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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.1 Publication

GO - Molecular functioni

GO - Biological processi

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.
MetaCyc:EG10876-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10876. rplO.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001047211 – 14450S ribosomal protein L15Add BLAST144

Proteomic databases

EPDiP02413.
PaxDbiP02413.
PRIDEiP02413.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Contacts the 5S rRNA.1 Publication

Binary interactionsi

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

Protein-protein interaction databases

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

Structurei

Secondary structure

1144
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni3 – 5Combined sources3
Beta strandi10 – 13Combined sources4
Turni23 – 25Combined sources3
Turni29 – 32Combined sources4
Beta strandi35 – 37Combined sources3
Helixi38 – 40Combined sources3
Beta strandi41 – 43Combined sources3
Beta strandi47 – 49Combined sources3
Beta strandi52 – 54Combined sources3
Helixi57 – 60Combined sources4
Turni70 – 73Combined sources4
Beta strandi74 – 78Combined sources5
Turni79 – 84Combined sources6
Beta strandi85 – 90Combined sources6
Helixi92 – 95Combined sources4
Turni96 – 99Combined sources4
Beta strandi103 – 105Combined sources3
Beta strandi107 – 112Combined sources6
Beta strandi121 – 124Combined sources4
Helixi129 – 137Combined sources9
Beta strandi141 – 143Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
3J9Yelectron microscopy3.90L1-144[»]
3J9Zelectron microscopy3.60LH1-144[»]
3JA1electron microscopy3.60LN1-144[»]
3JBUelectron microscopy3.64l1-144[»]
3JBVelectron microscopy3.32l1-144[»]
3JCDelectron microscopy3.70L1-144[»]
3JCEelectron microscopy3.20L1-144[»]
3JCJelectron microscopy3.70K1-144[»]
3JCNelectron microscopy4.60L1-144[»]
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[»]
4WOIX-ray3.00BL/CL1-144[»]
4WWWX-ray3.10RL/YL2-144[»]
4YBBX-ray2.10CM/DM1-144[»]
5ADYelectron microscopy4.50L1-144[»]
5AFIelectron microscopy2.90L1-144[»]
5AKAelectron microscopy5.70L1-144[»]
5GADelectron microscopy3.70M1-144[»]
5GAEelectron microscopy3.33M1-144[»]
5GAFelectron microscopy4.30M1-144[»]
5GAGelectron microscopy3.80M1-144[»]
5GAHelectron microscopy3.80M1-144[»]
5IQRelectron microscopy3.00L1-144[»]
5IT8X-ray3.12CM/DM1-144[»]
5J5BX-ray2.80CM/DM1-144[»]
5J7LX-ray3.00CM/DM1-144[»]
5J88X-ray3.32CM/DM1-144[»]
5J8AX-ray3.10CM/DM1-144[»]
5J91X-ray2.96CM/DM1-144[»]
5JC9X-ray3.03CM/DM1-144[»]
5JTEelectron microscopy3.60BL1-144[»]
5JU8electron microscopy3.60BL1-144[»]
5KCRelectron microscopy3.601P1-144[»]
5KCSelectron microscopy3.901P1-144[»]
5KPSelectron microscopy3.90L1-144[»]
5KPVelectron microscopy4.10K1-144[»]
5KPWelectron microscopy3.90K1-144[»]
5KPXelectron microscopy3.90K1-144[»]
5L3Pelectron microscopy3.70P1-144[»]
ProteinModelPortaliP02413.
SMRiP02413.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02413.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L15P family.Curated

Phylogenomic databases

eggNOGiENOG4108UZ0. Bacteria.
COG0200. LUCA.
HOGENOMiHOG000231262.
InParanoidiP02413.
KOiK02876.
OMAiRGHKGLK.
PhylomeDBiP02413.

