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Protein

50S ribosomal protein L25

Gene

rplY

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance. Binds to the 5S rRNA independently of L5 and L18. Not required for binding of the 5S rRNA/L5/L18 subcomplex to 23S rRNA.3 Publications

GO - Molecular functioni

  • 5S rRNA binding Source: EcoCyc
  • structural constituent of ribosome Source: InterPro

GO - Biological processi

  • negative regulation of translation Source: EcoCyc
  • translation Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10885-MONOMER.
ECOL316407:JW2173-MONOMER.
MetaCyc:EG10885-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L25
Gene namesi
Name:rplY
Ordered Locus Names:b2185, JW2173
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10885. rplY.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001814781 – 9450S ribosomal protein L25Add BLAST94

Proteomic databases

EPDiP68919.
PaxDbiP68919.
PRIDEiP68919.

2D gel databases

SWISS-2DPAGEP68919.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18/L25 subcomplex. Contacts the 5S rRNA.6 Publications

Protein-protein interaction databases

DIPiDIP-35885N.
IntActiP68919. 13 interactors.
MINTiMINT-1261165.
STRINGi511145.b2185.

Structurei

Secondary structure

194
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 5Combined sources3
Beta strandi6 – 8Combined sources3
Helixi14 – 22Combined sources9
Beta strandi25 – 31Combined sources7
Beta strandi33 – 35Combined sources3
Beta strandi38 – 43Combined sources6
Helixi44 – 50Combined sources7
Helixi54 – 57Combined sources4
Beta strandi61 – 65Combined sources5
Beta strandi72 – 79Combined sources8
Beta strandi81 – 84Combined sources4
Beta strandi86 – 93Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B75NMR-A1-94[»]
1D6KNMR-A1-94[»]
1DFUX-ray1.80P1-94[»]
1ML5electron microscopy14.00v1-94[»]
2J28electron microscopy8.00V1-94[»]
2RDOelectron microscopy9.10V1-94[»]
3BBXelectron microscopy10.00V1-94[»]
3J5Lelectron microscopy6.60V1-94[»]
3J7Zelectron microscopy3.90V1-94[»]
3J8Gelectron microscopy5.00W1-94[»]
3J9Yelectron microscopy3.90V1-94[»]
3J9Zelectron microscopy3.60LT1-94[»]
3JA1electron microscopy3.60LX1-94[»]
3JBUelectron microscopy3.64w1-94[»]
3JBVelectron microscopy3.32w1-94[»]
3JCDelectron microscopy3.70V1-94[»]
3JCEelectron microscopy3.20V1-94[»]
3JCJelectron microscopy3.70U1-94[»]
3JCNelectron microscopy4.60V1-94[»]
487Delectron microscopy7.50N1-94[»]
4CSUelectron microscopy5.50W1-94[»]
4U1UX-ray2.95BV/DV1-94[»]
4U1VX-ray3.00BV/DV1-94[»]
4U20X-ray2.90BV/DV1-94[»]
4U24X-ray2.90BV/DV1-94[»]
4U25X-ray2.90BV/DV1-94[»]
4U26X-ray2.80BV/DV1-94[»]
4U27X-ray2.80BV/DV1-94[»]
4UY8electron microscopy3.8081-94[»]
4V47electron microscopy12.30AT1-94[»]
4V48electron microscopy11.50AT1-94[»]
4V4HX-ray3.46BV/DV1-94[»]
4V4QX-ray3.46BV/DV1-94[»]
4V4Velectron microscopy15.00BT1-94[»]
4V4Welectron microscopy15.00BT1-94[»]
4V50X-ray3.22BV/DV1-94[»]
4V52X-ray3.21BV/DV1-94[»]
4V53X-ray3.54BV/DV1-94[»]
4V54X-ray3.30BV/DV1-94[»]
4V55X-ray4.00BV/DV1-94[»]
4V56X-ray3.93BV/DV1-94[»]
4V57X-ray3.50BV/DV1-94[»]
4V5BX-ray3.74AV/CV1-94[»]
4V5Helectron microscopy5.80BW1-94[»]
4V5YX-ray4.45BV/DV1-94[»]
4V64X-ray3.50BV/DV1-94[»]
4V65electron microscopy9.00BC1-94[»]
4V66electron microscopy9.00BC1-94[»]
4V69electron microscopy6.70BV1-94[»]
4V6CX-ray3.19BV/DV1-94[»]
4V6DX-ray3.81BV/DV1-94[»]
4V6EX-ray3.71BV/DV1-94[»]
4V6Kelectron microscopy8.25AW1-94[»]
4V6Lelectron microscopy13.20BW1-94[»]
4V6Melectron microscopy7.10BV1-94[»]
4V6Nelectron microscopy12.10AX1-94[»]
4V6Oelectron microscopy14.70BX1-94[»]
4V6Pelectron microscopy13.50BX1-94[»]
4V6Qelectron microscopy11.50BX1-94[»]
4V6Relectron microscopy11.50BX1-94[»]
4V6Selectron microscopy13.10AX1-94[»]
4V6Telectron microscopy8.30BV1-94[»]
4V6Velectron microscopy9.80BZ1-94[»]
4V6Yelectron microscopy12.00BV1-94[»]
4V6Zelectron microscopy12.00BV1-94[»]
4V70electron microscopy17.00BV1-94[»]
4V71electron microscopy20.00BV1-94[»]
4V72electron microscopy13.00BV1-94[»]
4V73electron microscopy15.00BV1-94[»]
4V74electron microscopy17.00BV1-94[»]
4V75electron microscopy12.00BV1-94[»]
4V76electron microscopy17.00BV1-94[»]
4V77electron microscopy17.00BV1-94[»]
4V78electron microscopy20.00BV1-94[»]
4V79electron microscopy15.00BV1-94[»]
4V7Aelectron microscopy9.00BV1-94[»]
4V7Belectron microscopy6.80BV1-94[»]
4V7Celectron microscopy7.60BX1-94[»]
4V7Delectron microscopy7.60AY1-94[»]
4V7Ielectron microscopy9.60AV1-94[»]
4V7SX-ray3.25BV/DV1-94[»]
4V7TX-ray3.19BV/DV1-94[»]
4V7UX-ray3.10BV/DV1-94[»]
4V7VX-ray3.29BV/DV1-94[»]
4V85X-ray3.20Z1-94[»]
4V89X-ray3.70BZ1-94[»]
4V9CX-ray3.30BV/DV1-94[»]
4V9DX-ray3.00CV/DV1-94[»]
4V9OX-ray2.90AV/CV/EV/GV1-94[»]
4V9PX-ray2.90AV/CV/EV/GV1-94[»]
4WF1X-ray3.09BV/DV1-94[»]
4WOIX-ray3.00BV/CV1-94[»]
4WWWX-ray3.10RV/YV1-94[»]
4YBBX-ray2.10CW/DW1-94[»]
5ADYelectron microscopy4.50V1-94[»]
5AFIelectron microscopy2.90V1-94[»]
5AKAelectron microscopy5.70V1-94[»]
5GADelectron microscopy3.70W1-94[»]
5GAEelectron microscopy3.33W1-94[»]
5GAFelectron microscopy4.30W1-94[»]
5GAGelectron microscopy3.80W1-94[»]
5GAHelectron microscopy3.80W1-94[»]
5IQRelectron microscopy3.00V1-94[»]
5IT8X-ray3.12CW/DW1-94[»]
5J5BX-ray2.80CW/DW1-94[»]
5J7LX-ray3.00CW/DW1-94[»]
5J88X-ray3.32CW/DW1-94[»]
5J8AX-ray3.10CW/DW1-94[»]
5J91X-ray2.96CW/DW1-94[»]
5JC9X-ray3.03CW/DW1-94[»]
5JTEelectron microscopy3.60BV1-94[»]
5JU8electron microscopy3.60BV1-94[»]
5KCRelectron microscopy3.601Z1-94[»]
5KCSelectron microscopy3.901Z1-94[»]
5KPSelectron microscopy3.90V1-94[»]
5KPVelectron microscopy4.10U1-94[»]
5KPWelectron microscopy3.90U1-94[»]
5KPXelectron microscopy3.90U1-94[»]
5L3Pelectron microscopy3.70Z1-94[»]
ProteinModelPortaliP68919.
SMRiP68919.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP68919.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L25P family.Curated

