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Protein

30S ribosomal protein S1

Gene

rpsA

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

Required for translation of most natural mRNAs except for leaderless mRNA (PubMed:9677288, PubMed:7003157, PubMed:12068815, PubMed:17376482, PubMed:24339747). Binds mRNA upstream of the Shine-Dalgarno (SD) sequence and helps it bind to the 30S ribosomal subunit; acts as an RNA chaperone to unfold structured mRNA on the ribosome but is not essential for mRNAs with strong SDs and little 5'-UTR structure, thus it may help fine-tune which mRNAs that are translated (PubMed:24339747). Unwinds dsRNA by binding to transiently formed ssRNA regions; binds about 10 nucleotides (PubMed:22908248). Has a preference for polypyrimidine tracts (PubMed:778845). Negatively autoregulates its own translation (PubMed:2120211).10 Publications
It is not clear if it plays a role in trans-translation (a process which rescues stalled ribosomes). Evidence for its role; binds to tmRNA with very high affinity, is required for binding of tmRNA to 30S subunit (PubMed:11101533, PubMed:15340139). Thought to play a role only in translation of the tmRNA in vitro (PubMed:17392345). Evidence against its role; overexpression of whole protein or various S1 fragments inhibits translation, they have no effect on trans-translation, and an in vitro system with S1-less ribosomes performs trans-translation (PubMed:15340139, PubMed:17376482). In trans-translation Ala-aminoacylated transfer-messenger RNA (tmRNA, product of the ssrA gene; the 2 termini fold to resemble tRNA(Ala) while it encodes a short internal open reading frame (the tag peptide)) acts like a tRNA, entering the A-site of the ribosome and displacing the stalled mRNA (which is subsequently degraded). The ribosome then switches to translate the ORF on the tmRNA, the nascent peptide is terminated with the "tag peptide" encoded by the tmRNA and thus targeted for degradation.4 Publications
In case of infection by bacteriophage Qbeta, part of the viral RNA-dependent RNA polymerase complex; this subunit is required for RNA replication initiation activity during synthesis of (-) strand RNA from the (+) strand genomic RNA but not for (+) strand synthesis from the (-) strand (PubMed:6358207, PubMed:25122749). Binds an approximately 70 mucleotide RNA internal to the viral replicase gene (the M-site) (PubMed:25122749). Others have reported it is not involved in RNA replication initiation but rather in termination of RNA synthesis and is required for termination whether it is the (+) or (-) strand that is being synthesized (PubMed:23653193).4 Publications
In case of infection by bacteriophage T4, plays a significant role in substrate choice by viral endoribonuclease RegB.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

  • mRNA binding Source: EcoCyc
  • RNA binding Source: EcoCyc
  • structural constituent of ribosome Source: CAFA

GO - Biological processi

  • negative regulation of cytoplasmic translation Source: EcoCyc
  • ribosomal small subunit assembly Source: CAFA
  • translation Source: EcoCyc

<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 functionChaperone, Repressor, Ribonucleoprotein, Ribosomal protein, RNA-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG10900-MONOMER
MetaCyc:EG10900-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 S1
Alternative name(s):
Bacteriophage Q beta RNA-directed RNA polymerase subunit I1 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:rpsA
Synonyms:ssyF
Ordered Locus Names:b0911, JW0894
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

Escherichia coli strain K12 genome database

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EcoGenei
EG10900 rpsA

<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

Keywords - Cellular componenti

Cytoplasm

<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

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Essential, it cannot be deleted. Upon depletion cell growth and total protein synthesis become linear.1 Publication

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>Mutagenesisi205Y → A: Decreased binding of Q beta-derived M-site RNA, 80% synthesis of (-) strand RNA, in construct expressing residues 1-273. 1 Publication1
Mutagenesisi208F → A: Decreased binding of Q beta-derived M-site RNA, 50% synthesis of (-) strand RNA, in construct expressing residues 1-273. 1 Publication1
Mutagenesisi219H → A: Decreased binding of Q beta-derived M-site RNA, 40% synthesis of (-) strand RNA, in construct expressing residues 1-273. 1 Publication1
Mutagenesisi254R → A: Decreased binding of Q beta-derived M-site RNA, 40% synthesis of (-) strand RNA, in construct expressing residues 1-273. 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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001960331 – 55730S ribosomal protein S1Add BLAST557

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 residuei229N6-acetyllysine1 Publication1
Modified residuei279N6-acetyllysine1 Publication1
Modified residuei363N6-acetyllysine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated; probably on a serine.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P0AG67

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P0AG67

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

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PaxDbi
P0AG67

PRoteomics IDEntifications database

More...
PRIDEi
P0AG67

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

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SWISS-2DPAGEi
P0AG67

PTM databases

CarbonylDB database of protein carbonylation sites

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CarbonylDBi
P0AG67

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P0AG67

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Represses its own translation via the N-terminus (at protein level).1 Publication

