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UniProtKB - P0A7S3 (RS12_ECOLI)

Entry version 169 (25 May 2022)
Sequence version 2 (23 Jan 2007)
Previous versions | rss
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Protein

30S ribosomal protein S12

Gene

rpsL

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

With S4 and S5 plays an important role in translational accuracy.

Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit (By similarity).

By similarity1 Publication

Cryo-EM studies suggest that S12 contacts the EF-Tu bound tRNA in the A-site during codon-recognition. This contact is most likely broken as the aminoacyl-tRNA moves into the peptidyl transferase center in the 50S subunit.

1 Publication

Miscellaneous

At least 19 substitutions or deletions in 11 codons can promote streptomycin resistance, dependence or pseudodependence; all but one of the streptomycin resistant mutations (K42R) are associated with hyperaccurate translation and thus reduced translational efficiency.2 Publications
The streptomycin sensitive allele is dominant to resistant alleles.

<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
Biological processAntibiotic resistance

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:EG10911-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 S12
Alternative name(s):
Small ribosomal subunit protein uS121 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:rpsL
Synonyms:strA
Ordered Locus Names:b3342, JW3304
<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>Mutagenesisi57L → H: Protein is not incorporated into ribosomes. 1 Publication1
Mutagenesisi88K → Q: Confers low-level resistance to streptomycin and a 15% decrease in the translational elongation rate. 1 Publication1

Chemistry databases

Drug and drug target database

More...DrugBanki		DB00479, Amikacin
DB06696, Arbekacin
DB00452, Framycetin
DB00798, Gentamicin
DB04729, Gentamicin C1a
DB01172, Kanamycin
DB00994, Neomycin
DB00955, Netilmicin
DB03615, Ribostamycin
DB00919, Spectinomycin
DB01082, Streptomycin
DB00560, Tigecycline

DrugCentral

More...DrugCentrali		P0A7S3

<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_00001462192 – 12430S ribosomal protein S12Add BLAST123

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 residuei893-methylthioaspartic acid1 Publication1
Modified residuei108N6-acetyllysine1 Publication1

Keywords - PTMi

Acetylation, Methylation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P0A7S3

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

More...PaxDbi		P0A7S3

PRoteomics IDEntifications database

More...PRIDEi		P0A7S3

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P0A7S3

<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:320034, PubMed:7556101, PubMed:12809609, PubMed:16272117, PubMed:27934701, PubMed:10094780, PubMed:12093756, PubMed:12379845, PubMed:12244297, PubMed:27906160, PubMed:27906161). Contacts proteins S8 and S17.

Interacts with ArfA (PubMed:27906160, PubMed:27906161). May interact with IF1 in the 30S initiation complex (By similarity).

By similarity11 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		852156, 1 interactor

ComplexPortal: manually curated resource of macromolecular complexes

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

Database of interacting proteins

More...DIPi		DIP-35806N

Protein interaction database and analysis system

More...IntActi		P0A7S3, 45 interactors

STRING: functional protein association networks

More...STRINGi		511145.b3342

<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

1124
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P0A7S3

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

More...SMRi		P0A7S3

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		P0A7S3

<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 uS12 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG0048, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_104295_1_2_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P0A7S3

Identification of Orthologs from Complete Genome Data

More...OMAi		SPALEKC

Database for complete collections of gene phylogenies

More...PhylomeDBi		P0A7S3

Family and domain databases

Conserved Domains Database

More...CDDi		cd03368, Ribosomal_S12, 1 hit

Database of protein disorder

More...DisProti		DP00145

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.40.50.140, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_00403_B, Ribosomal_S12_B, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR012340, NA-bd_OB-fold
IPR006032, Ribosomal_S12/S23
IPR005679, Ribosomal_S12_bac

The PANTHER Classification System

More...PANTHERi		PTHR11652, PTHR11652, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00164, Ribosom_S12_S23, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF002133, Ribosomal_S12/S23, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR01034, RIBOSOMALS12

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50249, SSF50249, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00981, rpsL_bact, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00055, RIBOSOMAL_S12, 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.

