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UniProtKB - P62399 (RL5_ECOLI)

Entry version 154 (08 May 2019)
Sequence version 2 (23 Jan 2007)
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Protein

50S ribosomal protein L5

Gene

rplE

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 is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. Its 5S rRNA binding is significantly enhanced in the presence of L18.3 Publications
In the 70S ribosome in the initiation state (PubMed:12809609) was modeled to contact protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; the protein-protein contacts between S13 and L5 in B1b change in the model with bound EF-G implicating this bridge in subunit movement (PubMed:12809609 and PubMed:18723842). In the two 3.5 A resolved ribosome structures (PubMed:16272117) the contacts between L5, S13 and S19 are different, confirming the dynamic nature of this interaction.3 Publications
Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.1 Publication

Miscellaneous

Identified as a multicopy suppressor of the slow growth phenotype of an rsgA (yjeQ) deletion mutant.1 Publication

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • 5S rRNA binding Source: EcoCyc
  • structural constituent of ribosome Source: GO_Central
  • tRNA binding Source: UniProtKB-UniRule
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • ribosomal large subunit assembly Source: EcoCyc
  • translation Source: UniProtKB-UniRule
View the complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding, tRNA-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:EG10868-MONOMER
ECOL316407:JW3270-MONOMER
MetaCyc:EG10868-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:
50S ribosomal protein L5
Alternative name(s):
Large ribosomal subunit protein uL51 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:rplE
Ordered Locus Names:b3308, JW3270
<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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<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		EG10868 rplE

<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

View the complete GO annotation on QuickGO ...

<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_00001249252 – 17950S ribosomal protein L5Add BLAST178

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 residuei3N6-acetyllysine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P62399

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P62399

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

More...PaxDbi		P62399

PRoteomics IDEntifications database

More...PRIDEi		P62399

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P62399

<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 50S ribosomal subunit (PubMed:791672, PubMed:12809609, PubMed:12859903, PubMed:16272117, PubMed:25310980, PubMed:24844575, PubMed:27934701, PubMed:27906160, PubMed:27906161); part of the 5S rRNA/L5/L18/L25 subcomplex (PubMed:354687, PubMed:8925931). Contacts the 5S rRNA; cross-links to the P site tRNA (PubMed:8925931). Forms a bridge to the 30S subunit in the 70S ribosome, contacting protein S13 and S19.13 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		852112, 1 interactor

