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Protein

30S ribosomal protein S9

Gene

rpsI

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

The C-terminal tail plays a role in the affinity of the 30S P site for different tRNAs. Mutations that decrease this affinity are suppressed in the 70S ribosome.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

  • RNA binding Source: GO_Central
  • structural constituent of ribosome Source: CAFA
  • tRNA binding Source: UniProtKB-KW

GO - Biological processi

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

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

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG10908-MONOMER
MetaCyc:EG10908-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 S9
Alternative name(s):
Small ribosomal subunit protein uS91 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:rpsI
Ordered Locus Names:b3230, JW3199
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

Escherichia coli strain K12 genome database

More...
EcoGenei
EG10908 rpsI

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi105 – 130Missing : Cold sensitive for growth at 30 degrees Celsius. 350-fold reduced affinity of the 30S subunit P site for certain tRNAs in vitro. 1 PublicationAdd BLAST26
Mutagenesisi128 – 130Missing : Very cold sensitive for growth at 30 degrees Celsius. Almost no P site binding of certain tRNAs in vitro. 1 Publication3

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB00453 Clomocycline
DB00618 Demeclocycline
DB00254 Doxycycline
DB00256 Lymecycline
DB01017 Minocycline
DB00595 Oxytetracycline
DB01301 Rolitetracycline
DB00560 Tigecycline

<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_00001113542 – 13030S ribosomal protein S9Add BLAST129

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P0A7X3

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0A7X3

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

More...
PaxDbi
P0A7X3

PRoteomics IDEntifications database

More...
PRIDEi
P0A7X3

<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:1091515, PubMed:7556101, PubMed:10094780, PubMed:12809609, PubMed:16272117, PubMed:27934701, PubMed:12244297, PubMed:27906160, PubMed:27906161, PubMed:28077875). Contacts 16S rRNA (PubMed:7556101). Cross-links to the P site tRNA and weakly to the A site tRNA (PubMed:8524654, PubMed:15308780).12 Publications