P0A7S3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MATVNQLVRK PRARKVAKSN VPALEACPQK RGVCTRVYTT TPKKPNSALR 
        60         70         80         90        100
KVCRVRLTNG FEVTSYIGGE GHNLQEHSVI LIRGGRVKDL PGVRYHTVRG 
       110        120 
ALDCSGVKDR KQARSKYGVK RPKA
Length:124
Mass (Da):13,737
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:i94A57F4C4FF0FC5E
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 13651.3 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 varianti43K → R Confers streptomycin resistance but not hyperaccurate translation. 1

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
V00355 Genomic DNA Translation: CAA23648.1
U18997 Genomic DNA Translation: AAA58139.1
U00096 Genomic DNA Translation: AAC76367.1
AP009048 Genomic DNA Translation: BAE77949.1
AF312716 Genomic DNA Translation: AAG30936.1
AF312717 Genomic DNA Translation: AAG30937.1
V00354 Genomic DNA Translation: CAA23647.1
J01688 Genomic DNA Translation: AAA50988.1

Protein sequence database of the Protein Information Resource

More...PIRi		S13738, R3EC12

NCBI Reference Sequences

More...RefSeqi		NP_417801.1, NC_000913.3
WP_000246815.1, NZ_STEB01000004.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC76367; AAC76367; b3342
BAE77949; BAE77949; BAE77949

Database of genes from NCBI RefSeq genomes

More...GeneIDi		64727495
67463992
947845

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW3304
eco:b3342

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.3389

<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
V00355 Genomic DNA Translation: CAA23648.1
U18997 Genomic DNA Translation: AAA58139.1
U00096 Genomic DNA Translation: AAC76367.1
AP009048 Genomic DNA Translation: BAE77949.1
AF312716 Genomic DNA Translation: AAG30936.1
AF312717 Genomic DNA Translation: AAG30937.1
V00354 Genomic DNA Translation: CAA23647.1
J01688 Genomic DNA Translation: AAA50988.1
PIRiS13738, R3EC12
RefSeqiNP_417801.1, NC_000913.3
WP_000246815.1, NZ_STEB01000004.1

