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UniProtKB - P0A7S9 (RS13_ECOLI)

Entry version 156 (07 Apr 2021)
Sequence version 2 (23 Jan 2007)
Previous versions | rss
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Protein

30S ribosomal protein S13

Gene

rpsM

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

Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA.1 Publication
In the E.coli 70S ribosome in the initiation state (PubMed:12809609) was modeled to contact the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; bridge B1a is broken in the model with bound EF-G, while the protein-protein contacts between S13 and L5 in B1b change (PubMed:12809609). The 23S rRNA contact site in bridge B1a is modeled to differ in different ribosomal states (PubMed:16272117), contacting alternately S13 or S19. In the two 3.5 angstroms resolved ribosome structures (PubMed:12859903) the contacts between L5, S13 and S19 bridge B1b are different, confirming the dynamic nature of this interaction. Bridge B1a is not visible in the crystallized ribosomes due to 23S rRNA disorder.4 Publications
Contacts the tRNAs in the A and P sites.1 Publication
The C-terminal tail plays a role in the affinity of the 30S P site for different tRNAs.1 Publication

<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:EG10912-MONOMER
MetaCyc:EG10912-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 S13
Alternative name(s):
Small ribosomal subunit protein uS131 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:rpsM
Ordered Locus Names:b3298, JW3260
<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>Mutagenesisi83 – 118Missing : Decreased growth rate at all temperatures. Decreased affinity of the 30S subunit P site for tRNA in vitro. 1 PublicationAdd BLAST36
Mutagenesisi114 – 118Missing : Decreased growth rate at all temperatures. Decreased affinity of the 30S subunit P site for tRNA in vitro. 1 Publication5

Chemistry databases

Drug and drug target database

More...DrugBanki		DB00560, Tigecycline

<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_00001320892 – 11830S ribosomal protein S13Add BLAST117

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P0A7S9

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

More...PaxDbi		P0A7S9

PRoteomics IDEntifications database

More...PRIDEi		P0A7S9

<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:330375, PubMed:3279034, PubMed:10094780, PubMed:12809609, PubMed:16272117, PubMed:12859903, PubMed:27934701, PubMed:12244297, PubMed:27906160, PubMed:27906161).

Forms a loose heterodimer with protein S19 (PubMed:3279034). Cross-links to the P site tRNA and weakly to the A site tRNA (PubMed:8524654). Forms two bridges to the 50S subunit in the 70S ribosome, contacting the 16S rRNA and proteins S19 and L5 (PubMed:12809609, PubMed:16272117, PubMed:12859903).

11 Publications

Protein-protein interaction databases

ComplexPortal: manually curated resource of macromolecular complexes

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

Database of interacting proteins

More...DIPi		DIP-35855N

Protein interaction database and analysis system

More...IntActi		P0A7S9, 108 interactors

STRING: functional protein association networks

More...STRINGi		511145.b3298

<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

1118
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		P0A7S9

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		P0A7S9

<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 uS13 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG0099, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_103849_1_2_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P0A7S9

Database for complete collections of gene phylogenies

More...PhylomeDBi		P0A7S9

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		4.10.910.10, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_01315, Ribosomal_S13_S18, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR027437, 30s_Rbsml_prot_S13_C
IPR001892, Ribosomal_S13
IPR010979, Ribosomal_S13-like_H2TH
IPR019980, Ribosomal_S13_bac-type
IPR018269, Ribosomal_S13_CS

The PANTHER Classification System

More...PANTHERi		PTHR10871:SF1, PTHR10871:SF1, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00416, Ribosomal_S13, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF002134, Ribosomal_S13, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF46946, SSF46946, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR03631, uS13_bact, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00646, RIBOSOMAL_S13_1, 1 hit
PS50159, RIBOSOMAL_S13_2, 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.

