        120        130 
PMVKAKDERR ERRDDFANET ADDAEAGDSE EEEEE
Length:135
Mass (Da):15,703
Last modified:July 21, 1986 - v1
<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:iF4CC629711C1FD0E
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAA97096 differs from that shown. Up to 4 Glu residues can be added post-translationally.1 Publication
The sequence AAC77157 differs from that shown. Up to 4 Glu residues can be added post-translationally.1 Publication
The sequence BAE78201 differs from that shown. Up to 4 Glu residues can be added post-translationally.1 Publication
The sequence CAA27652 differs from that shown. Up to 4 Glu residues can be added post-translationally.1 Publication

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 conflicti14Q → T AA sequence (PubMed:9868784).Curated1
Sequence conflicti20G → A AA sequence (PubMed:9868784).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 15187.2 Da. Determined by MALDI. 1 Publication

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
X04022 Genomic DNA Translation: CAA27652.1 Sequence problems.
U14003 Genomic DNA Translation: AAA97096.1 Sequence problems.
U00096 Genomic DNA Translation: AAC77157.5 Sequence problems.
AP009048 Genomic DNA Translation: BAE78201.1 Sequence problems.

Protein sequence database of the Protein Information Resource

More...PIRi		C65231, R3EC6

NCBI Reference Sequences

More...RefSeqi		NP_418621.5, NC_000913.3

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC77157; AAC77157; b4200
BAE78201; BAE78201; BAE78201

Database of genes from NCBI RefSeq genomes

More...GeneIDi		948723

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW4158
eco:b4200

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|511145.12.peg.4332

<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
X04022 Genomic DNA Translation: CAA27652.1 Sequence problems.
U14003 Genomic DNA Translation: AAA97096.1 Sequence problems.
U00096 Genomic DNA Translation: AAC77157.5 Sequence problems.
AP009048 Genomic DNA Translation: BAE78201.1 Sequence problems.
PIRiC65231, R3EC6
RefSeqiNP_418621.5, NC_000913.3