ComplexPortal: manually curated resource of macromolecular complexes

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

Database of interacting proteins

More...DIPi		DIP-35914N

Protein interaction database and analysis system

More...IntActi		P62399, 74 interactors

STRING: functional protein association networks

More...STRINGi		511145.b3308

<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

1179
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
1ML5electron microscopy14.00g2-177[»]
2J28electron microscopy8.00F2-179[»]
2RDOelectron microscopy9.10F2-179[»]
3BBXelectron microscopy10.00F2-179[»]
3J5Lelectron microscopy6.60F2-178[»]
3J5Selectron microscopy7.50G2-179[»]
3J7Zelectron microscopy3.90F1-179[»]
3J8Gelectron microscopy5.00F1-179[»]
3J9Yelectron microscopy3.90F1-179[»]
3J9Zelectron microscopy3.60L72-179[»]
3JA1electron microscopy3.60LG2-179[»]
3JBUelectron microscopy3.64f1-179[»]
3JBVelectron microscopy3.32f1-179[»]
3JCDelectron microscopy3.70F1-179[»]
3JCEelectron microscopy3.20F1-179[»]
3JCJelectron microscopy3.70E1-179[»]
3JCNelectron microscopy4.60F1-179[»]
4CSUelectron microscopy5.50F2-179[»]
4U1UX-ray2.95BF/DF2-178[»]
4U1VX-ray3.00BF/DF2-178[»]
4U20X-ray2.90BF/DF2-178[»]
4U24X-ray2.90BF/DF2-178[»]
4U25X-ray2.90BF/DF2-178[»]
4U26X-ray2.80BF/DF2-178[»]
4U27X-ray2.80BF/DF2-178[»]
4UY8electron microscopy3.80F2-178[»]
4V47electron microscopy12.30AD2-179[»]
4V48electron microscopy11.50AD2-179[»]
4V4HX-ray3.46BF/DF1-179[»]
4V4QX-ray3.46BF/DF2-179[»]
4V4Velectron microscopy15.00BD3-179[»]
4V4Welectron microscopy15.00BD3-179[»]
4V50X-ray3.22BF/DF2-179[»]
4V52X-ray3.21BF/DF2-179[»]
4V53X-ray3.54BF/DF2-179[»]
4V54X-ray3.30BF/DF2-179[»]
4V55X-ray4.00BF/DF2-179[»]
4V56X-ray3.93BF/DF2-179[»]
4V57X-ray3.50BF/DF2-179[»]
4V5BX-ray3.74AF/CF2-179[»]
4V5Helectron microscopy5.80BF2-179[»]
4V5YX-ray4.45BF/DF2-179[»]
4V64X-ray3.50BF/DF2-179[»]
4V65electron microscopy9.00B22-179[»]
4V66electron microscopy9.00B22-179[»]
4V69electron microscopy6.70BF2-179[»]
4V6CX-ray3.19BF/DF1-179[»]
4V6DX-ray3.81BF/DF1-179[»]
4V6EX-ray3.71BF/DF1-179[»]
4V6Kelectron microscopy8.25AG1-179[»]
4V6Lelectron microscopy13.20BG1-179[»]
4V6Melectron microscopy7.10BF2-179[»]
4V6Nelectron microscopy12.10AG2-179[»]
4V6Oelectron microscopy14.70BG2-179[»]
4V6Pelectron microscopy13.50BG2-179[»]
4V6Qelectron microscopy11.50BG2-179[»]
4V6Relectron microscopy11.50BG2-179[»]
4V6Selectron microscopy13.10AG2-179[»]
4V6Telectron microscopy8.30BF2-178[»]
4V6Velectron microscopy9.80BG2-179[»]
4V6Yelectron microscopy12.00BF1-179[»]
4V6Zelectron microscopy12.00BF1-179[»]
4V70electron microscopy17.00BF1-179[»]
4V71electron microscopy20.00BF1-179[»]
4V72electron microscopy13.00BF1-179[»]
4V73electron microscopy15.00BF1-179[»]
4V74electron microscopy17.00BF1-179[»]
4V75electron microscopy12.00BF1-179[»]
4V76electron microscopy17.00BF1-179[»]
4V77electron microscopy17.00BF1-179[»]
4V78electron microscopy20.00BF1-179[»]
4V79electron microscopy15.00BF1-179[»]
4V7Aelectron microscopy9.00BF1-179[»]
4V7Belectron microscopy6.80BF1-179[»]
4V7Celectron microscopy7.60BG2-179[»]
4V7Delectron microscopy7.60AG2-179[»]
4V7Ielectron microscopy9.60AF1-179[»]
4V7SX-ray3.25BF2-178[»]
DF2-179[»]
4V7TX-ray3.19BF2-178[»]
DF2-179[»]
4V7UX-ray3.10BF/DF2-179[»]
4V7VX-ray3.29BF2-178[»]
DF2-179[»]
4V85X-ray3.20BF1-179[»]
4V89X-ray3.70BF1-179[»]
4V9CX-ray3.30BF/DF1-179[»]
4V9DX-ray3.00CF/DF2-178[»]
4V9OX-ray2.90AF/CF/EF/GF1-179[»]
4V9PX-ray2.90AF/CF/EF/GF1-179[»]
4WF1X-ray3.09BF/DF2-178[»]
4WOIX-ray3.00BF/CF1-179[»]
4WWWX-ray3.10RF/YF2-179[»]
4YBBX-ray2.10CF/DF2-178[»]
5ADYelectron microscopy4.50F1-179[»]
5AFIelectron microscopy2.90F1-179[»]
5AKAelectron microscopy5.70F2-179[»]
5GADelectron microscopy3.70F1-179[»]
5GAEelectron microscopy3.33F1-179[»]
5GAFelectron microscopy4.30F2-178[»]
5GAGelectron microscopy3.80F1-179[»]
5GAHelectron microscopy3.80F1-179[»]
5H5Uelectron microscopy3.00F2-179[»]
5IQRelectron microscopy3.00E1-179[»]
5IT8X-ray3.12CF/DF2-178[»]
5J5BX-ray2.80CF/DF2-178[»]
5J7LX-ray3.00CF/DF2-178[»]
5J88X-ray3.32CF/DF2-179[»]
5J8AX-ray3.10CF/DF2-179[»]
5J91X-ray2.96CF/DF2-179[»]
5JC9X-ray3.03CF/DF2-178[»]
5JTEelectron microscopy3.60BF1-179[»]
5JU8electron microscopy3.60BF1-179[»]
5KCRelectron microscopy3.601G1-179[»]
5KCSelectron microscopy3.901G1-179[»]
5KPSelectron microscopy3.90E1-179[»]
5KPVelectron microscopy4.10D1-179[»]
5KPWelectron microscopy3.90D1-179[»]
5KPXelectron microscopy3.90D1-179[»]
5L3Pelectron microscopy3.70G1-179[»]
5LZAelectron microscopy3.60F2-178[»]
5LZBelectron microscopy5.30F2-178[»]
5LZCelectron microscopy4.80F2-178[»]
5LZDelectron microscopy3.40F2-178[»]
5LZEelectron microscopy3.50F2-178[»]
5LZFelectron microscopy4.60F2-178[»]
5MDVelectron microscopy2.97E1-179[»]
5MDWelectron microscopy3.06E1-179[»]
5MDYelectron microscopy3.35E1-179[»]
5MDZelectron microscopy3.10E1-179[»]
5MGPelectron microscopy3.10F2-178[»]
5NCOelectron microscopy4.80F2-178[»]
5NP6electron microscopy3.60d2-178[»]
5NWYelectron microscopy2.93S1-179[»]
5O2Relectron microscopy3.40F2-178[»]
5U4Ielectron microscopy3.50F1-179[»]
5U9Felectron microscopy3.20071-179[»]
5U9Gelectron microscopy3.20071-179[»]
5UYKelectron microscopy3.90072-178[»]
5UYLelectron microscopy3.60072-178[»]
5UYMelectron microscopy3.20072-178[»]
5UYNelectron microscopy4.00072-178[»]
5UYPelectron microscopy3.90072-178[»]
5UYQelectron microscopy3.80072-178[»]
5WDTelectron microscopy3.00F2-178[»]
5WE4electron microscopy3.10F2-178[»]
5WE6electron microscopy3.40F2-178[»]
5WFKelectron microscopy3.40F2-178[»]
6BU8electron microscopy3.50072-178[»]
6BY1X-ray3.94CF/DF2-178[»]
6C4Ielectron microscopy3.24F2-178[»]
6ENFelectron microscopy3.20F2-178[»]
6ENJelectron microscopy3.70F2-178[»]
6ENUelectron microscopy3.10F2-178[»]
6GBZelectron microscopy3.80F2-178[»]
6GC0electron microscopy3.80F2-178[»]
6GC4electron microscopy4.30F2-178[»]
6GC8electron microscopy3.80F2-178[»]
6GWTelectron microscopy3.80F2-178[»]
6GXMelectron microscopy3.80F2-178[»]
6GXNelectron microscopy3.90F2-178[»]
6GXOelectron microscopy3.90F2-178[»]
6GXPelectron microscopy4.40F2-178[»]
6H4Nelectron microscopy3.00F2-178[»]
6H58electron microscopy7.90F/FF2-178[»]
6HRMelectron microscopy2.96E2-178[»]
6I0Yelectron microscopy3.20F2-178[»]
6I7VX-ray2.90CF/DF2-178[»]
6Q98electron microscopy4.30E1-179[»]