P0A7S9-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MARIAGINIP DHKHAVIALT SIYGVGKTRS KAILAAAGIA EDVKISELSE 
        60         70         80         90        100
GQIDTLRDEV AKFVVEGDLR REISMSIKRL MDLGCYRGLR HRRGLPVRGQ 
       110 
RTKTNARTRK GPRKPIKK
Length:118
Mass (Da):13,099
Last modified:January 23, 2007 - v2
<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:i6277C365EBE4F732
GO

<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 12968.1 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 varianti89 – 99Missing in PW118; partially suppresses a rimM deletion. 1 PublicationAdd BLAST11
Natural varianti100 – 118Missing in rpsM413; pseudorevertant of streptomycin resistance. A strong antisuppressor of two tRNA suppressors, decreases translation step time and growth rate. 1 PublicationAdd BLAST19
Natural varianti105N → H in PW095; partially suppresses a rimM deletion. 1 Publication1
Natural varianti105N → K in PW097; partially suppresses a rimM deletion. 1 Publication1

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
X02543 Genomic DNA Translation: CAA26392.1
U18997 Genomic DNA Translation: AAA58093.1
U00096 Genomic DNA Translation: AAC76323.1
AP009048 Genomic DNA Translation: BAE77993.1
M12432 Genomic DNA Translation: AAA83903.1
M10213 Genomic DNA Translation: AAA72457.1

Protein sequence database of the Protein Information Resource

More...PIRi		A23807, R3EC13

NCBI Reference Sequences

More...RefSeqi		NP_417757.1, NC_000913.3
WP_000090775.1, NZ_STEB01000038.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC76323; AAC76323; b3298
BAE77993; BAE77993; BAE77993

Database of genes from NCBI RefSeq genomes

More...GeneIDi		58463223
947791

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW3260
eco:b3298

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.3433

<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
X02543 Genomic DNA Translation: CAA26392.1
U18997 Genomic DNA Translation: AAA58093.1
U00096 Genomic DNA Translation: AAC76323.1
AP009048 Genomic DNA Translation: BAE77993.1
M12432 Genomic DNA Translation: AAA83903.1
M10213 Genomic DNA Translation: AAA72457.1
PIRiA23807, R3EC13
RefSeqiNP_417757.1, NC_000913.3
WP_000090775.1, NZ_STEB01000038.1

