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UniProtKB - P0A7W1 (RS5_ECOLI)

Protein

30S ribosomal protein S5

Gene

rpsE

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 S12 plays an important role in translational accuracy. Many suppressors of streptomycin-dependent mutants of protein S12 are found in this protein, some but not all of which decrease translational accuracy (ram, ribosomal ambiguity mutations).1 Publication
Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body.1 Publication
The physical location of this protein suggests it may also play a role in mRNA unwinding by the ribosome, possibly by forming part of a processivity clamp.1 Publication

Miscellaneous

Altered S5 proteins have been identified in a number of mutants. Some mutations in S5 have been shown to increase translational error frequencies.
Some mutants in this protein can partially suppress an alanyl-tRNA synthetase mutant.

<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

  • rRNA binding Source: UniProtKB-UniRule
  • structural constituent of ribosome Source: CAFA
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • maintenance of translational fidelity Source: EcoCyc
  • response to antibiotic Source: UniProtKB-KW
  • ribosomal small subunit assembly Source: CAFA
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
Biological processAntibiotic resistance

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:EG10904-MONOMER
MetaCyc:EG10904-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 S5
Alternative name(s):
Small ribosomal subunit protein uS51 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:rpsE
Synonyms:spc
Ordered Locus Names:b3303, JW3265
<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		EG10904 rpsE

<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 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>Mutagenesisi20 – 29RVSKTVKGGR → AVSKTVKGGA: No effect on mRNA unwinding ability of the ribosome. 1 Publication10

<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_00001315112 – 16730S ribosomal protein S5Add BLAST166

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 residuei2N-acetylalanine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P0A7W1

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P0A7W1

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

More...PaxDbi		P0A7W1

PRoteomics IDEntifications database

More...PRIDEi		P0A7W1

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P0A7W1

<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:363452, PubMed:4273819, PubMed:12809609, PubMed:16272117, PubMed:27934701, PubMed:10094780, PubMed:12244297, PubMed:27906160, PubMed:27906161, PubMed:28077875). Contacts proteins S4 and S8. With proteins S4 and S5 encircles the mRNA as it enters the ribosome, which may play a role in mRNA helicase processivity (PubMed:15652481). Can be cross-linked to mRNA (PubMed:1712292).12 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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		4263408, 155 interactors