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
1MJ1electron microscopy13.00O5-123[»]
1ZN1electron microscopy14.10L28-124[»]
2YKRelectron microscopy9.80L2-124[»]
3DEGelectron microscopy-D2-124[»]
3EP2electron microscopy-L2-124[»]
3EQ3electron microscopy-L2-124[»]
3EQ4electron microscopy-L2-124[»]
3IY8electron microscopy14.10L2-124[»]
3J0Delectron microscopy11.10I2-124[»]
3J0Eelectron microscopy9.90F2-124[»]
3J9Yelectron microscopy3.90l1-124[»]
3J9Zelectron microscopy3.60SL2-124[»]
3JA1electron microscopy3.60SL2-124[»]
3JBUelectron microscopy3.64L1-124[»]
3JBVelectron microscopy3.32L1-124[»]
3JCDelectron microscopy3.70l1-124[»]
3JCEelectron microscopy3.20l1-124[»]
3JCJelectron microscopy3.70t1-124[»]
3JCNelectron microscopy4.60o1-124[»]
4A2Ielectron microscopy16.50L2-124[»]
4ADVelectron microscopy13.50L2-124[»]
4U1UX-ray2.95AL/CL2-124[»]
4U1VX-ray3.00AL/CL2-124[»]
4U20X-ray2.90AL/CL2-124[»]
4U24X-ray2.90AL/CL2-124[»]
4U25X-ray2.90AL/CL2-124[»]
4U26X-ray2.80AL/CL2-124[»]
4U27X-ray2.80AL/CL2-124[»]
4V47electron microscopy12.30BL2-124[»]
4V48electron microscopy11.50BL2-124[»]
4V4HX-ray3.46AL/CL1-124[»]
4V4QX-ray3.46AL/CL2-124[»]
4V4Velectron microscopy15.00AL23-123[»]
4V4Welectron microscopy15.00AL23-123[»]
4V50X-ray3.22AL/CL2-124[»]
4V52X-ray3.21AL/CL2-124[»]
4V53X-ray3.54AL/CL2-124[»]
4V54X-ray3.30AL/CL2-124[»]
4V55X-ray4.00AL/CL2-124[»]
4V56X-ray3.93AL/CL2-124[»]
4V57X-ray3.50AL/CL2-124[»]
4V5BX-ray3.74BL/DL2-124[»]
4V5Helectron microscopy5.80AL2-124[»]
4V5YX-ray4.45AL/CL2-124[»]
4V64X-ray3.50AL/CL2-124[»]
4V65electron microscopy9.00AD1-124[»]
4V66electron microscopy9.00AD1-124[»]
4V69electron microscopy6.70AL2-124[»]
4V6CX-ray3.19AL/CL1-124[»]
4V6DX-ray3.81AL/CL1-124[»]
4V6EX-ray3.71AL/CL1-124[»]
4V6Kelectron microscopy8.25BP1-124[»]
4V6Lelectron microscopy13.20AP1-124[»]
4V6Melectron microscopy7.10AL2-124[»]
AO2-89[»]
4V6Nelectron microscopy12.10BO2-124[»]
4V6Oelectron microscopy14.70AO2-124[»]
4V6Pelectron microscopy13.50AO2-124[»]
4V6Qelectron microscopy11.50AO2-124[»]
4V6Relectron microscopy11.50AO2-124[»]
4V6Selectron microscopy13.10BN2-124[»]
4V6Telectron microscopy8.30AL2-124[»]
4V6Velectron microscopy9.80AL2-124[»]
4V6Yelectron microscopy12.00AL1-124[»]
4V6Zelectron microscopy12.00AL1-124[»]
4V70electron microscopy17.00AL1-124[»]
4V71electron microscopy20.00AL1-124[»]
4V72electron microscopy13.00AL1-124[»]
4V73electron microscopy15.00AL1-124[»]
4V74electron microscopy17.00AL1-124[»]
4V75electron microscopy12.00AL1-124[»]
4V76electron microscopy17.00AL1-124[»]
4V77electron microscopy17.00AL1-124[»]
4V78electron microscopy20.00AL1-124[»]
4V79electron microscopy15.00AL1-124[»]
4V7Aelectron microscopy9.00AL1-124[»]
4V7Belectron microscopy6.80AL1-124[»]
4V7Celectron microscopy7.60AL2-124[»]
4V7Delectron microscopy7.60BL2-124[»]
4V7Ielectron microscopy9.60BL1-124[»]
4V7SX-ray3.25AL/CL2-124[»]
4V7TX-ray3.19AL/CL2-124[»]
4V7UX-ray3.10AL/CL2-124[»]
4V7VX-ray3.29AL/CL2-124[»]
4V85X-ray3.20AL1-124[»]
4V89X-ray3.70AL1-124[»]
4V9CX-ray3.30AL/CL1-124[»]
4V9DX-ray3.00AL/BL2-124[»]
4V9OX-ray2.90BL/DL/FL/HL1-124[»]
4V9PX-ray2.90BL/DL/FL/HL1-124[»]
4WF1X-ray3.09AL/CL2-124[»]
4WOIX-ray3.00AL/DL1-124[»]
4WWWX-ray3.10QL/XL2-124[»]
4YBBX-ray2.10AL/BL2-124[»]
5AFIelectron microscopy2.90l1-124[»]
5H5Uelectron microscopy3.00s2-124[»]
5IQRelectron microscopy3.00q1-124[»]
5IT8X-ray3.12AL/BL2-124[»]
5J5BX-ray2.80AL/BL2-124[»]
5J7LX-ray3.00AL/BL2-124[»]
5J88X-ray3.32AL/BL2-124[»]
5J8AX-ray3.10AL/BL2-124[»]
5J91X-ray2.96AL/BL2-124[»]
5JC9X-ray3.03AL/BL2-124[»]
5JTEelectron microscopy3.60AL1-124[»]
5JU8electron microscopy3.60AL1-124[»]
5KCRelectron microscopy3.601l1-124[»]
5KCSelectron microscopy3.901l1-124[»]
5KPSelectron microscopy3.90171-124[»]
5KPVelectron microscopy4.10161-124[»]
5KPWelectron microscopy3.90161-124[»]
5KPXelectron microscopy3.90161-124[»]
5L3Pelectron microscopy3.70l1-124[»]
5LZAelectron microscopy3.60l2-124[»]
5LZBelectron microscopy5.30l2-124[»]
5LZCelectron microscopy4.80l2-124[»]
5LZDelectron microscopy3.40l2-124[»]
5LZEelectron microscopy3.50l2-124[»]
5LZFelectron microscopy4.60l2-124[»]
5MDVelectron microscopy2.97q1-124[»]
5MDWelectron microscopy3.06q1-124[»]
5MDYelectron microscopy3.35q1-124[»]
5MDZelectron microscopy3.10q1-124[»]
5ME0electron microscopy13.50L2-124[»]
5ME1electron microscopy13.50L2-124[»]
5MGPelectron microscopy3.10l2-124[»]
5MY1electron microscopy7.60L2-124[»]
5NO2electron microscopy5.16L2-15[»]
5NO3electron microscopy5.16L2-15[»]
5NO4electron microscopy5.16L2-15[»]
5NP6electron microscopy3.60O2-124[»]