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
1M5Gmodel-M2-118[»]
2YKRelectron microscopy9.80M2-115[»]
3J9Yelectron microscopy3.90m1-118[»]
3J9Zelectron microscopy3.60SM2-118[»]
3JA1electron microscopy3.60SM2-118[»]
3JBUelectron microscopy3.64M1-118[»]
3JBVelectron microscopy3.32M1-118[»]
3JCDelectron microscopy3.70m1-118[»]
3JCEelectron microscopy3.20m1-118[»]
3JCJelectron microscopy3.70s1-118[»]
3JCNelectron microscopy4.60n1-118[»]
4A2Ielectron microscopy16.50M2-115[»]
4ADVelectron microscopy13.50M2-118[»]
4U1UX-ray2.95AM/CM2-115[»]
4U1VX-ray3.00AM/CM2-115[»]
4U20X-ray2.90AM/CM2-115[»]
4U24X-ray2.90AM/CM2-115[»]
4U25X-ray2.90AM/CM2-115[»]
4U26X-ray2.80AM/CM2-115[»]
4U27X-ray2.80AM/CM2-115[»]
4V47electron microscopy12.30BM2-118[»]
4V48electron microscopy11.50BM2-118[»]
4V4HX-ray3.46AM/CM1-118[»]
4V4QX-ray3.46AM/CM2-118[»]
4V4Velectron microscopy15.00AM2-116[»]
4V4Welectron microscopy15.00AM2-116[»]
4V50X-ray3.22AM/CM2-118[»]
4V52X-ray3.21AM/CM2-118[»]
4V53X-ray3.54AM/CM2-118[»]
4V54X-ray3.30AM/CM2-118[»]
4V55X-ray4.00AM/CM2-118[»]
4V56X-ray3.93AM/CM2-118[»]
4V57X-ray3.50AM/CM2-118[»]
4V5BX-ray3.74BM/DM2-118[»]
4V5Helectron microscopy5.80AM2-114[»]
4V5YX-ray4.45AM/CM2-118[»]
4V64X-ray3.50AM/CM2-118[»]
4V65electron microscopy9.00AF1-118[»]
4V66electron microscopy9.00AF1-118[»]
4V69electron microscopy6.70AM2-114[»]
4V6CX-ray3.19AM/CM1-118[»]
4V6DX-ray3.81AM/CM1-118[»]
4V6EX-ray3.71AM/CM1-118[»]
4V6Kelectron microscopy8.25BQ1-118[»]
4V6Lelectron microscopy13.20AQ1-118[»]
4V6Nelectron microscopy12.10BP2-118[»]
4V6Oelectron microscopy14.70AP2-118[»]
4V6Pelectron microscopy13.50AP2-118[»]
4V6Qelectron microscopy11.50AP2-118[»]
4V6Relectron microscopy11.50AP2-118[»]
4V6Selectron microscopy13.10BO2-118[»]
4V6Telectron microscopy8.30AM2-115[»]
4V6Velectron microscopy9.80AM2-118[»]
4V6Yelectron microscopy12.00AM1-114[»]
4V6Zelectron microscopy12.00AM1-114[»]
4V70electron microscopy17.00AM1-114[»]
4V71electron microscopy20.00AM1-114[»]
4V72electron microscopy13.00AM1-114[»]
4V73electron microscopy15.00AM1-114[»]
4V74electron microscopy17.00AM1-114[»]
4V75electron microscopy12.00AM1-114[»]
4V76electron microscopy17.00AM1-114[»]
4V77electron microscopy17.00AM1-114[»]
4V78electron microscopy20.00AM1-114[»]
4V79electron microscopy15.00AM1-114[»]
4V7Aelectron microscopy9.00AM1-114[»]
4V7Belectron microscopy6.80AM1-118[»]
4V7Celectron microscopy7.60AM2-118[»]
4V7Delectron microscopy7.60BM2-118[»]
4V7Ielectron microscopy9.60BM1-118[»]
4V7SX-ray3.25AM2-115[»]
CM2-114[»]
4V7TX-ray3.19AM2-115[»]
CM2-114[»]
4V7UX-ray3.10AM/CM2-115[»]
4V7VX-ray3.29AM2-115[»]
CM2-114[»]
4V85X-ray3.20AM1-118[»]
4V89X-ray3.70AM1-118[»]
4V9CX-ray3.30AM/CM1-118[»]
4V9DX-ray3.00AM/BM2-115[»]
4V9OX-ray2.90BM/DM/FM/HM1-118[»]
4V9PX-ray2.90BM/DM/FM/HM1-118[»]
4WF1X-ray3.09AM/CM2-115[»]
4WOIX-ray3.00AM/DM1-118[»]
4WWWX-ray3.10QM/XM2-115[»]
4YBBX-ray2.10AM/BM2-115[»]
5AFIelectron microscopy2.90m1-118[»]
5H5Uelectron microscopy3.00t2-118[»]
5IQRelectron microscopy3.00r1-118[»]
5IT8X-ray3.12AM/BM2-115[»]
5J5BX-ray2.80AM/BM2-115[»]
5J7LX-ray3.00AM/BM2-115[»]
5J88X-ray3.32AM/BM2-115[»]
5J8AX-ray3.10AM/BM2-115[»]
5J91X-ray2.96AM/BM2-115[»]
5JC9X-ray3.03AM/BM2-115[»]
5JTEelectron microscopy3.60AM1-118[»]
5JU8electron microscopy3.60AM1-118[»]
5KCRelectron microscopy3.601m1-118[»]
5KCSelectron microscopy3.901m1-118[»]
5KPSelectron microscopy3.90181-118[»]
5KPVelectron microscopy4.10171-118[»]
5KPWelectron microscopy3.90171-118[»]
5KPXelectron microscopy3.90171-118[»]
5L3Pelectron microscopy3.70m1-118[»]
5LZAelectron microscopy3.60m2-115[»]
5LZBelectron microscopy5.30m2-115[»]
