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UniProtKB - P61175 (RL22_ECOLI)

Entry version 176 (25 May 2022)
Sequence version 1 (21 Jul 1986)
Previous versions | rss
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Protein

50S ribosomal protein L22

Gene

rplV

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

This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.

1 Publication

The globular domain of the protein is one of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that penetrates into the center of the 70S ribosome where it lines the wall of the exit tunnel. Removal of most of this hairpin (residues 85-95) does not prevent its incorporation into 70S ribosomes. Two of the hairpin residues (91 and 93) seem to be involved in translation elongation arrest of the SecM protein, as their replacement by larger amino acids alleviates the arrest.

2 Publications

Miscellaneous

The wild-type allele (erythromycin sensitive) is dominant over the resistant allele, and is also dominant over the temperature-sensitive allele at both low and high temperatures.

<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
Biological processAntibiotic resistance

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:EG10882-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:
50S ribosomal protein L22
Alternative name(s):
Large ribosomal subunit protein uL221 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:rplV
Synonyms:eryB
Ordered Locus Names:b3315, JW3277
<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>Mutagenesisi82 – 99Missing : Incorporated into ribosomes in vivo, but is easily removed by a salt wash. 1 PublicationAdd BLAST18
Mutagenesisi85 – 95Missing : Incorporates into ribosomes in vivo. 1 PublicationAdd BLAST11
Mutagenesisi91G → A, D or S: Abolishes translation elongation arrest of SecM. 1 Publication1
Mutagenesisi93A → S, T or V: Abolishes translation elongation arrest of SecM. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001251531 – 11050S ribosomal protein L22Add BLAST110

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P61175

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

More...PaxDbi		P61175

PRoteomics IDEntifications database

More...PRIDEi		P61175

<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 50S ribosomal subunit.

10 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		852125, 1 interactor

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-3807, 50S large ribosomal subunit

Database of interacting proteins

More...DIPi		DIP-35983N

Protein interaction database and analysis system

More...IntActi		P61175, 142 interactors

STRING: functional protein association networks

More...STRINGi		511145.b3315

<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

1110
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P61175

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

More...SMRi		P61175

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		P61175

<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 uL22 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG0091, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_083987_3_3_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P61175

Identification of Orthologs from Complete Genome Data

More...OMAi		KRIQPRA

Database for complete collections of gene phylogenies

More...PhylomeDBi		P61175

Family and domain databases

Conserved Domains Database

More...CDDi		cd00336, Ribosomal_L22, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.90.470.10, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_01331_B, Ribosomal_L22_B, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR001063, Ribosomal_L22
IPR018260, Ribosomal_L22/L17_CS
IPR036394, Ribosomal_L22/L17_sf
IPR005727, Ribosomal_L22_bac/chlpt-type

The PANTHER Classification System

More...PANTHERi		PTHR13501, PTHR13501, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00237, Ribosomal_L22, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF54843, SSF54843, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR01044, rplV_bact, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00464, RIBOSOMAL_L22, 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.

P61175-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
METIAKHRHA RSSAQKVRLV ADLIRGKKVS QALDILTYTN KKAAVLVKKV 
        60         70         80         90        100
LESAIANAEH NDGADIDDLK VTKIFVDEGP SMKRIMPRAK GRADRILKRT 
       110
SHITVVVSDR
Length:110
Mass (Da):12,226
Last modified:July 21, 1986 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iF0E0C6982772277C
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 12225.3 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 varianti8R → C in strain: SK1048; decreases translational rate, tRNA binding and subunit association at 44 degrees Celsius; does not alter 23S rRNA or L4 interactions; not erythromycin resistant. 1 Publication1
Natural varianti82 – 84Missing in strain: N281; confers erythromycin resistance; ribosomes bind erythromycin normally and have normal peptidyltransferase activity; 50S subunits assemble normally, even in the presence of drug; the protein is incorporated into ribosomes in vivo; abolishes translation elongation arrest of SecM. 2 Publications3

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
X02613 Genomic DNA Translation: CAA26465.1
U18997 Genomic DNA Translation: AAA58112.1
U00096 Genomic DNA Translation: AAC76340.1
AP009048 Genomic DNA Translation: BAE77976.1

Protein sequence database of the Protein Information Resource

More...PIRi		G23129, R5EC22

NCBI Reference Sequences

More...RefSeqi		NP_417774.1, NC_000913.3
WP_000447529.1, NZ_STEB01000038.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC76340; AAC76340; b3315
BAE77976; BAE77976; BAE77976