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

More...SMRi		P62399

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P62399

<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 uL5 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG4105CW6 Bacteria
COG0094 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000231311

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P62399

KEGG Orthology (KO)

More...KOi		K02931

Database for complete collections of gene phylogenies

More...PhylomeDBi		P62399

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.30.1440.10, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_01333_B Ribosomal_L5_B, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR002132 Ribosomal_L5
IPR020930 Ribosomal_L5_bac-type
IPR031309 Ribosomal_L5_C
IPR020929 Ribosomal_L5_CS
IPR022803 Ribosomal_L5_dom_sf
IPR031310 Ribosomal_L5_N

The PANTHER Classification System

More...PANTHERi		PTHR11994 PTHR11994, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00281 Ribosomal_L5, 1 hit
PF00673 Ribosomal_L5_C, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF002161 Ribosomal_L5, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF55282 SSF55282, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00358 RIBOSOMAL_L5, 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.

P62399-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAKLHDYYKD EVVKKLMTEF NYNSVMQVPR VEKITLNMGV GEAIADKKLL 
        60         70         80         90        100
DNAAADLAAI SGQKPLITKA RKSVAGFKIR QGYPIGCKVT LRGERMWEFF 
       110        120        130        140        150
ERLITIAVPR IRDFRGLSAK SFDGRGNYSM GVREQIIFPE IDYDKVDRVR 
       160        170 
GLDITITTTA KSDEEGRALL AAFDFPFRK
Length:179
Mass (Da):20,302
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:iB2E95A8BE4B8D2A7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti94E → Q AA sequence (PubMed:791672).Curated1
Sequence conflicti127N → D AA sequence (PubMed:791672).Curated1

<p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Molecular mass is 20169.8 Da from positions 2 - 179. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
X01563 Genomic DNA Translation: CAA25717.1
U18997 Genomic DNA Translation: AAA58105.1
U00096 Genomic DNA Translation: AAC76333.1
AP009048 Genomic DNA Translation: BAE77983.1
M10195 Genomic DNA Translation: AAA24051.1

Protein sequence database of the Protein Information Resource

More...PIRi		G65123 R5EC5

NCBI Reference Sequences

More...RefSeqi		NP_417767.1, NC_000913.3
WP_001096200.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC76333; AAC76333; b3308
BAE77983; BAE77983; BAE77983