5LZCelectron microscopy4.80m2-115[»]
5LZDelectron microscopy3.40m2-115[»]
5LZEelectron microscopy3.50m2-115[»]
5LZFelectron microscopy4.60m2-115[»]
5MDVelectron microscopy2.97r1-118[»]
5MDWelectron microscopy3.06r1-118[»]
5MDYelectron microscopy3.35r1-118[»]
5MDZelectron microscopy3.10r1-118[»]
5ME0electron microscopy13.50M1-118[»]
5ME1electron microscopy13.50M1-118[»]
5MGPelectron microscopy3.10m2-115[»]
5MY1electron microscopy7.60M2-118[»]
5NO2electron microscopy5.16M2-115[»]
5NO3electron microscopy5.16M2-115[»]
5NO4electron microscopy5.16M2-115[»]
5NP6electron microscopy3.60P2-115[»]
5NWYelectron microscopy2.93C1-118[»]
5O2Relectron microscopy3.40m2-115[»]
5U4Ielectron microscopy3.50m1-118[»]
5U9Felectron microscopy3.20M1-118[»]
5U9Gelectron microscopy3.20M1-118[»]
5UYKelectron microscopy3.90M2-115[»]
5UYLelectron microscopy3.60M2-115[»]
5UYMelectron microscopy3.20M2-115[»]
5UYNelectron microscopy4.00M2-115[»]
5UYPelectron microscopy3.90M2-115[»]
5UYQelectron microscopy3.80M2-115[»]
5UZ4electron microscopy5.80M1-118[»]
5WDTelectron microscopy3.00m2-116[»]
5WE4electron microscopy3.10m2-116[»]
5WE6electron microscopy3.40m2-115[»]
5WFKelectron microscopy3.40m2-116[»]
6BU8electron microscopy3.50M2-115[»]
6BY1X-ray3.94AM/BM2-115[»]
6C4Ielectron microscopy3.24m1-118[»]
6DNCelectron microscopy3.70ZA1-118[»]
6ENFelectron microscopy3.20m2-115[»]
6ENJelectron microscopy3.70m2-115[»]
6ENUelectron microscopy3.10m2-115[»]
6GWTelectron microscopy3.80m2-115[»]
6GXMelectron microscopy3.80m2-115[»]
6GXNelectron microscopy3.90m2-115[»]
6GXOelectron microscopy3.90m2-115[»]
6GXPelectron microscopy4.40m2-115[»]
6H4Nelectron microscopy3.00m2-115[»]
6H58electron microscopy7.90m/mm2-115[»]
6HRMelectron microscopy2.96r2-117[»]
6I7VX-ray2.90AM/BM2-115[»]
6O9Jelectron microscopy3.90m2-115[»]
6O9Kelectron microscopy4.00m2-115[»]
6OFXelectron microscopy3.30R2-115[»]
6OG7electron microscopy3.30R2-115[»]
6OREelectron microscopy2.90r2-117[»]
6ORLelectron microscopy3.50r2-117[»]
6OSTelectron microscopy4.20r2-117[»]
6OT3electron microscopy3.90r2-117[»]
6OUOelectron microscopy3.70r2-117[»]
6Q98electron microscopy4.30r1-118[»]
6Q9Aelectron microscopy3.70r2-117[»]
6SZSelectron microscopy3.06m1-118[»]
6TBVelectron microscopy2.70S1311-118[»]
6TC3electron microscopy2.70S1311-118[»]
6VWLelectron microscopy3.10l1-118[»]
6VWMelectron microscopy3.40l1-118[»]
6VWNelectron microscopy3.40l1-118[»]
6W6Kelectron microscopy3.60M1-118[»]
6W77electron microscopy3.60M1-118[»]
6W7Melectron microscopy3.80M1-118[»]
6W7Nelectron microscopy3.40M1-118[»]
6WD6electron microscopy3.70R2-115[»]
6WDBelectron microscopy4.00R2-115[»]
6WDCelectron microscopy4.20R2-115[»]
6WDDelectron microscopy3.20R2-115[»]
6WDEelectron microscopy3.00R2-115[»]
6WDFelectron microscopy3.30R2-115[»]
6WDGelectron microscopy3.30R2-115[»]
6WDHelectron microscopy4.30R2-115[»]
6WDIelectron microscopy4.00R2-115[»]
6WDJelectron microscopy3.70R2-115[»]
6WDKelectron microscopy3.60R2-115[»]
6WDLelectron microscopy3.70R2-115[»]
6WDMelectron microscopy3.60R2-115[»]
6WNVelectron microscopy3.50R2-115[»]
6WNWelectron microscopy3.20R2-115[»]
6XE0electron microscopy6.80L2-115[»]
6XZAelectron microscopy2.66M12-115[»]
6XZBelectron microscopy2.54M12-115[»]
6Y69electron microscopy2.86m2-115[»]
6ZTLelectron microscopy3.50AM1-118[»]
7JSSelectron microscopy3.70R2-115[»]
7JSWelectron microscopy3.80R2-115[»]
7JSZelectron microscopy3.70R2-115[»]
7JT1electron microscopy3.30R2-115[»]
7JT2electron microscopy3.50R2-115[»]
7JT3electron microscopy3.70R2-115[»]
SMRiP0A7S9
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