Database of interacting proteins

More...DIPi		DIP-10781N

Protein interaction database and analysis system

More...IntActi		P0A7W1, 193 interactors

Molecular INTeraction database

More...MINTi		P0A7W1

STRING: functional protein association networks

More...STRINGi		316385.ECDH10B_3478

<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

1167
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
1EG0electron microscopy11.50B1-148[»]
1M5Gmodel-E10-159[»]
2YKRelectron microscopy9.80E10-159[»]
3J9Yelectron microscopy3.90e1-167[»]
3J9Zelectron microscopy3.60SE2-167[»]
3JA1electron microscopy3.60SE2-167[»]
3JBUelectron microscopy3.64E1-167[»]
3JBVelectron microscopy3.32E1-167[»]
3JCDelectron microscopy3.70e1-167[»]
3JCEelectron microscopy3.20e1-167[»]
3JCJelectron microscopy3.70k1-167[»]
3JCNelectron microscopy4.60f1-159[»]
4A2Ielectron microscopy16.50E10-159[»]
4ADVelectron microscopy13.50E2-167[»]
4U1UX-ray2.95AE/CE10-159[»]
4U1VX-ray3.00AE/CE10-159[»]
4U20X-ray2.90AE/CE10-159[»]
4U24X-ray2.90AE/CE10-159[»]
4U25X-ray2.90AE/CE10-159[»]
4U26X-ray2.80AE/CE10-159[»]
4U27X-ray2.80AE/CE10-159[»]
4V47electron microscopy12.30BE2-167[»]
4V48electron microscopy11.50BE2-167[»]
4V4HX-ray3.46AE/CE1-167[»]
4V4QX-ray3.46AE/CE2-167[»]
4V4Velectron microscopy15.00AE10-157[»]
4V4Welectron microscopy15.00AE10-157[»]
4V50X-ray3.22AE/CE2-167[»]
4V52X-ray3.21AE/CE2-167[»]
4V53X-ray3.54AE/CE2-167[»]
4V54X-ray3.30AE/CE2-167[»]
4V55X-ray4.00AE/CE2-167[»]
4V56X-ray3.93AE/CE2-167[»]
4V57X-ray3.50AE/CE2-167[»]
4V5BX-ray3.74BE/DE2-167[»]
4V5Helectron microscopy5.80AE10-159[»]
4V5YX-ray4.45AE/CE2-167[»]
4V64X-ray3.50AE/CE2-167[»]
4V65electron microscopy9.00AS1-159[»]
4V66electron microscopy9.00AS1-159[»]
4V69electron microscopy6.70AE10-159[»]
4V6CX-ray3.19AE/CE1-167[»]
4V6DX-ray3.81AE/CE1-167[»]
4V6EX-ray3.71AE/CE1-167[»]
4V6Kelectron microscopy8.25BI1-167[»]
4V6Lelectron microscopy13.20AI1-167[»]
4V6Melectron microscopy7.10AE2-167[»]
4V6Nelectron microscopy12.10BH2-167[»]
4V6Oelectron microscopy14.70AH2-167[»]
4V6Pelectron microscopy13.50AH2-167[»]
4V6Qelectron microscopy11.50AH2-167[»]
4V6Relectron microscopy11.50AH2-167[»]
4V6Selectron microscopy13.10BG2-167[»]
4V6Telectron microscopy8.30AE10-159[»]
4V6Velectron microscopy9.80AE2-167[»]
4V6Yelectron microscopy12.00AE10-159[»]
4V6Zelectron microscopy12.00AE10-159[»]
4V70electron microscopy17.00AE10-159[»]
4V71electron microscopy20.00AE10-159[»]
4V72electron microscopy13.00AE10-159[»]
4V73electron microscopy15.00AE10-159[»]
4V74electron microscopy17.00AE10-159[»]
4V75electron microscopy12.00AE10-159[»]
4V76electron microscopy17.00AE10-159[»]
4V77electron microscopy17.00AE10-159[»]
4V78electron microscopy20.00AE10-159[»]
4V79electron microscopy15.00AE10-159[»]
4V7Aelectron microscopy9.00AE10-159[»]
4V7Belectron microscopy6.80AE1-167[»]
4V7Celectron microscopy7.60AE2-167[»]
4V7Delectron microscopy7.60BE2-167[»]
4V7Ielectron microscopy9.60BE1-167[»]
4V7SX-ray3.25AE/CE10-159[»]
4V7TX-ray3.19AE/CE10-159[»]
4V7UX-ray3.10AE/CE10-159[»]
4V7VX-ray3.29AE/CE10-159[»]
4V85X-ray3.20E1-167[»]
4V89X-ray3.70AE1-167[»]
4V9CX-ray3.30AE/CE1-167[»]
4V9DX-ray3.00AE/BE10-159[»]
4V9OX-ray2.90BE/DE/FE/HE1-167[»]
4V9PX-ray2.90BE/DE/FE/HE1-167[»]
4WF1X-ray3.09AE/CE10-159[»]
4WOIX-ray3.00AE/DE1-167[»]
4WWWX-ray3.10QE/XE10-159[»]
4YBBX-ray2.10AE/BE10-164[»]
5AFIelectron microscopy2.90e1-167[»]
5H5Uelectron microscopy3.00l2-167[»]
5IQRelectron microscopy3.00j1-167[»]
5IT8X-ray3.12AE/BE10-164[»]
5J5BX-ray2.80AE/BE10-164[»]
5J7LX-ray3.00AE/BE10-164[»]
5J88X-ray3.32AE/BE10-164[»]
5J8AX-ray3.10AE/BE10-164[»]
5J91X-ray2.96AE/BE10-164[»]
5JC9X-ray3.03AE/BE10-164[»]
5JTEelectron microscopy3.60AE1-167[»]
5JU8electron microscopy3.60AE1-167[»]
5KCRelectron microscopy3.601e1-167[»]
5KCSelectron microscopy3.901e1-167[»]
5KPSelectron microscopy3.90101-167[»]
5KPVelectron microscopy4.1091-167[»]
5KPWelectron microscopy3.9091-167[»]
5KPXelectron microscopy3.9091-167[»]
5L3Pelectron microscopy3.70e1-167[»]
5LZAelectron microscopy3.60e10-166[»]
5LZBelectron microscopy5.30e10-166[»]
5LZCelectron microscopy4.80e10-166[»]
5LZDelectron microscopy3.40e10-166[»]
5LZEelectron microscopy3.50e10-166[»]
5LZFelectron microscopy4.60e10-166[»]
5MDVelectron microscopy2.97j1-167[»]
5MDWelectron microscopy3.06j1-167[»]
5MDYelectron microscopy3.35j1-167[»]
5MDZelectron microscopy3.10j1-167[»]
5ME0electron microscopy13.50E1-167[»]
5ME1electron microscopy13.50E1-167[»]
5MGPelectron microscopy3.10e10-166[»]
5MY1electron microscopy7.60E2-167[»]
5NO2electron microscopy5.16E10-164[»]
5NO3electron microscopy5.16E10-164[»]
5NO4electron microscopy5.16E10-164[»]
5NP6electron microscopy3.60H10-166[»]
5NWYelectron microscopy2.9341-166[»]
5O2Relectron microscopy3.40e10-166[»]
5U4Ielectron microscopy3.50e1-167[»]
5U4Jelectron microscopy3.70e1-167[»]
5U9Felectron microscopy3.20E1-167[»]
5U9Gelectron microscopy3.20E1-167[»]
5UYKelectron microscopy3.90E10-166[»]
5UYLelectron microscopy3.60E10-166[»]
5UYMelectron microscopy3.20E10-166[»]
5UYNelectron microscopy4.00E10-166[»]
5UYPelectron microscopy3.90E10-166[»]
5UYQelectron microscopy3.80E10-166[»]
5UZ4electron microscopy5.80E1-167[»]
5WDTelectron microscopy3.00e10-166[»]
5WE4electron microscopy3.10e10-166[»]
5WE6electron microscopy3.40e10-166[»]
5WFKelectron microscopy3.40e10-166[»]
6BU8electron microscopy3.50E10-166[»]
6C4Ielectron microscopy3.24e1-167[»]
6DNCelectron microscopy3.70RA1-167[»]
6ENFelectron microscopy3.20e10-166[»]
6ENJelectron microscopy3.70e10-166[»]
6ENUelectron microscopy3.10e10-166[»]
6GWTelectron microscopy3.80e10-166[»]
6GXMelectron microscopy3.80e10-166[»]
6GXNelectron microscopy3.90e10-166[»]
6GXOelectron microscopy3.90e10-166[»]
6GXPelectron microscopy4.40e10-166[»]
6H4Nelectron microscopy3.00e10-166[»]
6H58electron microscopy7.90e/ee10-166[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P0A7W1