Protein-protein interaction databases

Database of interacting proteins

More...
DIPi
DIP-35799N

Protein interaction database and analysis system

More...
IntActi
P0A7X3, 151 interactors

STRING: functional protein association networks

More...
STRINGi
316385.ECDH10B_3407

<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

1130
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
1M5Gmodel-I4-130[»]
2YKRelectron microscopy9.80I4-130[»]
3J9Yelectron microscopy3.90i1-130[»]
3J9Zelectron microscopy3.60SI2-130[»]
3JA1electron microscopy3.60SI2-130[»]
3JBUelectron microscopy3.64I1-130[»]
3JBVelectron microscopy3.32I1-130[»]
3JCDelectron microscopy3.70i1-130[»]
3JCEelectron microscopy3.20i1-130[»]
3JCJelectron microscopy3.70o1-130[»]
3JCNelectron microscopy4.60j1-130[»]
4A2Ielectron microscopy16.50I4-130[»]
4ADVelectron microscopy13.50I2-130[»]
4U1UX-ray2.95AI/CI4-130[»]
4U1VX-ray3.00AI/CI4-130[»]
4U20X-ray2.90AI/CI4-130[»]
4U24X-ray2.90AI/CI4-130[»]
4U25X-ray2.90AI/CI4-130[»]
4U26X-ray2.80AI/CI4-130[»]
4U27X-ray2.80AI/CI4-130[»]
4V47electron microscopy12.30BI2-130[»]
4V48electron microscopy11.50BI2-130[»]
4V4HX-ray3.46AI/CI1-130[»]
4V4QX-ray3.46AI/CI2-130[»]
4V4Velectron microscopy15.00AI5-130[»]
4V4Welectron microscopy15.00AI5-130[»]
4V50X-ray3.22AI/CI2-130[»]
4V52X-ray3.21AI/CI2-130[»]
4V53X-ray3.54AI/CI2-130[»]
4V54X-ray3.30AI/CI2-130[»]
4V55X-ray4.00AI/CI2-130[»]
4V56X-ray3.93AI/CI2-130[»]
4V57X-ray3.50AI/CI2-130[»]
4V5BX-ray3.74BI/DI2-130[»]
4V5Helectron microscopy5.80AI4-130[»]
4V5YX-ray4.45AI/CI2-130[»]
4V64X-ray3.50AI/CI2-130[»]
4V65electron microscopy9.00AW1-130[»]
4V66electron microscopy9.00AW1-130[»]
4V69electron microscopy6.70AI4-130[»]
4V6CX-ray3.19AI/CI1-130[»]
4V6DX-ray3.81AI/CI1-130[»]
4V6EX-ray3.71AI/CI1-130[»]
4V6Kelectron microscopy8.25BM1-130[»]
4V6Lelectron microscopy13.20AM1-130[»]
4V6Melectron microscopy7.10AI2-130[»]
4V6Nelectron microscopy12.10BL2-130[»]
4V6Oelectron microscopy14.70AL2-130[»]
4V6Pelectron microscopy13.50AL2-130[»]
4V6Qelectron microscopy11.50AL2-130[»]
4V6Relectron microscopy11.50AL2-130[»]
4V6Selectron microscopy13.10BK2-130[»]
4V6Telectron microscopy8.30AI4-130[»]
4V6Velectron microscopy9.80AI2-130[»]
4V6Yelectron microscopy12.00AI4-130[»]
4V6Zelectron microscopy12.00AI4-130[»]
4V70electron microscopy17.00AI4-130[»]
4V71electron microscopy20.00AI4-130[»]
4V72electron microscopy13.00AI4-130[»]
4V73electron microscopy15.00AI4-130[»]
4V74electron microscopy17.00AI4-130[»]
4V75electron microscopy12.00AI4-130[»]
4V76electron microscopy17.00AI4-130[»]
4V77electron microscopy17.00AI4-130[»]
4V78electron microscopy20.00AI4-130[»]
4V79electron microscopy15.00AI4-130[»]
4V7Aelectron microscopy9.00AI4-130[»]
4V7Belectron microscopy6.80AI1-130[»]
4V7Celectron microscopy7.60AI2-130[»]
4V7Delectron microscopy7.60BI2-130[»]
4V7Ielectron microscopy9.60BI1-130[»]
4V7SX-ray3.25AI/CI4-130[»]
4V7TX-ray3.19AI/CI4-130[»]
4V7UX-ray3.10AI/CI4-130[»]
4V7VX-ray3.29AI/CI4-130[»]
4V85X-ray3.20I1-130[»]
4V89X-ray3.70AI1-130[»]
4V9CX-ray3.30AI/CI1-130[»]
4V9DX-ray3.00AI/BI4-130[»]
4V9OX-ray2.90BI/DI/FI/HI1-130[»]
4V9PX-ray2.90BI/DI/FI/HI1-130[»]
4WF1X-ray3.09AI/CI4-130[»]
4WOIX-ray3.00AI/DI1-130[»]
4WWWX-ray3.10QI/XI4-130[»]
4YBBX-ray2.10AI/BI4-130[»]
5AFIelectron microscopy2.90i1-130[»]
5H5Uelectron microscopy3.00p2-130[»]
5IQRelectron microscopy3.00n1-130[»]
5IT8X-ray3.12AI/BI4-130[»]
5J5BX-ray2.80AI/BI4-130[»]
5J7LX-ray3.00AI/BI4-130[»]
5J88X-ray3.32AI/BI4-130[»]
5J8AX-ray3.10AI/BI4-130[»]
5J91X-ray2.96AI/BI4-130[»]
5JC9X-ray3.03AI/BI4-130[»]
5JTEelectron microscopy3.60AI1-130[»]
5JU8electron microscopy3.60AI1-130[»]
5KCRelectron microscopy3.601i1-130[»]
5KCSelectron microscopy3.901i1-130[»]
5KPSelectron microscopy3.90141-130[»]
5KPVelectron microscopy4.10131-130[»]
5KPWelectron microscopy3.90131-130[»]
5KPXelectron microscopy3.90131-130[»]
5L3Pelectron microscopy3.70i1-130[»]
5LZAelectron microscopy3.60i4-130[»]
5LZBelectron microscopy5.30i4-130[»]
5LZCelectron microscopy4.80i4-130[»]
5LZDelectron microscopy3.40i4-130[»]
5LZEelectron microscopy3.50i4-130[»]
5LZFelectron microscopy4.60i4-130[»]
5MDVelectron microscopy2.97n1-130[»]
5MDWelectron microscopy3.06n1-130[»]
5MDYelectron microscopy3.35n1-130[»]
5MDZelectron microscopy3.10n1-130[»]
5ME0electron microscopy13.50I1-130[»]
5ME1electron microscopy13.50I1-130[»]
5MGPelectron microscopy3.10i4-130[»]
5MY1electron microscopy7.60I2-130[»]
5NO2electron microscopy5.16I4-130[»]
5NO3electron microscopy5.16I4-130[»]
5NO4electron microscopy5.16I4-130[»]
5NP6electron microscopy3.60L4-130[»]
5NWYelectron microscopy2.9381-130[»]
5O2Relectron microscopy3.40i4-130[»]
5U4Ielectron microscopy3.50i1-130[»]
5U9Felectron microscopy3.20I1-130[»]
5U9Gelectron microscopy3.20I1-130[»]
5UYKelectron microscopy3.90I4-130[»]
5UYLelectron microscopy3.60I4-130[»]
5UYMelectron microscopy3.20I4-130[»]
5UYNelectron microscopy4.00I4-130[»]
5UYPelectron microscopy3.90I4-130[»]
5UYQelectron microscopy3.80I4-130[»]
5WDTelectron microscopy3.00i4-130[»]
5WE4electron microscopy3.10i4-130[»]
5WE6electron microscopy3.40i4-130[»]
5WFKelectron microscopy3.40i4-130[»]
6BU8electron microscopy3.50I4-130[»]
6C4Ielectron microscopy3.24i1-130[»]
6ENFelectron microscopy3.20i4-130[»]
6ENJelectron microscopy3.70i4-130[»]
6ENUelectron microscopy3.10i4-130[»]
6GWTelectron microscopy3.80i4-130[»]
6GXMelectron microscopy3.80i4-130[»]
6GXNelectron microscopy3.90i4-130[»]
6GXOelectron microscopy3.90i4-130[»]
6GXPelectron microscopy4.40i4-130[»]
6H4Nelectron microscopy3.00i4-130[»]
6H58electron microscopy7.90i/ii4-130[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P0A7X3

