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P0ADZ4 (RS15_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
30S ribosomal protein S15
Gene names
Name:rpsO
Synonyms:secC
Ordered Locus Names:b3165, JW3134
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length89 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. HAMAP-Rule MF_01343

In the E.coli 70S ribosome it has been modeled (Ref.12) to contact the 23S rRNA of the 50S subunit forming part of bridge B4. In the two 3.5 A resolved ribosome structures (Ref.13) there are minor differences between side-chain conformations. HAMAP-Rule MF_01343

Subunit structure

Part of the 30S ribosomal subunit. Forms a bridge to the 50S subunit in the 70S ribosome, contacting the 23S rRNA. Ref.12 Ref.13

Sequence similarities

Belongs to the ribosomal protein S15P family.

Mass spectrometry

Molecular mass is 10137.6 Da from positions 2 - 89. Determined by MALDI. Ref.10

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 898830S ribosomal protein S15 HAMAP-Rule MF_01343
PRO_0000115437

Experimental info

Sequence conflict661Missing Ref.3

Secondary structure

.......... 89
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0ADZ4 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: AABDDA6674B99B1C

FASTA8910,269
        10         20         30         40         50         60 
MSLSTEATAK IVSEFGRDAN DTGSTEVQVA LLTAQINHLQ GHFAEHKKDH HSRRGLLRMV 

        70         80 
SQRRKLLDYL KRKDVARYTQ LIERLGLRR 

« Hide

References

« Hide 'large scale' references
[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(1984) [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(1984) [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(1985) [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(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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(2006) [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(1976) [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(1988) [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(1997) [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(1999) [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(2002) [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(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS), INTERSUBUNIT BRIDGE FORMATION.
Strain: MRE-600.
[13]"Structures of the bacterial ribosome at 3.5 A resolution."
Schuwirth B.S., Borovinskaya M.A., Hau C.W., Zhang W., Vila-Sanjurjo A., Holton J.M., Cate J.H.D.
Science 310:827-834(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES INCLUDING THE INTERSUBUNIT BRIDGE.
Strain: MRE-600.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRR3EC15. B26118.
RefSeqNP_417634.1. NC_000913.3.
YP_491352.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EG0electron microscopy11.50F1-89[»]
1P6Gelectron microscopy12.30O2-89[»]
1P87electron microscopy11.50O2-89[»]
2AVYX-ray3.46O1-89[»]
2AW7X-ray3.46O1-89[»]
2GY9electron microscopy15.00O3-88[»]
2GYBelectron microscopy15.00O3-88[»]
2QALX-ray3.21O1-89[»]
2QANX-ray3.21O1-89[»]
2QB9X-ray3.54O1-89[»]
2QBBX-ray3.54O1-89[»]
2QBDX-ray3.30O1-89[»]
2QBFX-ray3.30O1-89[»]
2QBHX-ray4.00O1-89[»]
2QBJX-ray4.00O1-89[»]
2QOUX-ray3.93O1-89[»]
2QOWX-ray3.93O1-89[»]
2QOYX-ray3.50O1-89[»]
2QP0X-ray3.50O1-89[»]
2VAZelectron microscopy10.00F2-89[»]
2WWLelectron microscopy5.80O2-89[»]
2YKRelectron microscopy9.80O2-89[»]
2Z4KX-ray4.45O1-89[»]
2Z4MX-ray4.45O1-89[»]
3DF1X-ray3.50O1-89[»]
3DF3X-ray3.50O1-89[»]
3E1Aelectron microscopy9.00H1-89[»]
3E1Celectron microscopy9.00H1-89[»]
3FIHelectron microscopy6.70O2-89[»]
3I1MX-ray3.19O1-89[»]
3I1OX-ray3.19O1-89[»]
3I1QX-ray3.81O1-89[»]
3I1SX-ray3.81O1-89[»]
3I1ZX-ray3.71O1-89[»]
3I21X-ray3.71O1-89[»]
3IZVelectron microscopy-S1-89[»]
3IZWelectron microscopy-S1-89[»]
3J00electron microscopy-O2-89[»]
3J18electron microscopy8.30O2-89[»]
3J36electron microscopy9.80O2-89[»]
3J4Velectron microscopy12.00O1-89[»]
3J4Welectron microscopy12.00O1-89[»]
3J4Yelectron microscopy17.00O1-89[»]
3J4Zelectron microscopy20.00O1-89[»]
3J53electron microscopy13.00O1-89[»]
3J55electron microscopy15.00O1-89[»]
3J57electron microscopy17.00O1-89[»]
3J59electron microscopy12.00O1-89[»]
3J5Belectron microscopy17.00O1-89[»]
3J5Delectron microscopy17.00O1-89[»]
3J5Felectron microscopy20.00O1-89[»]
3J5Helectron microscopy15.00O1-89[»]
3J5Jelectron microscopy9.00O1-89[»]
3J5Nelectron microscopy6.80O1-89[»]
3J5Telectron microscopy7.60O2-89[»]
3J5Xelectron microscopy7.60O2-89[»]
3KC4electron microscopy-O1-89[»]
3OAQX-ray3.25O2-89[»]
3OARX-ray3.25O2-89[»]
3OFAX-ray3.19O2-89[»]
3OFBX-ray3.19O2-89[»]
3OFOX-ray3.10O2-89[»]
3OFPX-ray3.10O2-89[»]
3OFXX-ray3.29O2-89[»]
3OFYX-ray3.29O2-89[»]
3OR9X-ray3.30O1-89[»]
3ORAX-ray3.30O1-89[»]
3SFSX-ray3.20O1-89[»]
3UOQX-ray3.70O1-89[»]
4A2Ielectron microscopy16.50O2-89[»]
4ADVelectron microscopy13.50O1-89[»]
4GAQX-ray3.30O1-89[»]
4GASX-ray3.30O1-89[»]
4GD1X-ray3.00O2-89[»]
4GD2X-ray3.00O2-89[»]
4KIYX-ray2.90O1-89[»]
4KJ0X-ray2.90O1-89[»]
4KJ2X-ray2.90O1-89[»]
4KJ4X-ray2.90O1-89[»]
4KJ6X-ray2.90O1-89[»]
4KJ8X-ray2.90O1-89[»]
4KJAX-ray2.90O1-89[»]
4KJCX-ray2.90O1-89[»]
ProteinModelPortalP0ADZ4.
SMRP0ADZ4. Positions 3-88.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-47909N.
IntActP0ADZ4. 30 interactions.
MINTMINT-1299353.
STRING511145.b3165.

