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Protein

50S ribosomal protein L15

Gene

rplO

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. rRNA binding Source: UniProtKB-HAMAP
  2. structural constituent of ribosome Source: GO_Central

GO - Biological processi

  1. translation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10876-MONOMER.
ECOL316407:JW3263-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L15
Gene namesi
Name:rplO
Ordered Locus Names:b3301, JW3263
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10876. rplO.

Subcellular locationi

GO - Cellular componenti

  1. cytosolic large ribosomal subunit Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14414450S ribosomal protein L15PRO_0000104721Add
BLAST

Proteomic databases

PaxDbiP02413.
PRIDEiP02413.

Expressioni

Gene expression databases

GenevestigatoriP02413.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
rlmNP369793EBI-543017,EBI-559071

Protein-protein interaction databases

DIPiDIP-10752N.
IntActiP02413. 78 interactions.
MINTiMINT-1260355.
STRINGi511145.b3301.

Structurei

Secondary structure

1
144
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni3 – 53Combined sources
Beta strandi10 – 134Combined sources
Turni23 – 253Combined sources
Turni29 – 324Combined sources
Beta strandi35 – 373Combined sources
Helixi38 – 403Combined sources
Beta strandi41 – 433Combined sources
Beta strandi47 – 493Combined sources
Beta strandi52 – 543Combined sources
Helixi57 – 604Combined sources
Turni70 – 734Combined sources
Beta strandi74 – 785Combined sources
Turni79 – 846Combined sources
Beta strandi85 – 906Combined sources
Helixi92 – 954Combined sources
Turni96 – 994Combined sources
Beta strandi103 – 1053Combined sources
Beta strandi107 – 1126Combined sources
Beta strandi121 – 1244Combined sources
Helixi129 – 1379Combined sources
Beta strandi141 – 1433Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ML5electron microscopy14.00o2-144[»]
2J28electron microscopy8.00L1-144[»]
2RDOelectron microscopy9.10L1-144[»]
3BBXelectron microscopy10.00L1-144[»]
3IY9electron microscopy14.10L2-144[»]
3J5Lelectron microscopy6.60L2-144[»]
3J7Zelectron microscopy3.90L1-144[»]
3J8Gelectron microscopy5.00L1-144[»]
4CSUelectron microscopy5.50L2-144[»]
4U1UX-ray2.95BL/DL2-144[»]
4U1VX-ray3.00BL/DL2-144[»]
4U20X-ray2.90BL/DL2-144[»]
4U24X-ray2.90BL/DL2-144[»]
4U25X-ray2.90BL/DL2-144[»]
4U26X-ray2.80BL/DL2-144[»]
4U27X-ray2.80BL/DL2-144[»]
4UY8electron microscopy3.80L2-144[»]
4V47electron microscopy12.30AJ1-144[»]
4V48electron microscopy11.50AJ1-144[»]
4V4HX-ray3.46BL/DL1-144[»]
4V4QX-ray3.46BL/DL1-144[»]
4V4Velectron microscopy15.00BJ4-143[»]
4V4Welectron microscopy15.00BJ4-143[»]
4V50X-ray3.22BL/DL1-144[»]
4V52X-ray3.21BL/DL1-144[»]
4V53X-ray3.54BL/DL1-144[»]
4V54X-ray3.30BL/DL1-144[»]
4V55X-ray4.00BL/DL1-144[»]
4V56X-ray3.93BL/DL1-144[»]
4V57X-ray3.50BL/DL1-144[»]
4V5BX-ray3.74AL/CL1-144[»]
4V5Helectron microscopy5.80BL2-144[»]
4V5YX-ray4.45BL/DL1-144[»]
4V64X-ray3.50BL/DL1-144[»]
4V65electron microscopy9.00BE1-144[»]
4V66electron microscopy9.00BE1-144[»]
4V69electron microscopy6.70BL2-144[»]
4V6CX-ray3.19BL/DL1-144[»]
4V6DX-ray3.81BL/DL1-144[»]
4V6EX-ray3.71BL/DL1-144[»]
4V6Kelectron microscopy8.25AM1-144[»]
4V6Lelectron microscopy13.20BM1-144[»]
4V6Melectron microscopy7.10BL1-144[»]
4V6Nelectron microscopy12.10AN1-144[»]
4V6Oelectron microscopy14.70BN1-144[»]
4V6Pelectron microscopy13.50BN1-144[»]
4V6Qelectron microscopy11.50BN1-144[»]
4V6Relectron microscopy11.50BN1-144[»]
4V6Selectron microscopy13.10AN1-144[»]
4V6Telectron microscopy8.30BL2-144[»]
4V6Velectron microscopy9.80BP1-144[»]
4V6Yelectron microscopy12.00BL1-144[»]
4V6Zelectron microscopy12.00BL1-144[»]
4V70electron microscopy17.00BL1-144[»]
4V71electron microscopy20.00BL1-144[»]
4V72electron microscopy13.00BL1-144[»]
4V73electron microscopy15.00BL1-144[»]
4V74electron microscopy17.00BL1-144[»]
4V75electron microscopy12.00BL1-144[»]
4V76electron microscopy17.00BL1-144[»]
4V77electron microscopy17.00BL1-144[»]
4V78electron microscopy20.00BL1-144[»]
4V79electron microscopy15.00BL1-144[»]
4V7Aelectron microscopy9.00BL1-144[»]
4V7Belectron microscopy6.80BL1-144[»]
4V7Celectron microscopy7.60BN1-144[»]
4V7Delectron microscopy7.60AO1-144[»]
4V7Ielectron microscopy9.60AL1-144[»]
4V7SX-ray3.25BL/DL2-144[»]
4V7TX-ray3.19BL/DL2-144[»]
4V7UX-ray3.10BL/DL2-144[»]
4V7VX-ray3.29BL/DL2-144[»]
4V85X-ray3.20P1-144[»]
4V89X-ray3.70BP1-144[»]
4V9CX-ray3.30BL/DL1-144[»]
4V9DX-ray3.00CL/DL2-144[»]
4V9OX-ray2.90AL/CL/EL/GL1-144[»]
4V9PX-ray2.90AL/CL/EL/GL1-144[»]
4WF1X-ray3.09BL/DL2-144[»]
4WWWX-ray3.10RL/YL2-144[»]
5AFIelectron microscopy2.90L1-144[»]
ProteinModelPortaliP02413.
SMRiP02413. Positions 2-144.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02413.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L15P family.Curated