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

More...
SMRi
P0A7X3

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
P0A7X3

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG0103 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000019802

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0A7X3

KEGG Orthology (KO)

More...
KOi
K02996

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0A7X3

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_00532_B Ribosomal_S9_B, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR020568 Ribosomal_S5_D2-typ_fold
IPR014721 Ribosomal_S5_D2-typ_fold_subgr
IPR000754 Ribosomal_S9
IPR023035 Ribosomal_S9_bac/plastid
IPR020574 Ribosomal_S9_CS

The PANTHER Classification System

More...
PANTHERi
PTHR21569 PTHR21569, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00380 Ribosomal_S9, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF54211 SSF54211, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00360 RIBOSOMAL_S9, 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.

P0A7X3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAENQYYGTG RRKSSAARVF IKPGNGKIVI NQRSLEQYFG RETARMVVRQ
60 70 80 90 100
PLELVDMVEK LDLYITVKGG GISGQAGAIR HGITRALMEY DESLRSELRK
110 120 130
AGFVTRDARQ VERKKVGLRK ARRRPQFSKR
Length:130
Mass (Da):14,856
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:i757D599168812806
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 conflicti56D → N AA sequence (PubMed:1091515).Curated1
Sequence conflicti124Missing AA sequence (PubMed:1091515).Curated1
Sequence conflicti126Q → E AA sequence (PubMed:1091515).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 14723.3 Da from positions 2 - 130. Determined by MALDI. 1 Publication

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
X02130 Genomic DNA Translation: CAA26042.1
U18997 Genomic DNA Translation: AAA58032.1
U00096 Genomic DNA Translation: AAC76262.1
AP009048 Genomic DNA Translation: BAE77273.1

Protein sequence database of the Protein Information Resource

More...
PIRi
H65114 R3EC9

NCBI Reference Sequences

More...
RefSeqi
NP_417697.1, NC_000913.3
WP_000829818.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC76262; AAC76262; b3230
BAE77273; BAE77273; BAE77273

