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P02413 (RL15_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 144. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
50S ribosomal protein L15
Gene names
Name:rplO
Ordered Locus Names:b3301, JW3263
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length144 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This protein binds the 5S rRNA. It is required for the late stages of subunit assembly, and is essential for 5S rRNA assembly onto the ribosome. HAMAP-Rule MF_01341_B

Subunit structure

Part of the 50S ribosomal subunit. Contacts the 5S rRNA. Ref.5

Sequence similarities

Belongs to the ribosomal protein L15P family.

Mass spectrometry

Molecular mass is 14980.1 Da from positions 1 - 144. Determined by MALDI. Ref.6

Binary interactions

With

Entry

#Exp.

IntAct

Notes

rlmNP369793EBI-543017,EBI-559071

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14414450S ribosomal protein L15 HAMAP-Rule MF_01341_B
PRO_0000104721

Secondary structure

...................................... 144
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02413 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 53D14CD948815FD9

FASTA14414,980
        10         20         30         40         50         60 
MRLNTLSPAE GSKKAGKRLG RGIGSGLGKT GGRGHKGQKS RSGGGVRRGF EGGQMPLYRR 

        70         80         90        100        110        120 
LPKFGFTSRK AAITAEIRLS DLAKVEGGVV DLNTLKAANI IGIQIEFAKV ILAGEVTTPV 

       130        140 
TVRGLRVTKG ARAAIEAAGG KIEE 

« Hide

References

« Hide 'large scale' references
[1]"The primary structure of protein L15 located at the peptidyltransferase center of Escherichia coli ribosomes."
Giorginis S., Chen R.
FEBS Lett. 84:347-350(1977) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Strain: K.
[2]"The spc ribosomal protein operon of Escherichia coli: sequence and cotranscription of the ribosomal protein genes and a protein export gene."
Cerretti D.P., Dean D., Davis G.R., Bedwell D.M., Nomura M.
Nucleic Acids Res. 11:2599-2616(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[3]"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.
[4]"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.
[5]"Incorporation of six additional proteins to complete the assembly map of the 50 S subunit from Escherichia coli ribosomes."
Herold M., Nierhaus K.H.
J. Biol. Chem. 262:8826-8833(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSEMBLY MAP OF THE 50S SUBUNIT.
Strain: K12.
[6]"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.
[7]"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).
Strain: MRE-600.
[8]"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.
Strain: MRE-600.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X01563 Genomic DNA. Translation: CAA25724.1.
U18997 Genomic DNA. Translation: AAA58098.1.
U00096 Genomic DNA. Translation: AAC76326.1.
AP009048 Genomic DNA. Translation: BAE77990.1.
PIRR5EC15. A02794.
RefSeqNP_417760.1. NC_000913.3.
YP_492131.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ML5electron microscopy14.00o2-144[»]
1P85electron microscopy12.30J1-144[»]
1P86electron microscopy11.50J1-144[»]
1VS6X-ray3.46L1-144[»]
1VS8X-ray3.46L1-144[»]
1VT2X-ray3.30L1-144[»]
2AW4X-ray3.46L1-144[»]
2AWBX-ray3.46L1-144[»]
2GYAelectron microscopy15.00J4-143[»]
2GYCelectron microscopy15.00J4-143[»]
2I2TX-ray3.22L1-144[»]
2I2VX-ray3.22L1-144[»]
2J28electron microscopy8.00L1-144[»]
2QAMX-ray3.21L1-144[»]
2QAOX-ray3.21L1-144[»]
2QBAX-ray3.54L1-144[»]
2QBCX-ray3.54L1-144[»]
2QBEX-ray3.30L1-144[»]
2QBGX-ray3.30L1-144[»]
2QBIX-ray4.00L1-144[»]
2QBKX-ray4.00L1-144[»]
2QOVX-ray3.93L1-144[»]
2QOXX-ray3.93L1-144[»]
2QOZX-ray3.50L1-144[»]
2QP1X-ray3.50L1-144[»]
2RDOelectron microscopy9.10L1-144[»]
2VHMX-ray3.74L1-144[»]
2VHNX-ray3.74L1-144[»]
2WWQelectron microscopy5.80L2-144[»]
2Z4LX-ray4.45L1-144[»]
2Z4NX-ray4.45L1-144[»]
3BBXelectron microscopy10.00L1-144[»]
3DF2X-ray3.50L1-144[»]
3DF4X-ray3.50L1-144[»]
3E1Belectron microscopy-E1-144[»]
3E1Delectron microscopy-E1-144[»]
3FIKelectron microscopy6.70L2-144[»]
3I1NX-ray3.19L1-144[»]
3I1PX-ray3.19L1-144[»]
3I1RX-ray3.81L1-144[»]
3I1TX-ray3.81L1-144[»]
3I20X-ray3.71L1-144[»]
3I22X-ray3.71L1-144[»]
3IY9electron microscopy14.10L2-144[»]
3IZTelectron microscopy-M1-144[»]
3IZUelectron microscopy-M1-144[»]
3J01electron microscopy-L1-144[»]
3J0Telectron microscopy12.10N1-144[»]
3J0Welectron microscopy14.70N1-144[»]
3J0Yelectron microscopy13.50N1-144[»]
3J11electron microscopy13.10N1-144[»]
3J12electron microscopy11.50N1-144[»]
3J14electron microscopy11.50N1-144[»]
3J19electron microscopy8.30L2-144[»]
3J37electron microscopy9.80P1-144[»]
3J4Xelectron microscopy12.00L1-144[»]
3J50electron microscopy20.00L1-144[»]
3J51electron microscopy17.00L1-144[»]
3J52electron microscopy12.00L1-144[»]
3J54electron microscopy13.00L1-144[»]
3J56electron microscopy15.00L1-144[»]
3J58electron microscopy17.00L1-144[»]
3J5Aelectron microscopy12.00L1-144[»]
3J5Celectron microscopy17.00L1-144[»]
3J5Eelectron microscopy17.00L1-144[»]
3J5Gelectron microscopy20.00L1-144[»]
3J5Ielectron microscopy15.00L1-144[»]
3J5Kelectron microscopy9.00L1-144[»]
3J5Oelectron microscopy6.80L1-144[»]
3J5Uelectron microscopy7.60N1-144[»]
3J5Welectron microscopy7.60O1-144[»]
3KCRelectron microscopy-L1-144[»]
3OASX-ray3.25L2-144[»]
3OATX-ray3.25L2-144[»]
3OFCX-ray3.19L2-144[»]
3OFDX-ray3.19L2-144[»]
3OFQX-ray3.10L2-144[»]
3OFRX-ray3.10L2-144[»]
3OFZX-ray3.29L2-144[»]
3OG0X-ray3.29L2-144[»]
3ORBX-ray3.30L1-144[»]
3R8SX-ray3.00L2-144[»]
3R8TX-ray3.00L2-144[»]
3SGFX-ray3.20P1-144[»]
3UOSX-ray3.70P1-144[»]
4GARX-ray3.30L1-144[»]
4GAUX-ray3.30L1-144[»]
4KIXX-ray2.90L1-144[»]
4KIZX-ray2.90L1-144[»]
4KJ1X-ray2.90L1-144[»]
4KJ3X-ray2.90L1-144[»]
4KJ5X-ray2.90L1-144[»]
4KJ7X-ray2.90L1-144[»]
4KJ9X-ray2.90L1-144[»]
4KJBX-ray2.90L1-144[»]
ProteinModelPortalP02413.
SMRP02413. Positions 2-144.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10752N.
IntActP02413. 78 interactions.
MINTMINT-1260355.
STRING511145.b3301.