Database of genes from NCBI RefSeq genomes

More...GeneIDi		60373126
67415356
947813

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW3277
eco:b3315

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.3416

<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
X02613 Genomic DNA Translation: CAA26465.1
U18997 Genomic DNA Translation: AAA58112.1
U00096 Genomic DNA Translation: AAC76340.1
AP009048 Genomic DNA Translation: BAE77976.1
PIRiG23129, R5EC22
RefSeqiNP_417774.1, NC_000913.3
WP_000447529.1, 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
2J28electron microscopy8.00S1-110[»]
2RDOelectron microscopy9.10S1-110[»]
3BBXelectron microscopy10.00S1-110[»]
3J5Lelectron microscopy6.60S1-110[»]
3J7Zelectron microscopy3.90S1-110[»]
3J8Gelectron microscopy5.00S1-110[»]
3J9Yelectron microscopy3.90S1-110[»]
3J9Zelectron microscopy3.60LQ1-110[»]
3JA1electron microscopy3.60LU1-110[»]
3JBUelectron microscopy3.64s1-110[»]
3JBVelectron microscopy3.32s1-110[»]
3JCDelectron microscopy3.70S1-110[»]
3JCEelectron microscopy3.20S1-110[»]
3JCJelectron microscopy3.70R1-110[»]
3JCNelectron microscopy4.60S1-110[»]
4CSUelectron microscopy5.50S1-110[»]
4U1UX-ray2.95BS/DS1-110[»]
4U1VX-ray3.00BS/DS1-110[»]
4U20X-ray2.90BS/DS1-110[»]
4U24X-ray2.90BS/DS1-110[»]
4U25X-ray2.90BS/DS1-110[»]
4U26X-ray2.80BS/DS1-110[»]
4U27X-ray2.80BS/DS1-110[»]
4UY8electron microscopy3.80S1-110[»]
4V47electron microscopy12.30AQ1-110[»]
4V48electron microscopy11.50AQ1-110[»]
4V4HX-ray3.46BS/DS1-110[»]
4V4QX-ray3.46BS/DS1-110[»]
4V4Velectron microscopy15.00BQ5-110[»]
4V4Welectron microscopy15.00BQ5-110[»]
4V50X-ray3.22BS/DS1-110[»]
4V52X-ray3.21BS/DS1-110[»]
4V53X-ray3.54BS/DS1-110[»]
4V54X-ray3.30BS/DS1-110[»]
4V55X-ray4.00BS/DS1-110[»]
4V56X-ray3.93BS/DS1-110[»]
4V57X-ray3.50BS/DS1-110[»]
4V5BX-ray3.74AS/CS1-110[»]
4V5Helectron microscopy5.80BS1-110[»]
4V5YX-ray4.45BS/DS1-110[»]
4V64X-ray3.50BS/DS1-110[»]
4V65electron microscopy9.00BL1-110[»]
4V66electron microscopy9.00BL1-110[»]
4V69electron microscopy6.70BS1-110[»]
4V6CX-ray3.19BS/DS1-110[»]
4V6DX-ray3.81BS/DS1-110[»]
4V6EX-ray3.71BS/DS1-110[»]
4V6Kelectron microscopy8.25AT1-110[»]
4V6Lelectron microscopy13.20BT1-110[»]
4V6Melectron microscopy7.10BS1-110[»]
4V6Nelectron microscopy12.10AU1-110[»]
4V6Oelectron microscopy14.70BU1-110[»]
4V6Pelectron microscopy13.50BU1-110[»]
4V6Qelectron microscopy11.50BU1-110[»]
4V6Relectron microscopy11.50BU1-110[»]
4V6Selectron microscopy13.10AU1-110[»]
4V6Telectron microscopy8.30BS1-110[»]
4V6Velectron microscopy9.80BW1-110[»]
4V6Yelectron microscopy12.00BS1-110[»]
4V6Zelectron microscopy12.00BS1-110[»]
4V70electron microscopy17.00BS1-110[»]
4V71electron microscopy20.00BS1-110[»]
4V72electron microscopy13.00BS1-110[»]
4V73electron microscopy15.00BS1-110[»]
4V74electron microscopy17.00BS1-110[»]
4V75electron microscopy12.00BS1-110[»]
4V76electron microscopy17.00BS1-110[»]
4V77electron microscopy17.00BS1-110[»]
4V78electron microscopy20.00BS1-110[»]
4V79electron microscopy15.00BS1-110[»]
4V7Aelectron microscopy9.00BS1-110[»]
4V7Belectron microscopy6.80BS1-110[»]
4V7Celectron microscopy7.60BU1-110[»]
4V7Delectron microscopy7.60AV1-110[»]
4V7Ielectron microscopy9.60AS1-110[»]
4V7SX-ray3.25BS/DS1-110[»]
4V7TX-ray3.19BS/DS1-110[»]
4V7UX-ray3.10BS/DS1-110[»]
4V7VX-ray3.29BS/DS1-110[»]
4V85X-ray3.20BW1-110[»]
4V89X-ray3.70BW1-110[»]
4V9CX-ray3.30BS/DS1-110[»]
4V9DX-ray3.00CS/DS1-110[»]
4V9OX-ray2.90AS/CS/ES/GS1-110[»]
4V9PX-ray2.90AS/CS/ES/GS1-110[»]
4WF1X-ray3.09BS/DS1-110[»]