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
29458256
949000

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW3199
eco:b3230

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.3498

<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
X02130 Genomic DNA Translation: CAA26042.1
U18997 Genomic DNA Translation: AAA58032.1
U00096 Genomic DNA Translation: AAC76262.1
AP009048 Genomic DNA Translation: BAE77273.1
PIRiH65114 R3EC9
RefSeqiNP_417697.1, NC_000913.3
WP_000829818.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-I4-130[»]
2YKRelectron microscopy9.80I4-130[»]
3J9Yelectron microscopy3.90i1-130[»]
3J9Zelectron microscopy3.60SI2-130[»]
3JA1electron microscopy3.60SI2-130[»]
3JBUelectron microscopy3.64I1-130[»]
3JBVelectron microscopy3.32I1-130[»]
3JCDelectron microscopy3.70i1-130[»]
3JCEelectron microscopy3.20i1-130[»]
3JCJelectron microscopy3.70o1-130[»]
3JCNelectron microscopy4.60j1-130[»]
4A2Ielectron microscopy16.50I4-130[»]
4ADVelectron microscopy13.50I2-130[»]
4U1UX-ray2.95AI/CI4-130[»]
4U1VX-ray3.00AI/CI4-130[»]
4U20X-ray2.90AI/CI4-130[»]
4U24X-ray2.90AI/CI4-130[»]
4U25X-ray2.90AI/CI4-130[»]
4U26X-ray2.80AI/CI4-130[»]
4U27X-ray2.80AI/CI4-130[»]
4V47electron microscopy12.30BI2-130[»]
4V48electron microscopy11.50BI2-130[»]
4V4HX-ray3.46AI/CI1-130[»]
4V4QX-ray3.46AI/CI2-130[»]
4V4Velectron microscopy15.00AI5-130[»]
4V4Welectron microscopy15.00AI5-130[»]
4V50X-ray3.22AI/CI2-130[»]
4V52X-ray3.21AI/CI2-130[»]
4V53X-ray3.54AI/CI2-130[»]
4V54X-ray3.30AI/CI2-130[»]
4V55X-ray4.00AI/CI2-130[»]
4V56X-ray3.93AI/CI2-130[»]
4V57X-ray3.50AI/CI2-130[»]
4V5BX-ray3.74BI/DI2-130[»]
4V5Helectron microscopy5.80AI4-130[»]
4V5YX-ray4.45AI/CI2-130[»]
4V64X-ray3.50AI/CI2-130[»]
4V65electron microscopy9.00AW1-130[»]
4V66electron microscopy9.00AW1-130[»]
4V69electron microscopy6.70AI4-130[»]
4V6CX-ray3.19AI/CI1-130[»]
4V6DX-ray3.81AI/CI1-130[»]
4V6EX-ray3.71AI/CI1-130[»]
4V6Kelectron microscopy8.25BM1-130[»]
4V6Lelectron microscopy13.20AM1-130[»]
4V6Melectron microscopy7.10AI2-130[»]
4V6Nelectron microscopy12.10BL2-130[»]
4V6Oelectron microscopy14.70AL2-130[»]
4V6Pelectron microscopy13.50AL2-130[»]
4V6Qelectron microscopy11.50AL2-130[»]
4V6Relectron microscopy11.50AL2-130[»]
4V6Selectron microscopy13.10BK2-130[»]
4V6Telectron microscopy8.30AI4-130[»]
4V6Velectron microscopy9.80AI2-130[»]
4V6Yelectron microscopy12.00AI4-130[»]
4V6Zelectron microscopy12.00AI4-130[»]
4V70electron microscopy17.00AI4-130[»]
4V71electron microscopy20.00AI4-130[»]
4V72electron microscopy13.00AI4-130[»]
4V73electron microscopy15.00AI4-130[»]
4V74electron microscopy17.00AI4-130[»]
4V75electron microscopy12.00AI4-130[»]
4V76electron microscopy17.00AI4-130[»]
4V77electron microscopy17.00AI4-130[»]
4V78electron microscopy20.00AI4-130[»]
4V79electron microscopy15.00AI4-130[»]
4V7Aelectron microscopy9.00AI4-130[»]
4V7Belectron microscopy6.80AI1-130[»]
4V7Celectron microscopy7.60AI2-130[»]