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

More...SMRi		P0A7W1

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		P0A7W1

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini11 – 74S5 DRBMAdd BLAST64

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The N-terminal domain interacts with the head of the 30S subunit; the C-terminal domain interacts with the body and contacts protein S4. The interaction surface between S4 and S5 is involved in control of translational fidelity.

<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 uS5 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG0098 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000072595

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P0A7W1

KEGG Orthology (KO)

More...KOi		K02988

Database for complete collections of gene phylogenies

More...PhylomeDBi		P0A7W1

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.30.230.10, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_01307_B Ribosomal_S5_B, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR000851 Ribosomal_S5
IPR005712 Ribosomal_S5_bac-type
IPR005324 Ribosomal_S5_C
IPR020568 Ribosomal_S5_D2-typ_fold
IPR014721 Ribosomal_S5_D2-typ_fold_subgr
IPR013810 Ribosomal_S5_N
IPR018192 Ribosomal_S5_N_CS

The PANTHER Classification System

More...PANTHERi		PTHR13718 PTHR13718, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00333 Ribosomal_S5, 1 hit
PF03719 Ribosomal_S5_C, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF54211 SSF54211, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR01021 rpsE_bact, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00585 RIBOSOMAL_S5, 1 hit
PS50881 S5_DSRBD, 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.