<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; the largest protein subunit, it is loosely associated and rarely found in ribosomal crystal structures (PubMed:7041110, PubMed:7003157, PubMed:778845, PubMed:342903). Does not bind rRNA. Probably requires ribosomal protein S2 to associate with the 30S subunit (PubMed:12068815). Binds in the junction of the head, platform and main body of the 30S subunit; the N-terminus penetrates the 30S subunit while the C-terminus faces ribosomal protein S2 (PubMed:11593008). Nascent polypeptide chains cross-link this protein in situ (PubMed:9716382). Can be cross-linked to mRNA in the ribosome (PubMed:1712292). In case of infection by bacteriophage Qbeta, part of the viral RNA-dependent RNA polymerase complex, the other subunits are the viral replicase catalytic subunit (AC P14647), host EF-Tu and EF-Ts (PubMed:816798, PubMed:6358207, PubMed:25122749).11 Publications

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

WithEntry#Exp.IntActNotes
itself2EBI-546520,EBI-546520

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
4263060, 171 interactors
849910, 1 interactor

Database of interacting proteins

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DIPi
DIP-35884N

Protein interaction database and analysis system

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IntActi
P0AG67, 85 interactors

Molecular INTeraction database

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MINTi
P0AG67

STRING: functional protein association networks

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STRINGi
316385.ECDH10B_0981

<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

1557
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2BH8X-ray1.90A/B364-398[»]
2KHINMR-A267-361[»]
2KHJNMR-A441-528[»]
4Q7JX-ray2.90D/H1-273[»]
4R71X-ray3.21E/F2-171[»]
5XQ5NMR-A350-443[»]
6BU8electron microscopy3.50Z4-557[»]
6H4Nelectron microscopy3.00y1-557[»]
6H58electron microscopy7.90y/yy1-557[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P0AG67

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

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SMRi
P0AG67

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P0AG67

<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>Domaini21 – 87S1 motif 1PROSITE-ProRule annotationAdd BLAST67
Domaini105 – 171S1 motif 2PROSITE-ProRule annotationAdd BLAST67
Domaini192 – 260S1 motif 3PROSITE-ProRule annotationAdd BLAST69
Domaini277 – 347S1 motif 4PROSITE-ProRule annotationAdd BLAST71
Domaini364 – 434S1 motif 5PROSITE-ProRule annotationAdd BLAST71
Domaini451 – 520S1 motif 6PROSITE-ProRule annotationAdd BLAST70

<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 6 S1 motif domains are not equivalent; the first 2 no longer bind rRNA but instead are involved in protein-ribosome and protein-protein interactions. Binds to the 30S ribosomal subunit via its N-terminal fragment (190 residues, the first 2 S1 motifs) and allows translation by S1-free ribosomes (PubMed:7003157, PubMed:15340139). The same fragment represses its own translation (PubMed:2120211). The first 3 S1 motifs do however bind to mRNA pseudoknots in the 5'-UTR of at least 1 mRNA (rpsO); deletion of S1 motifs 1-3 but not motifs 4-6 is not viable, although a deletion of motifs 4-6 grows slowly and is cold-sensitive (PubMed:24339747). In case of infection by bacteriophage Qbeta the same N-terminal fragment is necessary and sufficient to form the Qbeta virus RNA-dependent RNA polymerase, although in vitro (-) strand RNA synthesis from the (+) strand genomic RNA also requires the third S1 motif (residues 1-273) (PubMed:6358207, PubMed:25122749). The third S1 motif is required to bind mRNA, tmRNA and viral M-site RNA but requires cooperation with other S1 motifs (PubMed:15340139, PubMed:25122749).6 Publications

<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

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105CAV Bacteria
COG0539 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000044052

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P0AG67

KEGG Orthology (KO)

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KOi
K02945

Database for complete collections of gene phylogenies

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PhylomeDBi
P0AG67

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR012340 NA-bd_OB-fold
IPR000110 Ribosomal_S1
IPR022967 S1_dom
IPR003029 S1_domain

Pfam protein domain database

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Pfami
View protein in Pfam
PF00575 S1, 6 hits

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF002111 RpsA, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00316 S1, 6 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF50249 SSF50249, 6 hits

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR00717 rpsA, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50126 S1, 6 hits

<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.

P0AG67-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTESFAQLFE ESLKEIETRP GSIVRGVVVA IDKDVVLVDA GLKSESAIPA
60 70 80 90 100
EQFKNAQGEL EIQVGDEVDV ALDAVEDGFG ETLLSREKAK RHEAWITLEK
110 120 130 140 150
AYEDAETVTG VINGKVKGGF TVELNGIRAF LPGSLVDVRP VRDTLHLEGK
160 170 180 190 200
ELEFKVIKLD QKRNNVVVSR RAVIESENSA ERDQLLENLQ EGMEVKGIVK
210 220 230 240 250
NLTDYGAFVD LGGVDGLLHI TDMAWKRVKH PSEIVNVGDE ITVKVLKFDR
260 270 280 290 300
ERTRVSLGLK QLGEDPWVAI AKRYPEGTKL TGRVTNLTDY GCFVEIEEGV
310 320 330 340 350
EGLVHVSEMD WTNKNIHPSK VVNVGDVVEV MVLDIDEERR RISLGLKQCK
360 370 380 390 400
ANPWQQFAET HNKGDRVEGK IKSITDFGIF IGLDGGIDGL VHLSDISWNV
410 420 430 440 450
AGEEAVREYK KGDEIAAVVL QVDAERERIS LGVKQLAEDP FNNWVALNKK
460 470 480 490 500
GAIVTGKVTA VDAKGATVEL ADGVEGYLRA SEASRDRVED ATLVLSVGDE
510 520 530 540 550
VEAKFTGVDR KNRAISLSVR AKDEADEKDA IATVNKQEDA NFSNNAMAEA