Database of genes from NCBI RefSeq genomes

More...GeneIDi		23845560
947800

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW3270
eco:b3308

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.3423

<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
X01563 Genomic DNA Translation: CAA25717.1
U18997 Genomic DNA Translation: AAA58105.1
U00096 Genomic DNA Translation: AAC76333.1
AP009048 Genomic DNA Translation: BAE77983.1
M10195 Genomic DNA Translation: AAA24051.1
PIRiG65123 R5EC5
RefSeqiNP_417767.1, NC_000913.3
WP_001096200.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ML5electron microscopy14.00g2-177[»]
2J28electron microscopy8.00F2-179[»]
2RDOelectron microscopy9.10F2-179[»]
3BBXelectron microscopy10.00F2-179[»]
3J5Lelectron microscopy6.60F2-178[»]
3J5Selectron microscopy7.50G2-179[»]
3J7Zelectron microscopy3.90F1-179[»]
3J8Gelectron microscopy5.00F1-179[»]
3J9Yelectron microscopy3.90F1-179[»]
3J9Zelectron microscopy3.60L72-179[»]
3JA1electron microscopy3.60LG2-179[»]
3JBUelectron microscopy3.64f1-179[»]
3JBVelectron microscopy3.32f1-179[»]
3JCDelectron microscopy3.70F1-179[»]
3JCEelectron microscopy3.20F1-179[»]
3JCJelectron microscopy3.70E1-179[»]
3JCNelectron microscopy4.60F1-179[»]
4CSUelectron microscopy5.50F2-179[»]
4U1UX-ray2.95BF/DF2-178[»]
4U1VX-ray3.00BF/DF2-178[»]
4U20X-ray2.90BF/DF2-178[»]
4U24X-ray2.90BF/DF2-178[»]
4U25X-ray2.90BF/DF2-178[»]
4U26X-ray2.80BF/DF2-178[»]
4U27X-ray2.80BF/DF2-178[»]
4UY8electron microscopy3.80F2-178[»]
4V47electron microscopy12.30AD2-179[»]
4V48electron microscopy11.50AD2-179[»]
4V4HX-ray3.46BF/DF1-179[»]
4V4QX-ray3.46BF/DF2-179[»]
4V4Velectron microscopy15.00BD3-179[»]
4V4Welectron microscopy15.00BD3-179[»]
4V50X-ray3.22BF/DF2-179[»]
4V52X-ray3.21BF/DF2-179[»]
4V53X-ray3.54BF/DF2-179[»]
4V54X-ray3.30BF/DF2-179[»]
4V55X-ray4.00BF/DF2-179[»]
4V56X-ray3.93BF/DF2-179[»]
4V57X-ray3.50BF/DF2-179[»]
4V5BX-ray3.74AF/CF2-179[»]
4V5Helectron microscopy5.80BF2-179[»]
4V5YX-ray4.45BF/DF2-179[»]
4V64X-ray3.50BF/DF2-179[»]
4V65electron microscopy9.00B22-179[»]
4V66electron microscopy9.00B22-179[»]
4V69electron microscopy6.70BF2-179[»]
4V6CX-ray3.19BF/DF1-179[»]
4V6DX-ray3.81BF/DF1-179[»]
4V6EX-ray3.71BF/DF1-179[»]
4V6Kelectron microscopy8.25AG1-179[»]
4V6Lelectron microscopy13.20BG1-179[»]
4V6Melectron microscopy7.10BF2-179[»]
4V6Nelectron microscopy12.10AG2-179[»]
4V6Oelectron microscopy14.70BG2-179[»]
4V6Pelectron microscopy13.50BG2-179[»]
4V6Qelectron microscopy11.50BG2-179[»]
4V6Relectron microscopy11.50BG2-179[»]
4V6Selectron microscopy13.10AG2-179[»]
4V6Telectron microscopy8.30BF2-178[»]
4V6Velectron microscopy9.80BG2-179[»]
4V6Yelectron microscopy12.00BF1-179[»]
4V6Zelectron microscopy12.00BF1-179[»]
4V70electron microscopy17.00BF1-179[»]
4V71electron microscopy20.00BF1-179[»]
4V72electron microscopy13.00BF1-179[»]
4V73electron microscopy15.00BF1-179[»]
4V74electron microscopy17.00BF1-179[»]
4V75electron microscopy12.00BF1-179[»]
4V76electron microscopy17.00BF1-179[»]
4V77electron microscopy17.00BF1-179[»]
4V78electron microscopy20.00BF1-179[»]
4V79electron microscopy15.00BF1-179[»]
4V7Aelectron microscopy9.00BF1-179[»]
4V7Belectron microscopy6.80BF1-179[»]
4V7Celectron microscopy7.60BG2-179[»]
4V7Delectron microscopy7.60AG2-179[»]
4V7Ielectron microscopy9.60AF1-179[»]
4V7SX-ray3.25BF2-178[»]