4WOIX-ray3.00BS/CS1-110[»]
4WWWX-ray3.10RS/YS1-110[»]
4YBBX-ray2.10CT/DT1-110[»]
5ADYelectron microscopy4.50S1-110[»]
5AFIelectron microscopy2.90S1-110[»]
5AKAelectron microscopy5.70S1-110[»]
5GADelectron microscopy3.70T1-110[»]
5GAEelectron microscopy3.33T1-110[»]
5GAFelectron microscopy4.30T1-110[»]
5GAGelectron microscopy3.80T1-110[»]
5GAHelectron microscopy3.80T1-110[»]
5H5Uelectron microscopy3.00T1-110[»]
5IQRelectron microscopy3.00S1-110[»]
5IT8X-ray3.12CT/DT1-110[»]
5J5BX-ray2.80CT/DT1-110[»]
5J7LX-ray3.00CT/DT1-110[»]
5J88X-ray3.32CT/DT1-110[»]
5J8AX-ray3.10CT/DT1-110[»]
5J91X-ray2.96CT/DT1-110[»]
5JC9X-ray3.03CT/DT1-110[»]
5JTEelectron microscopy3.60BS1-110[»]
5JU8electron microscopy3.60BS1-110[»]
5KCRelectron microscopy3.601W1-110[»]
5KCSelectron microscopy3.901W1-110[»]
5KPSelectron microscopy3.90S1-110[»]
5KPVelectron microscopy4.10R1-110[»]
5KPWelectron microscopy3.90R1-110[»]
5KPXelectron microscopy3.90R1-110[»]
5L3Pelectron microscopy3.70W1-110[»]
5LZAelectron microscopy3.60S1-110[»]
5LZBelectron microscopy5.30S1-110[»]
5LZCelectron microscopy4.80S1-110[»]
5LZDelectron microscopy3.40S1-110[»]
5LZEelectron microscopy3.50S1-110[»]
5LZFelectron microscopy4.60S1-110[»]
5MDVelectron microscopy2.97S1-110[»]
5MDWelectron microscopy3.06S1-110[»]
5MDYelectron microscopy3.35S1-110[»]
5MDZelectron microscopy3.10S1-110[»]
5MGPelectron microscopy3.10S1-110[»]
5NCOelectron microscopy4.80T1-110[»]
5NP6electron microscopy3.60q1-110[»]
5NWYelectron microscopy2.93f1-110[»]
5O2Relectron microscopy3.40S1-110[»]
5U4Ielectron microscopy3.50T1-110[»]
5U9Felectron microscopy3.20211-110[»]
5U9Gelectron microscopy3.20211-110[»]
5UYKelectron microscopy3.90211-110[»]
5UYLelectron microscopy3.60211-110[»]
5UYMelectron microscopy3.20211-110[»]
5UYNelectron microscopy4.00211-110[»]
5UYPelectron microscopy3.90211-110[»]
5UYQelectron microscopy3.80211-110[»]
5WDTelectron microscopy3.00S1-109[»]
5WE4electron microscopy3.10S1-109[»]
5WE6electron microscopy3.40S1-109[»]
5WFKelectron microscopy3.40S1-109[»]
6BU8electron microscopy3.50211-110[»]
6BY1X-ray3.94CS/DS1-110[»]
6C4Ielectron microscopy3.24T1-110[»]
6ENFelectron microscopy3.20S1-110[»]
6ENJelectron microscopy3.70S1-110[»]
6ENUelectron microscopy3.10S1-110[»]
6GBZelectron microscopy3.80S1-110[»]
6GC0electron microscopy3.80S1-110[»]
6GC4electron microscopy4.30S1-110[»]
6GC6electron microscopy4.30S1-110[»]
6GC7electron microscopy4.30S1-110[»]
6GC8electron microscopy3.80S1-110[»]
6GWTelectron microscopy3.80S1-110[»]
6GXMelectron microscopy3.80S1-110[»]
6GXNelectron microscopy3.90S1-110[»]
6GXOelectron microscopy3.90S1-110[»]
6GXPelectron microscopy4.40S1-110[»]
6H4Nelectron microscopy3.00S1-110[»]
6H58electron microscopy7.90S/SS1-110[»]
6HRMelectron microscopy2.96S1-110[»]
6I0Yelectron microscopy3.20S1-110[»]
6I7VX-ray2.90CT/DT1-110[»]
6O9Jelectron microscopy3.90S1-110[»]
6O9Kelectron microscopy4.00S1-110[»]
6OFXelectron microscopy3.30s1-110[»]
6OG7electron microscopy3.30s1-110[»]
6OREelectron microscopy2.90S1-110[»]
6ORLelectron microscopy3.50S1-110[»]
6OSTelectron microscopy4.20S1-110[»]
6OT3electron microscopy3.90S1-110[»]
6OUOelectron microscopy3.70S1-110[»]
6Q98electron microscopy4.30S1-110[»]
6Q9Aelectron microscopy3.70S1-109[»]
6QDWelectron microscopy2.83s1-110[»]
6QULelectron microscopy3.00T1-110[»]
6S0Kelectron microscopy3.10T1-110[»]
6SZSelectron microscopy3.06S1-110[»]
6TBVelectron microscopy2.70L2211-110[»]
6TC3electron microscopy2.70L2211-110[»]
6VWLelectron microscopy3.10Q1-110[»]