5NWYelectron microscopy2.93B1-124[»]
5O2Relectron microscopy3.40l2-124[»]
5U4Ielectron microscopy3.50l2-124[»]
5U4Jelectron microscopy3.70l1-124[»]
5U9Felectron microscopy3.20L1-124[»]
5U9Gelectron microscopy3.20L1-124[»]
5UYKelectron microscopy3.90L2-124[»]
5UYLelectron microscopy3.60L2-124[»]
5UYMelectron microscopy3.20L2-124[»]
5UYNelectron microscopy4.00L2-124[»]
5UYPelectron microscopy3.90L2-124[»]
5UYQelectron microscopy3.80L2-124[»]
5WDTelectron microscopy3.00l2-122[»]
5WE4electron microscopy3.10l2-122[»]
5WE6electron microscopy3.40l2-122[»]
5WFKelectron microscopy3.40l2-122[»]
6BU8electron microscopy3.50L2-124[»]
6BY1X-ray3.94AL/BL2-124[»]
6C4Ielectron microscopy3.24l1-124[»]
6ENFelectron microscopy3.20l2-124[»]
6ENJelectron microscopy3.70l2-124[»]
6ENUelectron microscopy3.10l2-124[»]
6GWTelectron microscopy3.80l2-124[»]
6GXMelectron microscopy3.80l2-124[»]
6GXNelectron microscopy3.90l2-124[»]
6GXOelectron microscopy3.90l2-124[»]
6GXPelectron microscopy4.40l2-124[»]
6H4Nelectron microscopy3.00l2-124[»]
6H58electron microscopy7.90l/ll2-124[»]
6HRMelectron microscopy2.96q2-124[»]
6I7VX-ray2.90AL/BL2-124[»]
6O9Jelectron microscopy3.90l2-124[»]
6O9Kelectron microscopy4.00l2-124[»]
6OFXelectron microscopy3.30Q2-124[»]
6OG7electron microscopy3.30Q2-124[»]
6OREelectron microscopy2.90q2-124[»]
6ORLelectron microscopy3.50q2-124[»]
6OSTelectron microscopy4.20q2-124[»]
6OT3electron microscopy3.90q2-88[»]
6OUOelectron microscopy3.70q2-88[»]
6Q9Aelectron microscopy3.70q2-123[»]
6SZSelectron microscopy3.06l1-124[»]
6TBVelectron microscopy2.70S1211-124[»]
6TC3electron microscopy2.70S1211-124[»]
6VWLelectron microscopy3.10k1-124[»]
6VWMelectron microscopy3.40k1-124[»]
6VWNelectron microscopy3.40k1-124[»]
6W6Kelectron microscopy3.60L1-124[»]
6W77electron microscopy3.60L1-124[»]
6W7Melectron microscopy3.80L1-124[»]
6W7Nelectron microscopy3.40L1-124[»]
6W7Welectron microscopy3.90K1-124[»]
6WD6electron microscopy3.70Q2-124[»]
6WDBelectron microscopy4.00Q2-124[»]
6WDCelectron microscopy4.20Q2-124[»]
6WDDelectron microscopy3.20Q2-124[»]
6WDEelectron microscopy3.00Q2-124[»]
6WDFelectron microscopy3.30Q2-124[»]
6WDGelectron microscopy3.30Q2-124[»]
6WDHelectron microscopy4.30Q2-124[»]
6WDIelectron microscopy4.00Q2-124[»]
6WDJelectron microscopy3.70Q2-124[»]
6WDKelectron microscopy3.60Q2-124[»]
6WDLelectron microscopy3.70Q2-124[»]
6WDMelectron microscopy3.60Q2-124[»]
6WNVelectron microscopy3.50Q2-124[»]
6WNWelectron microscopy3.20Q2-124[»]
6XE0electron microscopy6.80K2-124[»]
6XZAelectron microscopy2.66L12-124[»]
6XZBelectron microscopy2.54L12-124[»]
6Y69electron microscopy2.86l2-124[»]
6ZTLelectron microscopy3.50AL1-124[»]
7ABZelectron microscopy3.21q2-124[»]
7AC7electron microscopy3.08q2-124[»]
7ACJelectron microscopy3.20q2-123[»]
7ACRelectron microscopy3.44q2-123[»]
7B5Kelectron microscopy2.90l2-124[»]
7BODelectron microscopy2.88L1-124[»]
7BOEelectron microscopy2.90L1-124[»]
7BOFelectron microscopy2.92L1-124[»]
7BOGelectron microscopy2.75L1-124[»]
7BOHelectron microscopy2.82L1-124[»]
7BOIelectron microscopy2.98L1-124[»]
7D6Zelectron microscopy3.40s1-124[»]
7D80electron microscopy4.10M1-124[»]
7JSSelectron microscopy3.70Q2-124[»]
7JSWelectron microscopy3.80Q2-124[»]
7JSZelectron microscopy3.70Q2-124[»]
7JT1electron microscopy3.30Q2-124[»]
7JT2electron microscopy3.50Q2-124[»]
7JT3electron microscopy3.70Q2-124[»]
7K50electron microscopy3.40Q2-124[»]
7K51electron microscopy3.50Q2-124[»]
7K52electron microscopy3.40Q2-124[»]
7K53electron microscopy3.20Q2-124[»]
7K54electron microscopy3.20Q2-124[»]
7K55electron microscopy3.30Q2-124[»]
7LV0electron microscopy3.20Q2-124[»]
7NARelectron microscopy3.00L1-124[»]
7NASelectron microscopy3.31L1-124[»]
7NATelectron microscopy3.59L1-124[»]
7NAUelectron microscopy3.78L1-124[»]
7NAVelectron microscopy4.80L1-124[»]
7NWTelectron microscopy2.66q1-124[»]
7O19electron microscopy2.90AL1-124[»]
7O1Aelectron microscopy2.40AL1-124[»]
7O1Celectron microscopy2.60AL1-124[»]
7O5Helectron microscopy3.10L2-124[»]
7OE0electron microscopy2.69L2-124[»]
7OE1electron microscopy3.05L2-124[»]
7OI0electron microscopy2.76L2-124[»]
7OIZelectron microscopy2.90L1-124[»]
7OJ0electron microscopy3.50L1-124[»]
7P3Kelectron microscopy2.90L1-124[»]
7PJVelectron microscopy3.10l1-124[»]
7PJYelectron microscopy3.10l1-124[»]
7S1Kelectron microscopy2.42t1-124[»]
AlphaFoldDBiP0A7S3
SMRiP0A7S3
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi852156, 1 interactor
ComplexPortaliCPX-3802, 30S small ribosomal subunit
DIPiDIP-35806N
IntActiP0A7S3, 45 interactors
STRINGi511145.b3342