DF2-179[»]
4V7TX-ray3.19BF2-178[»]
DF2-179[»]
4V7UX-ray3.10BF/DF2-179[»]
4V7VX-ray3.29BF2-178[»]
DF2-179[»]
4V85X-ray3.20BF1-179[»]
4V89X-ray3.70BF1-179[»]
4V9CX-ray3.30BF/DF1-179[»]
4V9DX-ray3.00CF/DF2-178[»]
4V9OX-ray2.90AF/CF/EF/GF1-179[»]
4V9PX-ray2.90AF/CF/EF/GF1-179[»]
4WF1X-ray3.09BF/DF2-178[»]
4WOIX-ray3.00BF/CF1-179[»]
4WWWX-ray3.10RF/YF2-179[»]
4YBBX-ray2.10CF/DF2-178[»]
5ADYelectron microscopy4.50F1-179[»]
5AFIelectron microscopy2.90F1-179[»]
5AKAelectron microscopy5.70F2-179[»]
5GADelectron microscopy3.70F1-179[»]
5GAEelectron microscopy3.33F1-179[»]
5GAFelectron microscopy4.30F2-178[»]
5GAGelectron microscopy3.80F1-179[»]
5GAHelectron microscopy3.80F1-179[»]
5H5Uelectron microscopy3.00F2-179[»]
5IQRelectron microscopy3.00E1-179[»]
5IT8X-ray3.12CF/DF2-178[»]
5J5BX-ray2.80CF/DF2-178[»]
5J7LX-ray3.00CF/DF2-178[»]
5J88X-ray3.32CF/DF2-179[»]
5J8AX-ray3.10CF/DF2-179[»]
5J91X-ray2.96CF/DF2-179[»]
5JC9X-ray3.03CF/DF2-178[»]
5JTEelectron microscopy3.60BF1-179[»]
5JU8electron microscopy3.60BF1-179[»]
5KCRelectron microscopy3.601G1-179[»]
5KCSelectron microscopy3.901G1-179[»]
5KPSelectron microscopy3.90E1-179[»]
5KPVelectron microscopy4.10D1-179[»]
5KPWelectron microscopy3.90D1-179[»]
5KPXelectron microscopy3.90D1-179[»]
5L3Pelectron microscopy3.70G1-179[»]
5LZAelectron microscopy3.60F2-178[»]
5LZBelectron microscopy5.30F2-178[»]
5LZCelectron microscopy4.80F2-178[»]
5LZDelectron microscopy3.40F2-178[»]
5LZEelectron microscopy3.50F2-178[»]
5LZFelectron microscopy4.60F2-178[»]
5MDVelectron microscopy2.97E1-179[»]
5MDWelectron microscopy3.06E1-179[»]
5MDYelectron microscopy3.35E1-179[»]
5MDZelectron microscopy3.10E1-179[»]
5MGPelectron microscopy3.10F2-178[»]
5NCOelectron microscopy4.80F2-178[»]
5NP6electron microscopy3.60d2-178[»]
5NWYelectron microscopy2.93S1-179[»]
5O2Relectron microscopy3.40F2-178[»]
5U4Ielectron microscopy3.50F1-179[»]
5U9Felectron microscopy3.20071-179[»]
5U9Gelectron microscopy3.20071-179[»]
5UYKelectron microscopy3.90072-178[»]
5UYLelectron microscopy3.60072-178[»]
5UYMelectron microscopy3.20072-178[»]
5UYNelectron microscopy4.00072-178[»]
5UYPelectron microscopy3.90072-178[»]
5UYQelectron microscopy3.80072-178[»]
5WDTelectron microscopy3.00F2-178[»]
5WE4electron microscopy3.10F2-178[»]
5WE6electron microscopy3.40F2-178[»]
5WFKelectron microscopy3.40F2-178[»]
6BU8electron microscopy3.50072-178[»]
6BY1X-ray3.94CF/DF2-178[»]
6C4Ielectron microscopy3.24F2-178[»]
6ENFelectron microscopy3.20F2-178[»]
6ENJelectron microscopy3.70F2-178[»]
6ENUelectron microscopy3.10F2-178[»]
6GBZelectron microscopy3.80F2-178[»]
6GC0electron microscopy3.80F2-178[»]
6GC4electron microscopy4.30F2-178[»]
6GC8electron microscopy3.80F2-178[»]
6GWTelectron microscopy3.80F2-178[»]
6GXMelectron microscopy3.80F2-178[»]
6GXNelectron microscopy3.90F2-178[»]
6GXOelectron microscopy3.90F2-178[»]
6GXPelectron microscopy4.40F2-178[»]
6H4Nelectron microscopy3.00F2-178[»]
6H58electron microscopy7.90F/FF2-178[»]
6HRMelectron microscopy2.96E2-178[»]
6I0Yelectron microscopy3.20F2-178[»]
6I7VX-ray2.90CF/DF2-178[»]
6Q98electron microscopy4.30E1-179[»]
SMRiP62399
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi852112, 1 interactor
ComplexPortaliCPX-3807 50S large ribosomal subunit
DIPiDIP-35914N
IntActiP62399, 74 interactors
STRINGi511145.b3308