P0A7W1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAHIEKQAGE LQEKLIAVNR VSKTVKGGRI FSFTALTVVG DGNGRVGFGY 
        60         70         80         90        100
GKAREVPAAI QKAMEKARRN MINVALNNGT LQHPVKGVHT GSRVFMQPAS 
       110        120        130        140        150
EGTGIIAGGA MRAVLEVAGV HNVLAKAYGS TNPINVVRAT IDGLENMNSP 
       160 
EMVAAKRGKS VEEILGK
Length:167
Mass (Da):17,603
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:i0B7EA2CB34018CAB
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 17514.8 Da from positions 2 - 167. 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 varianti20R → L in strain: SPCR9; spectinomycin resistant. Not a ram mutation. 1
Natural varianti21V → E in strain: SPCR7; spectinomycin resistant. Not a ram mutation. 1
Natural varianti22S → P in strain: SPCR13 and SPCR15; spectinomycin resistant. Not a ram mutation. 1
Natural varianti104G → R in strain: N-660; suppresses S12 streptomycin dependence. 1
Natural varianti112R → G in strain: NEA-314; neamycin resistant. 1
Natural varianti112R → L in strain: N-421 and D-1023; suppresses S12 streptomycin-dependence. 1
Natural varianti112R → S in strain: NEA-319; neamycin resistant. 1
Natural varianti151E → S in strain: B. 1
Natural varianti162 – 167EEILGK → G in strain: 0-1; suppresses an alanyl-tRNA synthetase mutation. Blocks ribosome assembly below 25 degrees Celsius. 6

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: CAA25722.1
U18997 Genomic DNA Translation: AAA58100.1
U00096 Genomic DNA Translation: AAC76328.1
AP009048 Genomic DNA Translation: BAE77988.1

Protein sequence database of the Protein Information Resource

More...PIRi		B65123 R3EC5

NCBI Reference Sequences

More...RefSeqi		NP_417762.1, NC_000913.3
WP_000940121.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC76328; AAC76328; b3303
BAE77988; BAE77988; BAE77988