6VWMelectron microscopy3.40Q1-110[»]
6VWNelectron microscopy3.40Q1-110[»]
6WD6electron microscopy3.70s1-110[»]
6WDBelectron microscopy4.00s1-110[»]
6WDCelectron microscopy4.20s1-110[»]
6WDDelectron microscopy3.20s1-110[»]
6WDEelectron microscopy3.00s1-110[»]
6WDFelectron microscopy3.30s1-110[»]
6WDGelectron microscopy3.30s1-110[»]
6WDHelectron microscopy4.30s1-110[»]
6WDIelectron microscopy4.00s1-110[»]
6WDJelectron microscopy3.70s1-110[»]
6WDKelectron microscopy3.60s1-110[»]
6WDLelectron microscopy3.70s1-110[»]
6WDMelectron microscopy3.60s1-110[»]
6WNTelectron microscopy3.10s1-110[»]
6WNVelectron microscopy3.50s1-110[»]
6WNWelectron microscopy3.20s1-110[»]
6XZ7electron microscopy2.10S1-110[»]
6XZAelectron microscopy2.66S21-110[»]
6XZBelectron microscopy2.54S21-110[»]
6Y69electron microscopy2.86S1-110[»]
6YS3electron microscopy2.58s1-110[»]
6YSRelectron microscopy3.10S1-110[»]
6YSSelectron microscopy2.60S1-110[»]
6YSTelectron microscopy3.20S1-110[»]
6YSUelectron microscopy3.70S1-110[»]
6ZTJelectron microscopy3.40BT1-110[»]
6ZTLelectron microscopy3.50BT1-110[»]
6ZTMelectron microscopy3.30BT1-110[»]
6ZTNelectron microscopy3.90BT1-110[»]
6ZTOelectron microscopy3.00BT1-110[»]
6ZTPelectron microscopy3.00BT1-110[»]
6ZU1electron microscopy3.00BT1-110[»]
7ABZelectron microscopy3.21S1-110[»]
7AC7electron microscopy3.08S2-110[»]
7ACJelectron microscopy3.20S1-110[»]
7ACRelectron microscopy3.44S1-110[»]
7B5Kelectron microscopy2.90S1-110[»]
7BL2electron microscopy3.70S1-110[»]
7BL3electron microscopy3.50S1-110[»]
7BL4electron microscopy2.40S1-110[»]
7BL5electron microscopy3.30S1-110[»]
7BL6electron microscopy4.00S1-110[»]
7BV8electron microscopy3.14T1-110[»]
7D6Zelectron microscopy3.40S1-110[»]
7D80electron microscopy4.10r1-110[»]
7JSSelectron microscopy3.70s1-110[»]
7JSWelectron microscopy3.80s1-110[»]
7JSZelectron microscopy3.70s1-110[»]
7JT1electron microscopy3.30s1-110[»]
7JT2electron microscopy3.50s1-110[»]
7JT3electron microscopy3.70s1-110[»]
7K50electron microscopy3.40s1-110[»]
7K51electron microscopy3.50s1-110[»]
7K52electron microscopy3.40s1-110[»]
7K53electron microscopy3.20s1-110[»]
7K54electron microscopy3.20s1-110[»]
7K55electron microscopy3.30s1-110[»]
7LV0electron microscopy3.20s1-110[»]
7N1Pelectron microscopy2.33LV1-110[»]
7N2Celectron microscopy2.72LV1-110[»]
7N2Uelectron microscopy2.53LV1-110[»]
7N2Velectron microscopy2.54LV1-110[»]
7N30electron microscopy2.66LV1-110[»]
7N31electron microscopy2.69LV1-110[»]
7NSOelectron microscopy2.90S1-110[»]
7NSPelectron microscopy3.50S1-110[»]
7NSQelectron microscopy3.10S1-110[»]
7NWTelectron microscopy2.66S1-110[»]
7NWWelectron microscopy3.05R1-110[»]
7O19electron microscopy2.90BS1-110[»]
7O1Aelectron microscopy2.40BS1-110[»]
7O1Celectron microscopy2.60BS1-110[»]
7OIFelectron microscopy3.00R1-110[»]
7OIGelectron microscopy3.20R1-110[»]
7OIIelectron microscopy3.00R1-110[»]
7OIZelectron microscopy2.90r1-110[»]
7OJ0electron microscopy3.50r1-110[»]
7OT5electron microscopy2.90R1-110[»]
7P3Kelectron microscopy2.90r1-110[»]
7PJSelectron microscopy2.35S1-110[»]
7PJTelectron microscopy6.00S1-110[»]
7PJVelectron microscopy3.10S1-110[»]
7PJWelectron microscopy4.00S1-110[»]
7PJXelectron microscopy6.50S1-110[»]
7PJYelectron microscopy3.10S1-110[»]
7PJZelectron microscopy6.00S1-110[»]
AlphaFoldDBiP61175
SMRiP61175
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi852125, 1 interactor
ComplexPortaliCPX-3807, 50S large ribosomal subunit
DIPiDIP-35983N
IntActiP61175, 142 interactors
STRINGi511145.b3315

