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Protein

30S ribosomal protein S15

Gene

rpsO

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it helps nucleate assembly of the platform of the 30S subunit by binding and bridging several RNA helices of the 16S rRNA.
In the E.coli 70S ribosome it has been modeled (PubMed:12809609) to contact the 23S rRNA of the 50S subunit forming part of bridge B4. In the two 3.5 A resolved ribosome structures (PubMed:16272117) there are minor differences between side-chain conformations.2 Publications

GO - Molecular functioni

  1. rRNA binding Source: EcoliWiki
  2. structural constituent of ribosome Source: InterPro

GO - Biological processi

  1. mRNA polyadenylation Source: EcoliWiki
  2. translation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10914-MONOMER.
ECOL316407:JW3134-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S15UniRule annotation
Gene namesi
Name:rpsOUniRule annotation
Synonyms:secC
Ordered Locus Names:b3165, JW3134
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10914. rpsO.

Subcellular locationi

GO - Cellular componenti

  1. cytosolic small ribosomal subunit Source: EcoliWiki
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 898830S ribosomal protein S15PRO_0000115437Add
BLAST

Proteomic databases

PaxDbiP0ADZ4.
PRIDEiP0ADZ4.

Expressioni

Gene expression databases

GenevestigatoriP0ADZ4.

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit. Forms a bridge to the 50S subunit in the 70S ribosome, contacting the 23S rRNA.

Protein-protein interaction databases

DIPiDIP-47909N.
IntActiP0ADZ4. 30 interactions.
MINTiMINT-1299353.
STRINGi511145.b3165.

Structurei

Secondary structure

1
89
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1511Combined sources
Beta strandi16 – 183Combined sources
Helixi25 – 4420Combined sources
Helixi50 – 7324Combined sources
Helixi75 – 8511Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EG0electron microscopy11.50F1-89[»]
2VAZelectron microscopy10.00F2-89[»]
2YKRelectron microscopy9.80O2-89[»]
4A2Ielectron microscopy16.50O2-89[»]
4ADVelectron microscopy13.50O1-89[»]
4U1UX-ray2.95AO/CO2-89[»]
4U1VX-ray3.00AO/CO2-89[»]
4U20X-ray2.90AO/CO2-89[»]
4U24X-ray2.90AO/CO2-89[»]
4U25X-ray2.90AO/CO2-89[»]
4U26X-ray2.80AO/CO2-89[»]
4U27X-ray2.80AO/CO2-89[»]
4V47electron microscopy12.30BO2-89[»]
4V48electron microscopy11.50BO2-89[»]
4V4HX-ray3.46AO/CO1-89[»]
4V4QX-ray3.46AO/CO1-89[»]
4V4Velectron microscopy15.00AO3-88[»]
4V4Welectron microscopy15.00AO3-88[»]
4V50X-ray3.22AO/CO2-89[»]
4V52X-ray3.21AO/CO1-89[»]
4V53X-ray3.54AO/CO1-89[»]
4V54X-ray3.30AO/CO1-89[»]
4V55X-ray4.00AO/CO1-89[»]
4V56X-ray3.93AO/CO1-89[»]
4V57X-ray3.50AO/CO1-89[»]
4V5BX-ray3.74BO/DO1-89[»]
4V5Helectron microscopy5.80AO2-89[»]
4V5YX-ray4.45AO/CO1-89[»]
4V64X-ray3.50AO/CO1-89[»]
4V65electron microscopy9.00AH1-89[»]
4V66electron microscopy9.00AH1-89[»]
4V69electron microscopy6.70AO2-89[»]
4V6CX-ray3.19AO/CO1-89[»]
4V6DX-ray3.81AO/CO1-89[»]
4V6EX-ray3.71AO/CO1-89[»]
4V6Kelectron microscopy8.25BS1-89[»]
4V6Lelectron microscopy13.20AS1-89[»]
4V6Melectron microscopy-O2-89[»]
4V6Nelectron microscopy12.10BR2-89[»]
4V6Oelectron microscopy14.70AR2-89[»]
4V6Pelectron microscopy13.50AR2-89[»]
4V6Qelectron microscopy11.50AR2-89[»]
4V6Relectron microscopy11.50AR2-89[»]
4V6Selectron microscopy13.10BQ2-89[»]
4V6Telectron microscopy8.30AO2-89[»]
4V6Velectron microscopy9.80AO2-89[»]
4V6Yelectron microscopy12.00AO1-89[»]
4V6Zelectron microscopy12.00AO1-89[»]
4V70electron microscopy17.00AO1-89[»]
4V71electron microscopy20.00AO1-89[»]
4V72electron microscopy13.00AO1-89[»]
4V73electron microscopy15.00AO1-89[»]
4V74electron microscopy17.00AO1-89[»]
4V75electron microscopy12.00AO1-89[»]
4V76electron microscopy17.00AO1-89[»]
4V77electron microscopy17.00AO1-89[»]
4V78electron microscopy20.00AO1-89[»]
4V79electron microscopy15.00AO1-89[»]
4V7Aelectron microscopy9.00AO1-89[»]
4V7Belectron microscopy6.80AO1-89[»]
4V7Celectron microscopy7.60AO2-89[»]
4V7Delectron microscopy7.60BO2-89[»]
4V7Ielectron microscopy9.60BO1-89[»]
4V7SX-ray3.25AO/CO2-89[»]
4V7TX-ray3.19AO/CO2-89[»]
4V7UX-ray3.10AO/CO2-89[»]
4V7VX-ray3.29AO/CO2-89[»]
4V85X-ray3.20O1-89[»]
4V89X-ray3.70AO1-89[»]
4V9CX-ray3.30AO/CO1-89[»]
4V9DX-ray3.00AO/BO2-89[»]
4V9OX-ray2.90BO/DO/FO/HO1-89[»]
4V9PX-ray2.90BO/DO/FO/HO1-89[»]
4WF1X-ray3.09AO/CO2-89[»]
4WWWX-ray3.10QO/XO2-89[»]
ProteinModelPortaliP0ADZ4.
SMRiP0ADZ4. Positions 3-88.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ADZ4.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S15P family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0184.
HOGENOMiHOG000040097.
InParanoidiP0ADZ4.
KOiK02956.
OMAiFKTHVKD.
OrthoDBiEOG6B368J.
PhylomeDBiP0ADZ4.