Phylogenomic databases

eggNOGiCOG0200.
HOGENOMiHOG000231262.
InParanoidiP02413.
KOiK02876.
OMAiRGHKGLK.
OrthoDBiEOG6CGCM5.
PhylomeDBiP02413.

Family and domain databases

HAMAPiMF_01341. Ribosomal_L15.
InterProiIPR030878. Ribosomal_L15.
IPR005749. Ribosomal_L15_bac-type.
IPR001196. Ribosomal_L15_CS.
IPR021131. Ribosomal_L18e/L15P.
[Graphical view]
PANTHERiPTHR12934. PTHR12934. 1 hit.
PfamiPF00828. Ribosomal_L18e. 1 hit.
[Graphical view]
SUPFAMiSSF52080. SSF52080. 1 hit.
TIGRFAMsiTIGR01071. rplO_bact. 1 hit.
PROSITEiPS00475. RIBOSOMAL_L15. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P02413-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLNTLSPAE GSKKAGKRLG RGIGSGLGKT GGRGHKGQKS RSGGGVRRGF
60 70 80 90 100
EGGQMPLYRR LPKFGFTSRK AAITAEIRLS DLAKVEGGVV DLNTLKAANI
110 120 130 140
IGIQIEFAKV ILAGEVTTPV TVRGLRVTKG ARAAIEAAGG KIEE
Length:144
Mass (Da):14,980
Last modified:July 21, 1986 - v1
Checksum:i53D14CD948815FD9
GO