4V7Delectron microscopy7.60BI2-130[»]
4V7Ielectron microscopy9.60BI1-130[»]
4V7SX-ray3.25AI/CI4-130[»]
4V7TX-ray3.19AI/CI4-130[»]
4V7UX-ray3.10AI/CI4-130[»]
4V7VX-ray3.29AI/CI4-130[»]
4V85X-ray3.20I1-130[»]
4V89X-ray3.70AI1-130[»]
4V9CX-ray3.30AI/CI1-130[»]
4V9DX-ray3.00AI/BI4-130[»]
4V9OX-ray2.90BI/DI/FI/HI1-130[»]
4V9PX-ray2.90BI/DI/FI/HI1-130[»]
4WF1X-ray3.09AI/CI4-130[»]
4WOIX-ray3.00AI/DI1-130[»]
4WWWX-ray3.10QI/XI4-130[»]
4YBBX-ray2.10AI/BI4-130[»]
5AFIelectron microscopy2.90i1-130[»]
5H5Uelectron microscopy3.00p2-130[»]
5IQRelectron microscopy3.00n1-130[»]
5IT8X-ray3.12AI/BI4-130[»]
5J5BX-ray2.80AI/BI4-130[»]
5J7LX-ray3.00AI/BI4-130[»]
5J88X-ray3.32AI/BI4-130[»]
5J8AX-ray3.10AI/BI4-130[»]
5J91X-ray2.96AI/BI4-130[»]
5JC9X-ray3.03AI/BI4-130[»]
5JTEelectron microscopy3.60AI1-130[»]
5JU8electron microscopy3.60AI1-130[»]
5KCRelectron microscopy3.601i1-130[»]
5KCSelectron microscopy3.901i1-130[»]
5KPSelectron microscopy3.90141-130[»]
5KPVelectron microscopy4.10131-130[»]
5KPWelectron microscopy3.90131-130[»]
5KPXelectron microscopy3.90131-130[»]
5L3Pelectron microscopy3.70i1-130[»]
5LZAelectron microscopy3.60i4-130[»]
5LZBelectron microscopy5.30i4-130[»]
5LZCelectron microscopy4.80i4-130[»]
5LZDelectron microscopy3.40i4-130[»]
5LZEelectron microscopy3.50i4-130[»]
5LZFelectron microscopy4.60i4-130[»]
5MDVelectron microscopy2.97n1-130[»]
5MDWelectron microscopy3.06n1-130[»]
5MDYelectron microscopy3.35n1-130[»]
5MDZelectron microscopy3.10n1-130[»]
5ME0electron microscopy13.50I1-130[»]
5ME1electron microscopy13.50I1-130[»]
5MGPelectron microscopy3.10i4-130[»]
5MY1electron microscopy7.60I2-130[»]
5NO2electron microscopy5.16I4-130[»]
5NO3electron microscopy5.16I4-130[»]
5NO4electron microscopy5.16I4-130[»]
5NP6electron microscopy3.60L4-130[»]
5NWYelectron microscopy2.9381-130[»]
5O2Relectron microscopy3.40i4-130[»]
5U4Ielectron microscopy3.50i1-130[»]
5U9Felectron microscopy3.20I1-130[»]
5U9Gelectron microscopy3.20I1-130[»]
5UYKelectron microscopy3.90I4-130[»]
5UYLelectron microscopy3.60I4-130[»]
5UYMelectron microscopy3.20I4-130[»]
5UYNelectron microscopy4.00I4-130[»]
5UYPelectron microscopy3.90I4-130[»]
5UYQelectron microscopy3.80I4-130[»]
5WDTelectron microscopy3.00i4-130[»]
5WE4electron microscopy3.10i4-130[»]
5WE6electron microscopy3.40i4-130[»]
5WFKelectron microscopy3.40i4-130[»]
6BU8electron microscopy3.50I4-130[»]
6C4Ielectron microscopy3.24i1-130[»]
6ENFelectron microscopy3.20i4-130[»]
6ENJelectron microscopy3.70i4-130[»]
6ENUelectron microscopy3.10i4-130[»]
6GWTelectron microscopy3.80i4-130[»]
6GXMelectron microscopy3.80i4-130[»]
6GXNelectron microscopy3.90i4-130[»]
6GXOelectron microscopy3.90i4-130[»]
6GXPelectron microscopy4.40i4-130[»]
6H4Nelectron microscopy3.00i4-130[»]
6H58electron microscopy7.90i/ii4-130[»]
ProteinModelPortaliP0A7X3
SMRiP0A7X3
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-35799N
IntActiP0A7X3, 151 interactors
STRINGi316385.ECDH10B_3407