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 microscopy11.50C1-97[»]
2YKRelectron microscopy9.80F1-100[»]
3IY8electron microscopy14.10F2-100[»]
3J9Yelectron microscopy3.90f1-135[»]
3J9Zelectron microscopy3.60SF1-135[»]
3JA1electron microscopy3.60SF1-135[»]
3JBUelectron microscopy3.64F1-131[»]
3JBVelectron microscopy3.32F1-131[»]
3JCDelectron microscopy3.70f1-135[»]
3JCEelectron microscopy3.20f1-135[»]
3JCJelectron microscopy3.70n1-135[»]
3JCNelectron microscopy4.60i1-135[»]
4A2Ielectron microscopy16.50F1-100[»]
4ADVelectron microscopy13.50F1-135[»]
4U1UX-ray2.95AF/CF1-100[»]
4U1VX-ray3.00AF/CF1-100[»]
4U20X-ray2.90AF/CF1-100[»]
4U24X-ray2.90AF/CF1-100[»]
4U25X-ray2.90AF/CF1-100[»]
4U26X-ray2.80AF/CF1-100[»]
4U27X-ray2.80AF/CF1-100[»]
4V47electron microscopy12.30BF1-135[»]
4V48electron microscopy11.50BF1-135[»]
4V4HX-ray3.46AF/CF1-135[»]
4V4QX-ray3.46AF/CF1-135[»]
4V4Velectron microscopy15.00AF1-95[»]
4V4Welectron microscopy15.00AF1-95[»]
4V50X-ray3.22AF/CF1-135[»]
4V52X-ray3.21AF/CF1-135[»]
4V53X-ray3.54AF/CF1-135[»]
4V54X-ray3.30AF/CF1-135[»]
4V55X-ray4.00AF/CF1-135[»]
4V56X-ray3.93AF/CF1-135[»]
4V57X-ray3.50AF/CF1-135[»]
4V5BX-ray3.74BF/DF1-135[»]
4V5Helectron microscopy5.80AF1-100[»]
4V5YX-ray4.45AF/CF1-135[»]
4V64X-ray3.50AF/CF1-135[»]
4V65electron microscopy9.00AT1-135[»]
4V66electron microscopy9.00AT1-135[»]
4V69electron microscopy6.70AF1-100[»]
4V6CX-ray3.19AF/CF1-135[»]
4V6DX-ray3.81AF/CF1-135[»]
4V6EX-ray3.71AF/CF1-135[»]
4V6Kelectron microscopy8.25BJ1-135[»]
4V6Lelectron microscopy13.20AJ1-135[»]
4V6Melectron microscopy7.10AF1-135[»]
4V6Nelectron microscopy12.10BI1-135[»]
4V6Oelectron microscopy14.70AI1-135[»]
4V6Pelectron microscopy13.50AI1-135[»]
4V6Qelectron microscopy11.50AI1-135[»]
4V6Relectron microscopy11.50AI1-135[»]
4V6Selectron microscopy13.10BH1-135[»]
4V6Telectron microscopy8.30AF1-100[»]
4V6Velectron microscopy9.80AF1-135[»]
4V6Yelectron microscopy12.00AF1-100[»]
4V6Zelectron microscopy12.00AF1-100[»]
4V70electron microscopy17.00AF1-100[»]
4V71electron microscopy20.00AF1-100[»]
4V72electron microscopy13.00AF1-100[»]
4V73electron microscopy15.00AF1-100[»]
4V74electron microscopy17.00AF1-100[»]
4V75electron microscopy12.00AF1-100[»]
4V76electron microscopy17.00AF1-100[»]
4V77electron microscopy17.00AF1-100[»]
4V78electron microscopy20.00AF1-100[»]
4V79electron microscopy15.00AF1-100[»]
4V7Aelectron microscopy9.00AF1-100[»]
4V7Belectron microscopy6.80AF1-135[»]
4V7Celectron microscopy7.60AF1-131[»]
4V7Delectron microscopy7.60BF1-131[»]
4V7Ielectron microscopy9.60BF1-135[»]
4V7SX-ray3.25AF/CF1-100[»]
4V7TX-ray3.19AF/CF1-100[»]
4V7UX-ray3.10AF/CF1-100[»]
4V7VX-ray3.29AF/CF1-100[»]
4V85X-ray3.20AF1-131[»]
4V89X-ray3.70AF1-135[»]
4V9CX-ray3.30AF/CF1-135[»]
4V9DX-ray3.00AF/BF1-100[»]
4V9OX-ray2.90BF/DF/FF/HF1-135[»]
4V9PX-ray2.90BF/DF/FF/HF1-135[»]
4WF1X-ray3.09AF/CF1-100[»]
4WOIX-ray3.00AF/DF1-135[»]
4WWWX-ray3.10QF/XF1-100[»]
4YBBX-ray2.10AF/BF1-106[»]
5AFIelectron microscopy2.90f1-135[»]
5H5Uelectron microscopy3.00m1-135[»]
5IQRelectron microscopy3.00k1-135[»]
5IT8X-ray3.12AF/BF1-106[»]
5J5BX-ray2.80AF/BF1-106[»]
5J7LX-ray3.00AF/BF1-106[»]
5J88X-ray3.32AF/BF1-106[»]
5J8AX-ray3.10AF/BF1-106[»]
5J91X-ray2.96AF/BF1-106[»]
5JC9X-ray3.03AF/BF1-106[»]
5JTEelectron microscopy3.60AF1-135[»]
5JU8electron microscopy3.60AF1-135[»]
5KCRelectron microscopy3.601f1-135[»]
5KCSelectron microscopy3.901f1-135[»]
5KPSelectron microscopy3.90111-135[»]
5KPVelectron microscopy4.10101-135[»]