Proteomic databases

jPOSTiP61175
PaxDbiP61175
PRIDEiP61175

Genome annotation databases

EnsemblBacteriaiAAC76340; AAC76340; b3315
BAE77976; BAE77976; BAE77976
GeneIDi60373126
67415356
947813
KEGGiecj:JW3277
eco:b3315
PATRICifig|1411691.4.peg.3416

Organism-specific databases

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

More...EchoBASEi		EB0875

Phylogenomic databases

eggNOGiCOG0091, Bacteria
HOGENOMiCLU_083987_3_3_6
InParanoidiP61175
OMAiKRIQPRA
PhylomeDBiP61175

Enzyme and pathway databases

BioCyciEcoCyc:EG10882-MONOMER

Miscellaneous databases

EvolutionaryTraceiP61175

Protein Ontology

More...PROi		PR:P61175

Family and domain databases

CDDicd00336, Ribosomal_L22, 1 hit
Gene3Di3.90.470.10, 1 hit
HAMAPiMF_01331_B, Ribosomal_L22_B, 1 hit
InterProiView protein in InterPro
IPR001063, Ribosomal_L22
IPR018260, Ribosomal_L22/L17_CS
IPR036394, Ribosomal_L22/L17_sf
IPR005727, Ribosomal_L22_bac/chlpt-type
PANTHERiPTHR13501, PTHR13501, 1 hit
PfamiView protein in Pfam
PF00237, Ribosomal_L22, 1 hit
SUPFAMiSSF54843, SSF54843, 1 hit
TIGRFAMsiTIGR01044, rplV_bact, 1 hit
PROSITEiView protein in PROSITE
PS00464, RIBOSOMAL_L22, 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 nameiRL22_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: P61175
Secondary accession number(s): P02423, Q2M6Y0
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 25, 2022
This is version 176 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

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