Chemistry

ChEMBLCHEMBL2363135.

Proteomic databases

PaxDbP0ADZ4.
PRIDEP0ADZ4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76199; AAC76199; b3165.
BAE77211; BAE77211; BAE77211.
GeneID12933439.
947686.
KEGGecj:Y75_p3087.
eco:b3165.
PATRIC32121748. VBIEscCol129921_3260.

Organism-specific databases

EchoBASEEB0907.
EcoGeneEG10914. rpsO.

Phylogenomic databases

eggNOGCOG0184.
HOGENOMHOG000040097.
KOK02956.
OMANKQDHHS.
OrthoDBEOG6B368J.
PhylomeDBP0ADZ4.

Enzyme and pathway databases

BioCycEcoCyc:EG10914-MONOMER.
ECOL316407:JW3134-MONOMER.

Gene expression databases

GenevestigatorP0ADZ4.

Family and domain databases

Gene3D1.10.287.10. 1 hit.
HAMAPMF_01343_B. Ribosomal_S15_B.
InterProIPR000589. Ribosomal_S15.
IPR005290. Ribosomal_S15_bac-type.
IPR009068. S15_NS1_RNA-bd.
[Graphical view]
PfamPF00312. Ribosomal_S15. 1 hit.
[Graphical view]
SUPFAMSSF47060. SSF47060. 1 hit.
TIGRFAMsTIGR00952. S15_bact. 1 hit.
PROSITEPS00362. RIBOSOMAL_S15. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0ADZ4.
PROP0ADZ4.

Entry information

Entry nameRS15_ECOLI
AccessionPrimary (citable) accession number: P0ADZ4
Secondary accession number(s): P02371, Q2M945
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene