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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

  • misfolded RNA binding Source: EcoCyc
  • rRNA binding Source: EcoCyc
  • structural constituent of ribosome Source: CAFA
  • tRNA binding Source: UniProtKB-UniRule

GO - Biological processi

<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
MetaCyc: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_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
30S ribosomal protein S12
Alternative name(s):
Small ribosomal subunit protein uS121 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:rpsL
Synonyms:strA
Ordered Locus Names:b3342, JW3304
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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

Organism-specific databases

Escherichia coli strain K12 genome database

More...
EcoGenei
EG10911 rpsL

<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

GO - Cellular componenti

<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_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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
DB00684 Tobramycin

<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_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_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

Encyclopedia of Proteome Dynamics

More...
EPDi
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_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
rimPP0A8A83EBI-543960,EBI-561065

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
852156, 1 interactor

Database of interacting proteins

More...
DIPi
DIP-35806N

Protein interaction database and analysis system

More...
IntActi
P0A7S3, 29 interactors

STRING: functional protein association networks

More...
STRINGi
316385.ECDH10B_p2

<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

Database of protein disorder

More...
DisProti
DP00145

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P0A7S3

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

More...
SMRi
P0A7S3

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG0048 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000040063

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P0A7S3

KEGG Orthology (KO)

More...
KOi
K02950

Database for complete collections of gene phylogenies

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PhylomeDBi
P0A7S3

Family and domain databases

Conserved Domains Database

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CDDi
cd03368 Ribosomal_S12, 1 hit

HAMAP database of protein families

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HAMAPi
MF_00403_B Ribosomal_S12_B, 1 hit

Integrated resource of protein families, domains and functional sites

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

The PANTHER Classification System

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PANTHERi
PTHR11652 PTHR11652, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00164 Ribosom_S12_S23, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF002133 Ribosomal_S12/S23, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR01034 RIBOSOMALS12

Superfamily database of structural and functional annotation

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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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

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 from positions 2 - 124. 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

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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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_CP011343.2

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
34154647
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_CP011343.2

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-L2-124[»]
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[»]
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-ray3.20L1-124[»]
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[»]
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[»]
DisProtiDP00145
ProteinModelPortaliP0A7S3
SMRiP0A7S3
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi852156, 1 interactor
DIPiDIP-35806N
IntActiP0A7S3, 29 interactors
STRINGi316385.ECDH10B_p2

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
DB00684 Tobramycin

PTM databases

iPTMnetiP0A7S3

Proteomic databases

EPDiP0A7S3
PaxDbiP0A7S3
PRIDEiP0A7S3

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76367; AAC76367; b3342
BAE77949; BAE77949; BAE77949
GeneIDi34154647
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
EcoGeneiEG10911 rpsL

Phylogenomic databases

eggNOGiCOG0048 LUCA
HOGENOMiHOG000040063
InParanoidiP0A7S3
KOiK02950
PhylomeDBiP0A7S3

Enzyme and pathway databases

BioCyciEcoCyc:EG10911-MONOMER
MetaCyc:EG10911-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0A7S3

Protein Ontology

More...
PROi
PR:P0A7S3

Family and domain databases

CDDicd03368 Ribosomal_S12, 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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry 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_and_isoforms">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: November 7, 2018
This is version 148 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Ribosomal proteins
    Ribosomal proteins families and list of entries
  4. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
UniProt is an ELIXIR core data resource
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