Database of genes from NCBI RefSeq genomes

More...GeneIDi		947795

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW3265
eco:b3303

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.3428

<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: CAA25722.1
U18997 Genomic DNA Translation: AAA58100.1
U00096 Genomic DNA Translation: AAC76328.1
AP009048 Genomic DNA Translation: BAE77988.1
PIRiB65123 R3EC5
RefSeqiNP_417762.1, NC_000913.3
WP_000940121.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EG0electron microscopy11.50B1-148[»]
1M5Gmodel-E10-159[»]
2YKRelectron microscopy9.80E10-159[»]
3J9Yelectron microscopy3.90e1-167[»]
3J9Zelectron microscopy3.60SE2-167[»]
3JA1electron microscopy3.60SE2-167[»]
3JBUelectron microscopy3.64E1-167[»]
3JBVelectron microscopy3.32E1-167[»]
3JCDelectron microscopy3.70e1-167[»]
3JCEelectron microscopy3.20e1-167[»]
3JCJelectron microscopy3.70k1-167[»]
3JCNelectron microscopy4.60f1-159[»]
4A2Ielectron microscopy16.50E10-159[»]
4ADVelectron microscopy13.50E2-167[»]
4U1UX-ray2.95AE/CE10-159[»]
4U1VX-ray3.00AE/CE10-159[»]
4U20X-ray2.90AE/CE10-159[»]
4U24X-ray2.90AE/CE10-159[»]
4U25X-ray2.90AE/CE10-159[»]
4U26X-ray2.80AE/CE10-159[»]
4U27X-ray2.80AE/CE10-159[»]
4V47electron microscopy12.30BE2-167[»]
4V48electron microscopy11.50BE2-167[»]
4V4HX-ray3.46AE/CE1-167[»]
4V4QX-ray3.46AE/CE2-167[»]
4V4Velectron microscopy15.00AE10-157[»]
4V4Welectron microscopy15.00AE10-157[»]
4V50X-ray3.22AE/CE2-167[»]
4V52X-ray3.21AE/CE2-167[»]
4V53X-ray3.54AE/CE2-167[»]
4V54X-ray3.30AE/CE2-167[»]
4V55X-ray4.00AE/CE2-167[»]
4V56X-ray3.93AE/CE2-167[»]
4V57X-ray3.50AE/CE2-167[»]
4V5BX-ray3.74BE/DE2-167[»]
4V5Helectron microscopy5.80AE10-159[»]
4V5YX-ray4.45AE/CE2-167[»]
4V64X-ray3.50AE/CE2-167[»]
4V65electron microscopy9.00AS1-159[»]
4V66electron microscopy9.00AS1-159[»]
4V69electron microscopy6.70AE10-159[»]
4V6CX-ray3.19AE/CE1-167[»]
4V6DX-ray3.81AE/CE1-167[»]
4V6EX-ray3.71AE/CE1-167[»]
4V6Kelectron microscopy8.25BI1-167[»]
4V6Lelectron microscopy13.20AI1-167[»]
4V6Melectron microscopy7.10AE2-167[»]
4V6Nelectron microscopy12.10BH2-167[»]
4V6Oelectron microscopy14.70AH2-167[»]
4V6Pelectron microscopy13.50AH2-167[»]
4V6Qelectron microscopy11.50AH2-167[»]
4V6Relectron microscopy11.50AH2-167[»]
4V6Selectron microscopy13.10BG2-167[»]
4V6Telectron microscopy8.30AE10-159[»]
4V6Velectron microscopy9.80AE2-167[»]
4V6Yelectron microscopy12.00AE10-159[»]
4V6Zelectron microscopy12.00AE10-159[»]
4V70electron microscopy17.00AE10-159[»]
4V71electron microscopy20.00AE10-159[»]
4V72electron microscopy13.00AE10-159[»]
4V73electron microscopy15.00AE10-159[»]
4V74electron microscopy17.00AE10-159[»]
4V75electron microscopy12.00AE10-159[»]
4V76electron microscopy17.00AE10-159[»]
4V77electron microscopy17.00AE10-159[»]
4V78electron microscopy20.00AE10-159[»]
4V79electron microscopy15.00AE10-159[»]
4V7Aelectron microscopy9.00AE10-159[»]
4V7Belectron microscopy6.80AE1-167[»]
4V7Celectron microscopy7.60AE2-167[»]
4V7Delectron microscopy7.60BE2-167[»]
4V7Ielectron microscopy9.60BE1-167[»]
4V7SX-ray3.25AE/CE10-159[»]
4V7TX-ray3.19AE/CE10-159[»]
4V7UX-ray3.10AE/CE10-159[»]
4V7VX-ray3.29AE/CE10-159[»]
4V85X-ray3.20E1-167[»]
4V89X-ray3.70AE1-167[»]
4V9CX-ray3.30AE/CE1-167[»]
4V9DX-ray3.00AE/BE10-159[»]
4V9OX-ray2.90BE/DE/FE/HE1-167[»]
4V9PX-ray2.90BE/DE/FE/HE1-167[»]
4WF1X-ray3.09AE/CE10-159[»]
4WOIX-ray3.00AE/DE1-167[»]
4WWWX-ray3.10QE/XE10-159[»]
4YBBX-ray2.10AE/BE10-164[»]
5AFIelectron microscopy2.90e1-167[»]
5H5Uelectron microscopy3.00l2-167[»]
5IQRelectron microscopy3.00j1-167[»]
5IT8X-ray3.12AE/BE10-164[»]
5J5BX-ray2.80AE/BE10-164[»]
5J7LX-ray3.00AE/BE10-164[»]
5J88X-ray3.32AE/BE10-164[»]
5J8AX-ray3.10AE/BE10-164[»]
5J91X-ray2.96AE/BE10-164[»]
5JC9X-ray3.03AE/BE10-164[»]
5JTEelectron microscopy3.60AE1-167[»]
5JU8electron microscopy3.60AE1-167[»]
5KCRelectron microscopy3.601e1-167[»]
5KCSelectron microscopy3.901e1-167[»]
5KPSelectron microscopy3.90101-167[»]
5KPVelectron microscopy4.1091-167[»]
5KPWelectron microscopy3.9091-167[»]
5KPXelectron microscopy3.9091-167[»]
5L3Pelectron microscopy3.70e1-167[»]
5LZAelectron microscopy3.60e10-166[»]
5LZBelectron microscopy5.30e10-166[»]
5LZCelectron microscopy4.80e10-166[»]
5LZDelectron microscopy3.40e10-166[»]
5LZEelectron microscopy3.50e10-166[»]
5LZFelectron microscopy4.60e10-166[»]
5MDVelectron microscopy2.97j1-167[»]
5MDWelectron microscopy3.06j1-167[»]
5MDYelectron microscopy3.35j1-167[»]
5MDZelectron microscopy3.10j1-167[»]
5ME0electron microscopy13.50E1-167[»]
5ME1electron microscopy13.50E1-167[»]
5MGPelectron microscopy3.10e10-166[»]
5MY1electron microscopy7.60E2-167[»]
5NO2electron microscopy5.16E10-164[»]
5NO3electron microscopy5.16E10-164[»]
5NO4electron microscopy5.16E10-164[»]
5NP6electron microscopy3.60H10-166[»]
5NWYelectron microscopy2.9341-166[»]
5O2Relectron microscopy3.40e10-166[»]
5U4Ielectron microscopy3.50e1-167[»]
5U4Jelectron microscopy3.70e1-167[»]
5U9Felectron microscopy3.20E1-167[»]
5U9Gelectron microscopy3.20E1-167[»]
5UYKelectron microscopy3.90E10-166[»]
5UYLelectron microscopy3.60E10-166[»]
5UYMelectron microscopy3.20E10-166[»]
5UYNelectron microscopy4.00E10-166[»]
5UYPelectron microscopy3.90E10-166[»]
5UYQelectron microscopy3.80E10-166[»]
5UZ4electron microscopy5.80E1-167[»]
5WDTelectron microscopy3.00e10-166[»]
5WE4electron microscopy3.10e10-166[»]
5WE6electron microscopy3.40e10-166[»]
5WFKelectron microscopy3.40e10-166[»]
6BU8electron microscopy3.50E10-166[»]
6C4Ielectron microscopy3.24e1-167[»]
6DNCelectron microscopy3.70RA1-167[»]
6ENFelectron microscopy3.20e10-166[»]
6ENJelectron microscopy3.70e10-166[»]
6ENUelectron microscopy3.10e10-166[»]
6GWTelectron microscopy3.80e10-166[»]
6GXMelectron microscopy3.80e10-166[»]
6GXNelectron microscopy3.90e10-166[»]
6GXOelectron microscopy3.90e10-166[»]
6GXPelectron microscopy4.40e10-166[»]
6H4Nelectron microscopy3.00e10-166[»]
6H58electron microscopy7.90e/ee10-166[»]
ProteinModelPortaliP0A7W1
SMRiP0A7W1
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263408, 155 interactors
DIPiDIP-10781N
IntActiP0A7W1, 193 interactors
MINTiP0A7W1
STRINGi316385.ECDH10B_3478