Chemistry databases

DrugBankiDB00453 Clomocycline
DB00618 Demeclocycline
DB00254 Doxycycline
DB00256 Lymecycline
DB01017 Minocycline
DB00595 Oxytetracycline
DB01301 Rolitetracycline
DB00560 Tigecycline

Proteomic databases

EPDiP0A7X3
jPOSTiP0A7X3
PaxDbiP0A7X3
PRIDEiP0A7X3

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76262; AAC76262; b3230
BAE77273; BAE77273; BAE77273
GeneIDi29458256
949000
KEGGiecj:JW3199
eco:b3230
PATRICifig|1411691.4.peg.3498

Organism-specific databases

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

More...
EchoBASEi
EB0901
EcoGeneiEG10908 rpsI

Phylogenomic databases

eggNOGiCOG0103 LUCA
HOGENOMiHOG000019802
InParanoidiP0A7X3
KOiK02996
PhylomeDBiP0A7X3

Enzyme and pathway databases

BioCyciEcoCyc:EG10908-MONOMER
MetaCyc:EG10908-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0A7X3

Protein Ontology

More...
PROi
PR:P0A7X3

Family and domain databases

Gene3Di3.30.230.10, 1 hit
HAMAPiMF_00532_B Ribosomal_S9_B, 1 hit
InterProiView protein in InterPro
IPR020568 Ribosomal_S5_D2-typ_fold
IPR014721 Ribosomal_S5_D2-typ_fold_subgr
IPR000754 Ribosomal_S9
IPR023035 Ribosomal_S9_bac/plastid
IPR020574 Ribosomal_S9_CS
PANTHERiPTHR21569 PTHR21569, 1 hit
PfamiView protein in Pfam
PF00380 Ribosomal_S9, 1 hit
SUPFAMiSSF54211 SSF54211, 1 hit
PROSITEiView protein in PROSITE
PS00360 RIBOSOMAL_S9, 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 nameiRS9_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: P0A7X3
Secondary accession number(s): P02363, Q2M8Y3
<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 137 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
UniProt is an ELIXIR core data resource
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