Chemistry

ChEMBLCHEMBL2363135.

Proteomic databases

PaxDbP02413.
PRIDEP02413.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76326; AAC76326; b3301.
BAE77990; BAE77990; BAE77990.
GeneID12934400.
947798.
KEGGecj:Y75_p3875.
eco:b3301.
PATRIC32122034. VBIEscCol129921_3394.

Organism-specific databases

EchoBASEEB0869.
EcoGeneEG10876. rplO.

Phylogenomic databases

eggNOGCOG0200.
HOGENOMHOG000231262.
KOK02876.
OMAPWFRRIG.
OrthoDBEOG6CGCM5.
PhylomeDBP02413.
ProtClustDBPRK05592.

Enzyme and pathway databases

BioCycEcoCyc:EG10876-MONOMER.
ECOL316407:JW3263-MONOMER.

Gene expression databases

GenevestigatorP02413.

Family and domain databases

HAMAPMF_01341_B. Ribosomal_L15_B.
InterProIPR005749. Ribosomal_L15_bac-type.
IPR001196. Ribosomal_L15_CS.
IPR021131. Ribosomal_L18e/L15P.
[Graphical view]
PANTHERPTHR12934. PTHR12934. 1 hit.
PfamPF00828. Ribosomal_L18e. 1 hit.
[Graphical view]
SUPFAMSSF52080. SSF52080. 1 hit.
TIGRFAMsTIGR01071. rplO_bact. 1 hit.
PROSITEPS00475. RIBOSOMAL_L15. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP02413.
PROP02413.

Entry information

Entry nameRL15_ECOLI
AccessionPrimary (citable) accession number: P02413
Secondary accession number(s): Q2M6W6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 16, 2014
This is version 144 of the entry and version 1 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