ComplexPortaliCPX-3802, 30S small ribosomal subunit
DIPiDIP-35855N
IntActiP0A7S9, 108 interactors
STRINGi511145.b3298

Chemistry databases

DrugBankiDB00560, Tigecycline

Proteomic databases

jPOSTiP0A7S9
PaxDbiP0A7S9
PRIDEiP0A7S9

Genome annotation databases

EnsemblBacteriaiAAC76323; AAC76323; b3298
BAE77993; BAE77993; BAE77993
GeneIDi58463223
947791
KEGGiecj:JW3260
eco:b3298
PATRICifig|1411691.4.peg.3433

Organism-specific databases

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

More...EchoBASEi		EB0905

Phylogenomic databases

eggNOGiCOG0099, Bacteria
HOGENOMiCLU_103849_1_2_6
InParanoidiP0A7S9
PhylomeDBiP0A7S9

Enzyme and pathway databases

BioCyciEcoCyc:EG10912-MONOMER
MetaCyc:EG10912-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0A7S9

Protein Ontology

More...PROi		PR:P0A7S9

Family and domain databases

Gene3Di4.10.910.10, 1 hit
HAMAPiMF_01315, Ribosomal_S13_S18, 1 hit
InterProiView protein in InterPro
IPR027437, 30s_Rbsml_prot_S13_C
IPR001892, Ribosomal_S13
IPR010979, Ribosomal_S13-like_H2TH
IPR019980, Ribosomal_S13_bac-type
IPR018269, Ribosomal_S13_CS
PANTHERiPTHR10871:SF1, PTHR10871:SF1, 1 hit
PfamiView protein in Pfam
PF00416, Ribosomal_S13, 1 hit
PIRSFiPIRSF002134, Ribosomal_S13, 1 hit
SUPFAMiSSF46946, SSF46946, 1 hit
TIGRFAMsiTIGR03631, uS13_bact, 1 hit
PROSITEiView protein in PROSITE
PS00646, RIBOSOMAL_S13_1, 1 hit
PS50159, RIBOSOMAL_S13_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

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 nameiRS13_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: P0A7S9
Secondary accession number(s): P02369, Q2M6W3
<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: April 7, 2021
This is version 156 of the entry and version 2 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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