PTM databases

iPTMnetiP0A7W1

Proteomic databases

EPDiP0A7W1
jPOSTiP0A7W1
PaxDbiP0A7W1
PRIDEiP0A7W1

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76328; AAC76328; b3303
BAE77988; BAE77988; BAE77988
GeneIDi947795
KEGGiecj:JW3265
eco:b3303
PATRICifig|1411691.4.peg.3428

Organism-specific databases

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

More...EchoBASEi		EB0897
EcoGeneiEG10904 rpsE

Phylogenomic databases

eggNOGiCOG0098 LUCA
HOGENOMiHOG000072595
InParanoidiP0A7W1
KOiK02988
PhylomeDBiP0A7W1

Enzyme and pathway databases

BioCyciEcoCyc:EG10904-MONOMER
MetaCyc:EG10904-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0A7W1

Protein Ontology

More...PROi		PR:P0A7W1

Family and domain databases

Gene3Di3.30.230.10, 1 hit
HAMAPiMF_01307_B Ribosomal_S5_B, 1 hit
InterProiView protein in InterPro
IPR000851 Ribosomal_S5
IPR005712 Ribosomal_S5_bac-type
IPR005324 Ribosomal_S5_C
IPR020568 Ribosomal_S5_D2-typ_fold
IPR014721 Ribosomal_S5_D2-typ_fold_subgr
IPR013810 Ribosomal_S5_N
IPR018192 Ribosomal_S5_N_CS
PANTHERiPTHR13718 PTHR13718, 1 hit
PfamiView protein in Pfam
PF00333 Ribosomal_S5, 1 hit
PF03719 Ribosomal_S5_C, 1 hit
SUPFAMiSSF54211 SSF54211, 1 hit
TIGRFAMsiTIGR01021 rpsE_bact, 1 hit
PROSITEiView protein in PROSITE
PS00585 RIBOSOMAL_S5, 1 hit
PS50881 S5_DSRBD, 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 nameiRS5_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: P0A7W1
Secondary accession number(s): O54299, P02356, Q2M6W8
<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: January 16, 2019
This is version 145 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. Ribosomal proteins
    Ribosomal proteins families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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