5KPWelectron microscopy3.90101-135[»]
5KPXelectron microscopy3.90101-135[»]
5L3Pelectron microscopy3.70f1-135[»]
5LZAelectron microscopy3.60f1-100[»]
5LZBelectron microscopy5.30f1-100[»]
5LZCelectron microscopy4.80f1-100[»]
5LZDelectron microscopy3.40f1-100[»]
5LZEelectron microscopy3.50f1-100[»]
5LZFelectron microscopy4.60f1-100[»]
5MDVelectron microscopy2.97k1-135[»]
5MDWelectron microscopy3.06k1-135[»]
5MDYelectron microscopy3.35k1-135[»]
5MDZelectron microscopy3.10k1-135[»]
5ME0electron microscopy13.50F1-131[»]
5ME1electron microscopy13.50F1-131[»]
5MGPelectron microscopy3.10f1-100[»]
5MY1electron microscopy7.60F1-135[»]
5NO2electron microscopy5.16F1-106[»]
5NO3electron microscopy5.16F1-106[»]
5NO4electron microscopy5.16F1-106[»]
5NP6electron microscopy3.60I1-100[»]
5NWYelectron microscopy2.9351-131[»]
5O2Relectron microscopy3.40f1-100[»]
5U4Ielectron microscopy3.50f1-135[»]
5U9Felectron microscopy3.20F1-131[»]
5U9Gelectron microscopy3.20F1-131[»]
5UYKelectron microscopy3.90F1-100[»]
5UYLelectron microscopy3.60F1-100[»]
5UYMelectron microscopy3.20F1-100[»]
5UYNelectron microscopy4.00F1-100[»]
5UYPelectron microscopy3.90F1-100[»]
5UYQelectron microscopy3.80F1-100[»]
5UZ4electron microscopy5.80F1-131[»]
5WDTelectron microscopy3.00f1-100[»]
5WE4electron microscopy3.10f1-100[»]
5WE6electron microscopy3.40f1-100[»]
5WFKelectron microscopy3.40f1-100[»]
6BU8electron microscopy3.50F1-126[»]
6BY1X-ray3.94AF/BF1-100[»]
6C4Ielectron microscopy3.24f1-135[»]
6DNCelectron microscopy3.70SA1-131[»]
6ENFelectron microscopy3.20f1-100[»]
6ENJelectron microscopy3.70f1-100[»]
6ENUelectron microscopy3.10f1-100[»]
6GWTelectron microscopy3.80f1-100[»]
6GXMelectron microscopy3.80f1-100[»]
6GXNelectron microscopy3.90f1-100[»]
6GXOelectron microscopy3.90f1-100[»]
6GXPelectron microscopy4.40f1-100[»]
6H4Nelectron microscopy3.00f1-100[»]
6H58electron microscopy7.90f/ff1-100[»]
6HRMelectron microscopy2.96k1-104[»]
6I7VX-ray2.90AF/BF1-100[»]
6NQBelectron microscopy3.80F1-93[»]
6O9Jelectron microscopy3.90f1-100[»]
6O9Kelectron microscopy4.00f1-100[»]
6OFXelectron microscopy3.30K1-101[»]
6OG7electron microscopy3.30K1-101[»]
6OM6electron microscopy3.10k1-135[»]
6OREelectron microscopy2.90k1-104[»]
6ORLelectron microscopy3.50k1-104[»]
6OSTelectron microscopy4.20k1-104[»]
6OT3electron microscopy3.90k1-104[»]
6OUOelectron microscopy3.70k1-104[»]
6Q97electron microscopy3.90k1-104[»]
6Q98electron microscopy4.30k1-135[»]
6Q9Aelectron microscopy3.70k1-104[»]
6SZSelectron microscopy3.06f1-135[»]
6TBVelectron microscopy2.70S0611-135[»]
6TC3electron microscopy2.70S0611-135[»]
6VWLelectron microscopy3.10e1-135[»]
6VWMelectron microscopy3.40e1-135[»]
6VWNelectron microscopy3.40e1-135[»]
6VYQelectron microscopy3.70L1-135[»]
6VYRelectron microscopy3.80L1-135[»]
6VYSelectron microscopy3.70L1-135[»]
6VYTelectron microscopy14.00L1-135[»]
6VYUelectron microscopy7.00L1-135[»]
6VYXelectron microscopy9.90L1-135[»]
6VYYelectron microscopy9.90L1-135[»]
6VYZelectron microscopy9.90L1-135[»]
6VZ2electron microscopy10.00L1-135[»]
6VZ5electron microscopy8.90L1-135[»]
6VZJelectron microscopy4.10L1-135[»]
6W6Kelectron microscopy3.60F1-135[»]
6W77electron microscopy3.60F1-135[»]
6W7Melectron microscopy3.80F1-135[»]
6W7Welectron microscopy3.90E1-135[»]
6WD6electron microscopy3.70K1-100[»]
6WDBelectron microscopy4.00K1-100[»]
6WDCelectron microscopy4.20K1-100[»]
6WDDelectron microscopy3.20K1-100[»]
6WDEelectron microscopy3.00K1-100[»]
6WDFelectron microscopy3.30K1-100[»]