Chemistry databases

DrugBankiDB00479, Amikacin
DB06696, Arbekacin
DB00452, Framycetin
DB00798, Gentamicin
DB04729, Gentamicin C1a
DB01172, Kanamycin
DB00994, Neomycin
DB00955, Netilmicin
DB03615, Ribostamycin
DB00919, Spectinomycin
DB01082, Streptomycin
DB00560, Tigecycline
DrugCentraliP0A7S3

PTM databases

iPTMnetiP0A7S3

Proteomic databases

jPOSTiP0A7S3
PaxDbiP0A7S3
PRIDEiP0A7S3

Genome annotation databases

EnsemblBacteriaiAAC76367; AAC76367; b3342
BAE77949; BAE77949; BAE77949
GeneIDi64727495
67463992
947845
KEGGiecj:JW3304
eco:b3342
PATRICifig|1411691.4.peg.3389

Organism-specific databases

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

More...EchoBASEi		EB0904

Phylogenomic databases

eggNOGiCOG0048, Bacteria
HOGENOMiCLU_104295_1_2_6
InParanoidiP0A7S3
OMAiSPALEKC
PhylomeDBiP0A7S3

Enzyme and pathway databases

BioCyciEcoCyc:EG10911-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0A7S3

Protein Ontology

More...PROi		PR:P0A7S3

Family and domain databases

CDDicd03368, Ribosomal_S12, 1 hit
DisProtiDP00145
Gene3Di2.40.50.140, 1 hit
HAMAPiMF_00403_B, Ribosomal_S12_B, 1 hit
InterProiView protein in InterPro
IPR012340, NA-bd_OB-fold
IPR006032, Ribosomal_S12/S23
IPR005679, Ribosomal_S12_bac
PANTHERiPTHR11652, PTHR11652, 1 hit
PfamiView protein in Pfam
PF00164, Ribosom_S12_S23, 1 hit
PIRSFiPIRSF002133, Ribosomal_S12/S23, 1 hit
PRINTSiPR01034, RIBOSOMALS12
SUPFAMiSSF50249, SSF50249, 1 hit
TIGRFAMsiTIGR00981, rpsL_bact, 1 hit
PROSITEiView protein in PROSITE
PS00055, RIBOSOMAL_S12, 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 nameiRS12_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: P0A7S3
Secondary accession number(s): P02367, Q2M707, Q9F5N3
<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: May 25, 2022
This is version 169 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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