Mass spectrometryi

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01563 Genomic DNA. Translation: CAA25724.1.
U18997 Genomic DNA. Translation: AAA58098.1.
U00096 Genomic DNA. Translation: AAC76326.1.
AP009048 Genomic DNA. Translation: BAE77990.1.
PIRiA02794. R5EC15.
RefSeqiNP_417760.1. NC_000913.3.
YP_492131.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76326; AAC76326; b3301.
BAE77990; BAE77990; BAE77990.
GeneIDi12934400.
947798.
KEGGiecj:Y75_p3875.
eco:b3301.
PATRICi32122034. VBIEscCol129921_3394.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01563 Genomic DNA. Translation: CAA25724.1.
U18997 Genomic DNA. Translation: AAA58098.1.
U00096 Genomic DNA. Translation: AAC76326.1.
AP009048 Genomic DNA. Translation: BAE77990.1.
PIRiA02794. R5EC15.
RefSeqiNP_417760.1. NC_000913.3.
YP_492131.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ML5electron microscopy14.00o2-144[»]
2J28electron microscopy8.00L1-144[»]
2RDOelectron microscopy9.10L1-144[»]
3BBXelectron microscopy10.00L1-144[»]
3IY9electron microscopy14.10L2-144[»]
3J5Lelectron microscopy6.60L2-144[»]
3J7Zelectron microscopy3.90L1-144[»]
3J8Gelectron microscopy5.00L1-144[»]
4CSUelectron microscopy5.50L2-144[»]
4U1UX-ray2.95BL/DL2-144[»]
4U1VX-ray3.00BL/DL2-144[»]
4U20X-ray2.90BL/DL2-144[»]
4U24X-ray2.90BL/DL2-144[»]
4U25X-ray2.90BL/DL2-144[»]
4U26X-ray2.80BL/DL2-144[»]
4U27X-ray2.80BL/DL2-144[»]
4UY8electron microscopy3.80L2-144[»]
4V47electron microscopy12.30AJ1-144[»]
4V48electron microscopy11.50AJ1-144[»]
4V4HX-ray3.46BL/DL1-144[»]
4V4QX-ray3.46BL/DL1-144[»]
4V4Velectron microscopy15.00BJ4-143[»]
4V4Welectron microscopy15.00BJ4-143[»]
4V50X-ray3.22BL/DL1-144[»]
4V52X-ray3.21BL/DL1-144[»]
4V53X-ray3.54BL/DL1-144[»]
4V54X-ray3.30BL/DL1-144[»]
4V55X-ray4.00BL/DL1-144[»]
4V56X-ray3.93BL/DL1-144[»]
4V57X-ray3.50BL/DL1-144[»]
4V5BX-ray3.74AL/CL1-144[»]
4V5Helectron microscopy5.80BL2-144[»]
4V5YX-ray4.45BL/DL1-144[»]
4V64X-ray3.50BL/DL1-144[»]
4V65electron microscopy9.00BE1-144[»]
4V66electron microscopy9.00BE1-144[»]
4V69electron microscopy6.70BL2-144[»]
4V6CX-ray3.19BL/DL1-144[»]
4V6DX-ray3.81BL/DL1-144[»]
4V6EX-ray3.71BL/DL1-144[»]
4V6Kelectron microscopy8.25AM1-144[»]
4V6Lelectron microscopy13.20BM1-144[»]
4V6Melectron microscopy7.10BL1-144[»]
4V6Nelectron microscopy12.10AN1-144[»]
4V6Oelectron microscopy14.70BN1-144[»]
4V6Pelectron microscopy13.50BN1-144[»]
4V6Qelectron microscopy11.50BN1-144[»]
4V6Relectron microscopy11.50BN1-144[»]
4V6Selectron microscopy13.10AN1-144[»]
4V6Telectron microscopy8.30BL2-144[»]
4V6Velectron microscopy9.80BP1-144[»]
4V6Yelectron microscopy12.00BL1-144[»]
4V6Zelectron microscopy12.00BL1-144[»]
4V70electron microscopy17.00BL1-144[»]
4V71electron microscopy20.00BL1-144[»]
4V72electron microscopy13.00BL1-144[»]
4V73electron microscopy15.00BL1-144[»]
4V74electron microscopy17.00BL1-144[»]
4V75electron microscopy12.00BL1-144[»]
4V76electron microscopy17.00BL1-144[»]
4V77electron microscopy17.00BL1-144[»]
4V78electron microscopy20.00BL1-144[»]
4V79electron microscopy15.00BL1-144[»]
4V7Aelectron microscopy9.00BL1-144[»]
4V7Belectron microscopy6.80BL1-144[»]
4V7Celectron microscopy7.60BN1-144[»]
4V7Delectron microscopy7.60AO1-144[»]
4V7Ielectron microscopy9.60AL1-144[»]
4V7SX-ray3.25BL/DL2-144[»]
4V7TX-ray3.19BL/DL2-144[»]
4V7UX-ray3.10BL/DL2-144[»]
4V7VX-ray3.29BL/DL2-144[»]
4V85X-ray3.20P1-144[»]
4V89X-ray3.70BP1-144[»]
4V9CX-ray3.30BL/DL1-144[»]
4V9DX-ray3.00CL/DL2-144[»]
4V9OX-ray2.90AL/CL/EL/GL1-144[»]
4V9PX-ray2.90AL/CL/EL/GL1-144[»]
4WF1X-ray3.09BL/DL2-144[»]
4WWWX-ray3.10RL/YL2-144[»]
5AFIelectron microscopy2.90L1-144[»]
ProteinModelPortaliP02413.
SMRiP02413. Positions 2-144.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-10752N.
IntActiP02413. 78 interactions.
MINTiMINT-1260355.
STRINGi511145.b3301.