Family and domain databases

Gene3Di1.10.287.10. 1 hit.
HAMAPiMF_01343_B. Ribosomal_S15_B.
InterProiIPR000589. Ribosomal_S15.
IPR005290. Ribosomal_S15_bac-type.
IPR009068. S15_NS1_RNA-bd.
[Graphical view]
PfamiPF00312. Ribosomal_S15. 1 hit.
[Graphical view]
SUPFAMiSSF47060. SSF47060. 1 hit.
TIGRFAMsiTIGR00952. S15_bact. 1 hit.
PROSITEiPS00362. RIBOSOMAL_S15. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0ADZ4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLSTEATAK IVSEFGRDAN DTGSTEVQVA LLTAQINHLQ GHFAEHKKDH
60 70 80
HSRRGLLRMV SQRRKLLDYL KRKDVARYTQ LIERLGLRR
Length:89
Mass (Da):10,269
Last modified:January 22, 2007 - v2
Checksum:iAABDDA6674B99B1C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti66 – 661Missing (PubMed:3005122).Curated

Mass spectrometryi

Molecular mass is 10137.6 Da from positions 2 - 89. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01073 Genomic DNA. Translation: CAA25536.1.
X00761 Genomic DNA. Translation: CAA25331.1.
M14425 Genomic DNA. Translation: AAA24595.1.
J02638 Genomic DNA. Translation: AAA83904.1.
U18997 Genomic DNA. Translation: AAA57968.1.
U00096 Genomic DNA. Translation: AAC76199.1.
AP009048 Genomic DNA. Translation: BAE77211.1.
X13775 Genomic DNA. Translation: CAA32022.1.
PIRiB26118. R3EC15.
RefSeqiNP_417634.1. NC_000913.3.
YP_491352.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76199; AAC76199; b3165.
BAE77211; BAE77211; BAE77211.
GeneIDi12933439.
947686.
KEGGiecj:Y75_p3087.
eco:b3165.
PATRICi32121748. VBIEscCol129921_3260.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01073 Genomic DNA. Translation: CAA25536.1.
X00761 Genomic DNA. Translation: CAA25331.1.
M14425 Genomic DNA. Translation: AAA24595.1.
J02638 Genomic DNA. Translation: AAA83904.1.
U18997 Genomic DNA. Translation: AAA57968.1.
U00096 Genomic DNA. Translation: AAC76199.1.
AP009048 Genomic DNA. Translation: BAE77211.1.
X13775 Genomic DNA. Translation: CAA32022.1.
PIRiB26118. R3EC15.
RefSeqiNP_417634.1. NC_000913.3.
YP_491352.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EG0electron microscopy11.50F1-89[»]
2VAZelectron microscopy10.00F2-89[»]
2YKRelectron microscopy9.80O2-89[»]
4A2Ielectron microscopy16.50O2-89[»]
4ADVelectron microscopy13.50O1-89[»]
4U1UX-ray2.95AO/CO2-89[»]
4U1VX-ray3.00AO/CO2-89[»]
4U20X-ray2.90AO/CO2-89[»]
4U24X-ray2.90AO/CO2-89[»]