PTM databases

iPTMnetiP62399

Proteomic databases

EPDiP62399
jPOSTiP62399
PaxDbiP62399
PRIDEiP62399

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76333; AAC76333; b3308
BAE77983; BAE77983; BAE77983
GeneIDi23845560
947800
KEGGiecj:JW3270
eco:b3308
PATRICifig|1411691.4.peg.3423

Organism-specific databases

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

More...EchoBASEi		EB0861
EcoGeneiEG10868 rplE

Phylogenomic databases

eggNOGiENOG4105CW6 Bacteria
COG0094 LUCA
HOGENOMiHOG000231311
InParanoidiP62399
KOiK02931
PhylomeDBiP62399

Enzyme and pathway databases

BioCyciEcoCyc:EG10868-MONOMER
ECOL316407:JW3270-MONOMER
MetaCyc:EG10868-MONOMER

Miscellaneous databases

EvolutionaryTraceiP62399

Protein Ontology

More...PROi		PR:P62399

Family and domain databases

Gene3Di3.30.1440.10, 1 hit
HAMAPiMF_01333_B Ribosomal_L5_B, 1 hit
InterProiView protein in InterPro
IPR002132 Ribosomal_L5
IPR020930 Ribosomal_L5_bac-type
IPR031309 Ribosomal_L5_C
IPR020929 Ribosomal_L5_CS
IPR022803 Ribosomal_L5_dom_sf
IPR031310 Ribosomal_L5_N
PANTHERiPTHR11994 PTHR11994, 1 hit
PfamiView protein in Pfam
PF00281 Ribosomal_L5, 1 hit
PF00673 Ribosomal_L5_C, 1 hit
PIRSFiPIRSF002161 Ribosomal_L5, 1 hit
SUPFAMiSSF55282 SSF55282, 1 hit
PROSITEiView protein in PROSITE
PS00358 RIBOSOMAL_L5, 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 nameiRL5_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: P62399
Secondary accession number(s): P02389, Q2M6X3
<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: May 8, 2019
This is version 154 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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