Chemistry

ChEMBLiCHEMBL2363135.

Proteomic databases

PaxDbiP02413.
PRIDEiP02413.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76326; AAC76326; b3301.
BAE77990; BAE77990; BAE77990.
GeneIDi12934400.
947798.
KEGGiecj:Y75_p3875.
eco:b3301.
PATRICi32122034. VBIEscCol129921_3394.

Organism-specific databases

EchoBASEiEB0869.
EcoGeneiEG10876. rplO.

Phylogenomic databases

eggNOGiCOG0200.
HOGENOMiHOG000231262.
InParanoidiP02413.
KOiK02876.
OMAiRGHKGLK.
OrthoDBiEOG6CGCM5.
PhylomeDBiP02413.

Enzyme and pathway databases

BioCyciEcoCyc:EG10876-MONOMER.
ECOL316407:JW3263-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP02413.
PROiP02413.

Gene expression databases

GenevestigatoriP02413.

Family and domain databases

HAMAPiMF_01341. Ribosomal_L15.
InterProiIPR030878. Ribosomal_L15.
IPR005749. Ribosomal_L15_bac-type.
IPR001196. Ribosomal_L15_CS.
IPR021131. Ribosomal_L18e/L15P.
[Graphical view]
PANTHERiPTHR12934. PTHR12934. 1 hit.
PfamiPF00828. Ribosomal_L18e. 1 hit.
[Graphical view]
SUPFAMiSSF52080. SSF52080. 1 hit.
TIGRFAMsiTIGR01071. rplO_bact. 1 hit.
PROSITEiPS00475. RIBOSOMAL_L15. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.

Entry informationi

Entry nameiRL15_ECOLI
AccessioniPrimary (citable) accession number: P02413
Secondary accession number(s): Q2M6W6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 29, 2015
This is version 155 of the entry and version 1 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.