4U25X-ray2.90AO/CO2-89[»]
4U26X-ray2.80AO/CO2-89[»]
4U27X-ray2.80AO/CO2-89[»]
4V47electron microscopy12.30BO2-89[»]
4V48electron microscopy11.50BO2-89[»]
4V4HX-ray3.46AO/CO1-89[»]
4V4QX-ray3.46AO/CO1-89[»]
4V4Velectron microscopy15.00AO3-88[»]
4V4Welectron microscopy15.00AO3-88[»]
4V50X-ray3.22AO/CO2-89[»]
4V52X-ray3.21AO/CO1-89[»]
4V53X-ray3.54AO/CO1-89[»]
4V54X-ray3.30AO/CO1-89[»]
4V55X-ray4.00AO/CO1-89[»]
4V56X-ray3.93AO/CO1-89[»]
4V57X-ray3.50AO/CO1-89[»]
4V5BX-ray3.74BO/DO1-89[»]
4V5Helectron microscopy5.80AO2-89[»]
4V5YX-ray4.45AO/CO1-89[»]
4V64X-ray3.50AO/CO1-89[»]
4V65electron microscopy9.00AH1-89[»]
4V66electron microscopy9.00AH1-89[»]
4V69electron microscopy6.70AO2-89[»]
4V6CX-ray3.19AO/CO1-89[»]
4V6DX-ray3.81AO/CO1-89[»]
4V6EX-ray3.71AO/CO1-89[»]
4V6Kelectron microscopy8.25BS1-89[»]
4V6Lelectron microscopy13.20AS1-89[»]
4V6Melectron microscopy-O2-89[»]
4V6Nelectron microscopy12.10BR2-89[»]
4V6Oelectron microscopy14.70AR2-89[»]
4V6Pelectron microscopy13.50AR2-89[»]
4V6Qelectron microscopy11.50AR2-89[»]
4V6Relectron microscopy11.50AR2-89[»]
4V6Selectron microscopy13.10BQ2-89[»]
4V6Telectron microscopy8.30AO2-89[»]
4V6Velectron microscopy9.80AO2-89[»]
4V6Yelectron microscopy12.00AO1-89[»]
4V6Zelectron microscopy12.00AO1-89[»]
4V70electron microscopy17.00AO1-89[»]
4V71electron microscopy20.00AO1-89[»]
4V72electron microscopy13.00AO1-89[»]
4V73electron microscopy15.00AO1-89[»]
4V74electron microscopy17.00AO1-89[»]
4V75electron microscopy12.00AO1-89[»]
4V76electron microscopy17.00AO1-89[»]
4V77electron microscopy17.00AO1-89[»]
4V78electron microscopy20.00AO1-89[»]
4V79electron microscopy15.00AO1-89[»]
4V7Aelectron microscopy9.00AO1-89[»]
4V7Belectron microscopy6.80AO1-89[»]
4V7Celectron microscopy7.60AO2-89[»]
4V7Delectron microscopy7.60BO2-89[»]
4V7Ielectron microscopy9.60BO1-89[»]
4V7SX-ray3.25AO/CO2-89[»]
4V7TX-ray3.19AO/CO2-89[»]
4V7UX-ray3.10AO/CO2-89[»]
4V7VX-ray3.29AO/CO2-89[»]
4V85X-ray3.20O1-89[»]
4V89X-ray3.70AO1-89[»]
4V9CX-ray3.30AO/CO1-89[»]
4V9DX-ray3.00AO/BO2-89[»]
4V9OX-ray2.90BO/DO/FO/HO1-89[»]
4V9PX-ray2.90BO/DO/FO/HO1-89[»]
4WF1X-ray3.09AO/CO2-89[»]
4WWWX-ray3.10QO/XO2-89[»]
ProteinModelPortaliP0ADZ4.
SMRiP0ADZ4. Positions 3-88.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-47909N.
IntActiP0ADZ4. 30 interactions.
MINTiMINT-1299353.
STRINGi511145.b3165.