6WDGelectron microscopy3.30K1-100[»]
6WDHelectron microscopy4.30K1-100[»]
6WDIelectron microscopy4.00K1-100[»]
6WDJelectron microscopy3.70K1-100[»]
6WDKelectron microscopy3.60K1-100[»]
6WDLelectron microscopy3.70K1-100[»]
6WDMelectron microscopy3.60K1-100[»]
6WNVelectron microscopy3.50K1-100[»]
6WNWelectron microscopy3.20K1-100[»]
6X6Telectron microscopy3.20L1-135[»]
6X7Felectron microscopy3.50L1-135[»]
6X7Kelectron microscopy3.10L1-135[»]
6X9Qelectron microscopy4.80L1-135[»]
6XDQelectron microscopy3.70L1-135[»]
6XDRelectron microscopy4.70L1-135[»]
6XE0electron microscopy6.80E1-100[»]
6XGFelectron microscopy5.00L1-135[»]
6XIIelectron microscopy7.00L1-135[»]
6XIJelectron microscopy8.00L1-135[»]
6XZAelectron microscopy2.66F11-106[»]
6XZBelectron microscopy2.54F11-106[»]
6Y69electron microscopy2.86f1-100[»]
7ABZelectron microscopy3.21k1-100[»]
7AC7electron microscopy3.08k1-104[»]
7ACJelectron microscopy3.20k1-104[»]
7ACRelectron microscopy3.44k1-104[»]
7AFIelectron microscopy3.53F1-135[»]
7AFLelectron microscopy4.20F1-135[»]
7AFOelectron microscopy3.93F1-135[»]
7B5Kelectron microscopy2.90f1-106[»]
7BODelectron microscopy2.88F1-135[»]
7BOEelectron microscopy2.90F1-135[»]
7BOFelectron microscopy2.92F1-135[»]
7BOGelectron microscopy2.75F1-135[»]
7BOHelectron microscopy2.82F1-135[»]
7BOIelectron microscopy2.98F1-135[»]
7CPJelectron microscopy3.30f1-135[»]
7D6Zelectron microscopy3.40m1-135[»]
7D80electron microscopy4.10G1-135[»]
7JSSelectron microscopy3.70K1-100[»]
7JSWelectron microscopy3.80K1-100[»]
7JSZelectron microscopy3.70K1-100[»]
7JT1electron microscopy3.30K1-100[»]
7JT2electron microscopy3.50K1-100[»]
7JT3electron microscopy3.70K1-100[»]
7K00electron microscopy1.98F1-135[»]
7K50electron microscopy3.40K1-100[»]
7K51electron microscopy3.50K1-100[»]
7K52electron microscopy3.40K1-100[»]
7K53electron microscopy3.20K1-100[»]
7K54electron microscopy3.20K1-100[»]
7K55electron microscopy3.30K1-100[»]
7LV0electron microscopy3.20K1-100[»]
7N1Pelectron microscopy2.33SF1-135[»]
7N2Celectron microscopy2.72SF1-135[»]
7N2Uelectron microscopy2.53SF1-135[»]
7N2Velectron microscopy2.54SF1-135[»]
7N30electron microscopy2.66SF1-135[»]
7N31electron microscopy2.69SF1-135[»]
7NARelectron microscopy3.00F1-135[»]
7NASelectron microscopy3.31F1-135[»]
7NATelectron microscopy3.59F1-135[»]
7NAUelectron microscopy3.78F1-135[»]
7NAVelectron microscopy4.80F1-135[»]
7NAXelectron microscopy2.96F1-135[»]
7NWTelectron microscopy2.66k1-135[»]
7O19electron microscopy2.90AF1-135[»]
7O1Aelectron microscopy2.40AF1-135[»]
7O1Celectron microscopy2.60AF1-135[»]
7O5Helectron microscopy3.10F1-106[»]
7OE0electron microscopy2.69F1-135[»]
7OE1electron microscopy3.05F1-135[»]
7OI0electron microscopy2.76F1-135[»]
7OIZelectron microscopy2.90F1-135[»]
7OJ0electron microscopy3.50F1-135[»]
7P3Kelectron microscopy2.90F1-135[»]
7PJSelectron microscopy2.35f1-135[»]
7PJTelectron microscopy6.00f1-135[»]
7PJUelectron microscopy9.50f1-135[»]
7PJVelectron microscopy3.10f1-135[»]
7PJWelectron microscopy4.00f1-135[»]
7PJXelectron microscopy6.50f1-135[»]
7PJYelectron microscopy3.10f1-135[»]
7PJZelectron microscopy6.00f1-135[»]
7S1Gelectron microscopy2.48H1-135[»]
7S1Helectron microscopy2.35H1-135[»]
7S1Kelectron microscopy2.42H1-135[»]
AlphaFoldDBiP02358
SMRiP02358
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4259641, 276 interactors
853015, 1 interactor
ComplexPortaliCPX-3802, 30S small ribosomal subunit
DIPiDIP-10782N
IntActiP02358, 80 interactors
STRINGi511145.b4200