FKAAKGE
Length:557
Mass (Da):61,158
Last modified:December 20, 2005 - 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:i0ABCDEB9E510C267
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 conflicti125N → D AA sequence (PubMed:7041110).Curated1
Sequence conflicti181 – 182ER → D in CAA23630 (PubMed:7041110).Curated2
Sequence conflicti181 – 182ER → D in CAA23644 (PubMed:6281725).Curated2

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
V00342 Genomic DNA Translation: CAA23630.1
V00352 Genomic DNA Translation: CAA23644.1
U00096 Genomic DNA Translation: AAC73997.1
AP009048 Genomic DNA Translation: BAA35655.1
X00785 Genomic DNA Translation: CAA25361.1
X04864 Genomic DNA Translation: CAA28556.1

Protein sequence database of the Protein Information Resource

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PIRi
F64830 R3EC1

NCBI Reference Sequences

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RefSeqi
NP_415431.1, NC_000913.3
WP_000140327.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

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EnsemblBacteriai
AAC73997; AAC73997; b0911
BAA35655; BAA35655; BAA35655

Database of genes from NCBI RefSeq genomes

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GeneIDi
945536

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
ecj:JW0894
eco:b0911

Pathosystems Resource Integration Center (PATRIC)

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PATRICi
fig|1411691.4.peg.1365

<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
V00342 Genomic DNA Translation: CAA23630.1
V00352 Genomic DNA Translation: CAA23644.1
U00096 Genomic DNA Translation: AAC73997.1
AP009048 Genomic DNA Translation: BAA35655.1
X00785 Genomic DNA Translation: CAA25361.1
X04864 Genomic DNA Translation: CAA28556.1
PIRiF64830 R3EC1
RefSeqiNP_415431.1, NC_000913.3
WP_000140327.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2BH8X-ray1.90A/B364-398[»]
2KHINMR-A267-361[»]
2KHJNMR-A441-528[»]
4Q7JX-ray2.90D/H1-273[»]
4R71X-ray3.21E/F2-171[»]
5XQ5NMR-A350-443[»]
6BU8electron microscopy3.50Z4-557[»]
6H4Nelectron microscopy3.00y1-557[»]
6H58electron microscopy7.90y/yy1-557[»]
ProteinModelPortaliP0AG67
SMRiP0AG67
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263060, 171 interactors
849910, 1 interactor
DIPiDIP-35884N
IntActiP0AG67, 85 interactors
MINTiP0AG67
STRINGi316385.ECDH10B_0981

PTM databases

CarbonylDBiP0AG67
iPTMnetiP0AG67

2D gel databases

SWISS-2DPAGEiP0AG67

Proteomic databases

EPDiP0AG67
jPOSTiP0AG67
PaxDbiP0AG67
PRIDEiP0AG67

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73997; AAC73997; b0911
BAA35655; BAA35655; BAA35655
GeneIDi945536
KEGGiecj:JW0894
eco:b0911
PATRICifig|1411691.4.peg.1365

Organism-specific databases

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

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EchoBASEi
EB0893
EcoGeneiEG10900 rpsA

Phylogenomic databases

eggNOGiENOG4105CAV Bacteria
COG0539 LUCA
HOGENOMiHOG000044052
InParanoidiP0AG67
KOiK02945
PhylomeDBiP0AG67

Enzyme and pathway databases

BioCyciEcoCyc:EG10900-MONOMER
MetaCyc:EG10900-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0AG67

Protein Ontology

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PROi
PR:P0AG67

Family and domain databases

InterProiView protein in InterPro
IPR012340 NA-bd_OB-fold
IPR000110 Ribosomal_S1
IPR022967 S1_dom
IPR003029 S1_domain
PfamiView protein in Pfam
PF00575 S1, 6 hits
PIRSFiPIRSF002111 RpsA, 1 hit
SMARTiView protein in SMART
SM00316 S1, 6 hits
SUPFAMiSSF50249 SSF50249, 6 hits
TIGRFAMsiTIGR00717 rpsA, 1 hit
PROSITEiView protein in PROSITE
PS50126 S1, 6 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<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 nameiRS1_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: P0AG67
Secondary accession number(s): P02349, P77352
<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: December 20, 2005
Last modified: January 16, 2019
This is version 119 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, 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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