Chemistry

ChEMBLiCHEMBL2363135.

Proteomic databases

PaxDbiP0ADZ4.
PRIDEiP0ADZ4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76199; AAC76199; b3165.
BAE77211; BAE77211; BAE77211.
GeneIDi12933439.
947686.
KEGGiecj:Y75_p3087.
eco:b3165.
PATRICi32121748. VBIEscCol129921_3260.

Organism-specific databases

EchoBASEiEB0907.
EcoGeneiEG10914. rpsO.

Phylogenomic databases

eggNOGiCOG0184.
HOGENOMiHOG000040097.
InParanoidiP0ADZ4.
KOiK02956.
OMAiFKTHVKD.
OrthoDBiEOG6B368J.
PhylomeDBiP0ADZ4.

Enzyme and pathway databases

BioCyciEcoCyc:EG10914-MONOMER.
ECOL316407:JW3134-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0ADZ4.
PROiP0ADZ4.

Gene expression databases

GenevestigatoriP0ADZ4.

Family and domain databases

Gene3Di1.10.287.10. 1 hit.
HAMAPiMF_01343_B. Ribosomal_S15_B.
InterProiIPR000589. Ribosomal_S15.
IPR005290. Ribosomal_S15_bac-type.
IPR009068. S15_NS1_RNA-bd.
[Graphical view]
PfamiPF00312. Ribosomal_S15. 1 hit.
[Graphical view]
SUPFAMiSSF47060. SSF47060. 1 hit.
TIGRFAMsiTIGR00952. S15_bact. 1 hit.
PROSITEiPS00362. RIBOSOMAL_S15. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the gene for Escherichia coli ribosomal protein S15 (rpsO)."
    Takata R., Mukai T., Aoyagi M., Hori K.
    Mol. Gen. Genet. 197:225-229(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Expression of the rpsO and pnp genes: structural analysis of a DNA fragment carrying their control regions."
    Portier C., Regnier P.
    Nucleic Acids Res. 12:6091-6102(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Promoter activity and transcript mapping in the regulatory region for genes encoding ribosomal protein S15 and polynucleotide phosphorylase of Escherichia coli."
    Evans S., Dennis P.P.
    Gene 40:15-22(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Nucleotide sequence of the pnp gene of Escherichia coli encoding polynucleotide phosphorylase. Homology of the primary structure of the protein with the RNA-binding domain of ribosomal protein S1."
    Regnier P., Grunberg-Manago M., Portier C.
    J. Biol. Chem. 262:63-68(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  6. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  7. "Primary structure of the 16S rRNA binding protein S15 from Escherichia coli ribosomes."
    Morinaga T., Funatsu G., Funatsu M., Wittmann H.G.
    FEBS Lett. 64:307-309(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-89.
    Strain: K.
  8. "The existence of two genes between infB and rpsO in the Escherichia coli genome: DNA sequencing and S1 nuclease mapping."
    Sands J.F., Regnier P., Cummings H.S., Grunberg-Manago M., Hershey J.W.B.
    Nucleic Acids Res. 16:10803-10816(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
  9. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  10. "Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry."
    Arnold R.J., Reilly J.P.
    Anal. Biochem. 269:105-112(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY.
    Strain: K12 / ATCC 25404 / DSM 5698 / NCIMB 11290.
  11. "All-atom homology model of the Escherichia coli 30S ribosomal subunit."
    Tung C.-S., Joseph S., Sanbonmatsu K.Y.
    Nat. Struct. Biol. 9:750-755(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING.
  12. "Study of the structural dynamics of the E. coli 70S ribosome using real-space refinement."
    Gao H., Sengupta J., Valle M., Korostelev A., Eswar N., Stagg S.M., Van Roey P., Agrawal R.K., Harvey S.C., Sali A., Chapman M.S., Frank J.
    Cell 113:789-801(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS), INTERSUBUNIT BRIDGE FORMATION.
    Strain: MRE-600.
  13. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES INCLUDING THE INTERSUBUNIT BRIDGE.
    Strain: MRE-600.

Entry informationi

Entry nameiRS15_ECOLI
AccessioniPrimary (citable) accession number: P0ADZ4
Secondary accession number(s): P02371, Q2M945
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 20, 1986
Last sequence update: January 22, 2007
Last modified: March 31, 2015
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Ribosomal proteins
    Ribosomal proteins families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.