Family and domain databases

HAMAPiMF_01341. Ribosomal_L15. 1 hit.
InterProiIPR030878. Ribosomal_L15.
IPR005749. Ribosomal_L15_bac-type.
IPR001196. Ribosomal_L15_CS.
IPR021131. Ribosomal_L18e/L15P.
[Graphical view]
PANTHERiPTHR12934. PTHR12934. 1 hit.
PfamiPF00828. Ribosomal_L27A. 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.
WP_001238914.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76326; AAC76326; b3301.
BAE77990; BAE77990; BAE77990.
GeneIDi947798.
KEGGiecj:JW3263.
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.
WP_001238914.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
3J9Yelectron microscopy3.90L1-144[»]
3J9Zelectron microscopy3.60LH1-144[»]
3JA1electron microscopy3.60LN1-144[»]
3JBUelectron microscopy3.64l1-144[»]
3JBVelectron microscopy3.32l1-144[»]
3JCDelectron microscopy3.70L1-144[»]
3JCEelectron microscopy3.20L1-144[»]
3JCJelectron microscopy3.70K1-144[»]
3JCNelectron microscopy4.60L1-144[»]
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[»]
4WOIX-ray3.00BL/CL1-144[»]
4WWWX-ray3.10RL/YL2-144[»]
4YBBX-ray2.10CM/DM1-144[»]
5ADYelectron microscopy4.50L1-144[»]
5AFIelectron microscopy2.90L1-144[»]
5AKAelectron microscopy5.70L1-144[»]
5GADelectron microscopy3.70M1-144[»]
5GAEelectron microscopy3.33M1-144[»]
5GAFelectron microscopy4.30M1-144[»]
5GAGelectron microscopy3.80M1-144[»]
5GAHelectron microscopy3.80M1-144[»]
5IQRelectron microscopy3.00L1-144[»]
5IT8X-ray3.12CM/DM1-144[»]
5J5BX-ray2.80CM/DM1-144[»]
5J7LX-ray3.00CM/DM1-144[»]
5J88X-ray3.32CM/DM1-144[»]
5J8AX-ray3.10CM/DM1-144[»]
5J91X-ray2.96CM/DM1-144[»]
5JC9X-ray3.03CM/DM1-144[»]
5JTEelectron microscopy3.60BL1-144[»]
5JU8electron microscopy3.60BL1-144[»]
5KCRelectron microscopy3.601P1-144[»]
5KCSelectron microscopy3.901P1-144[»]
5KPSelectron microscopy3.90L1-144[»]
5KPVelectron microscopy4.10K1-144[»]
5KPWelectron microscopy3.90K1-144[»]
5KPXelectron microscopy3.90K1-144[»]
5L3Pelectron microscopy3.70P1-144[»]
ProteinModelPortaliP02413.
SMRiP02413.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

EPDiP02413.
PaxDbiP02413.
PRIDEiP02413.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76326; AAC76326; b3301.
BAE77990; BAE77990; BAE77990.
GeneIDi947798.
KEGGiecj:JW3263.
eco:b3301.
PATRICi32122034. VBIEscCol129921_3394.

Organism-specific databases

EchoBASEiEB0869.
EcoGeneiEG10876. rplO.

Phylogenomic databases

eggNOGiENOG4108UZ0. Bacteria.
COG0200. LUCA.
HOGENOMiHOG000231262.
InParanoidiP02413.
KOiK02876.
OMAiRGHKGLK.
PhylomeDBiP02413.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP02413.
PROiP02413.

Family and domain databases

HAMAPiMF_01341. Ribosomal_L15. 1 hit.
InterProiIPR030878. Ribosomal_L15.
IPR005749. Ribosomal_L15_bac-type.
IPR001196. Ribosomal_L15_CS.
IPR021131. Ribosomal_L18e/L15P.
[Graphical view]
PANTHERiPTHR12934. PTHR12934. 1 hit.
PfamiPF00828. Ribosomal_L27A. 1 hit.
[Graphical view]
SUPFAMiSSF52080. SSF52080. 1 hit.
TIGRFAMsiTIGR01071. rplO_bact. 1 hit.
PROSITEiPS00475. RIBOSOMAL_L15. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 169 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

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 one 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.