PTM databases

iPTMnetiP02358

2D gel databases

SWISS-2DPAGEiP02358

Proteomic databases

jPOSTiP02358
PaxDbiP02358
PRIDEiP02358

Genome annotation databases

EnsemblBacteriaiAAC77157; AAC77157; b4200
BAE78201; BAE78201; BAE78201
GeneIDi948723
KEGGiecj:JW4158
eco:b4200
PATRICifig|511145.12.peg.4332

Organism-specific databases

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

More...EchoBASEi		EB0898

Phylogenomic databases

eggNOGiCOG0360, Bacteria
HOGENOMiCLU_113441_6_1_6
InParanoidiP02358
PhylomeDBiP02358

Enzyme and pathway databases

BioCyciEcoCyc:EG10905-MONOMER

Miscellaneous databases

EvolutionaryTraceiP02358

Protein Ontology

More...PROi		PR:P02358

Family and domain databases

CDDicd00473, bS6, 1 hit
Gene3Di3.30.70.60, 1 hit
HAMAPiMF_00360, Ribosomal_S6, 1 hit
InterProiView protein in InterPro
IPR000529, Ribosomal_S6
IPR020815, Ribosomal_S6_CS
IPR020814, Ribosomal_S6_plastid/chlpt
IPR035980, Ribosomal_S6_sf
IPR014717, Transl_elong_EF1B/ribosomal_S6
PANTHERiPTHR21011, PTHR21011, 1 hit
PfamiView protein in Pfam
PF01250, Ribosomal_S6, 1 hit
SUPFAMiSSF54995, SSF54995, 1 hit
TIGRFAMsiTIGR00166, S6, 1 hit
PROSITEiView protein in PROSITE
PS01048, RIBOSOMAL_S6, 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 nameiRS6_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: P02358
Secondary accession number(s): Q2M6A5
<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: July 21, 1986
Last modified: May 25, 2022
This is version 219 of the entry and version 1 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
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again