Phylogenomic databases

eggNOGiENOG4105KW6. Bacteria.
COG1825. LUCA.
HOGENOMiHOG000277629.
KOiK02897.
OMAiHAGKFPA.
PhylomeDBiP68919.

Family and domain databases

CDDicd00495. Ribosomal_L25_TL5_CTC. 1 hit.
Gene3Di2.40.240.10. 1 hit.
HAMAPiMF_01336. Ribosomal_L25. 1 hit.
InterProiIPR020056. Rbsml_L25/Gln-tRNA_synth_b-brl.
IPR029751. Ribosomal_L25.
IPR011035. Ribosomal_L25/Gln-tRNA_synth.
IPR020055. Ribosomal_L25_short.
[Graphical view]
PfamiPF01386. Ribosomal_L25p. 1 hit.
[Graphical view]
ProDomiPD012503. Ribosomal_L25. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF50715. SSF50715. 1 hit.

Sequencei

Sequence statusi: Complete.

P68919-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFTINAEVRK EQGKGASRRL RAANKFPAII YGGKEAPLAI ELDHDKVMNM
60 70 80 90
QAKAEFYSEV LTIVVDGKEI KVKAQDVQRH PYKPKLQHID FVRA
Length:94
Mass (Da):10,693
Last modified:July 21, 1986 - v1
Checksum:i85DAF5ACBA1C5F86
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti86 – 94LQHIDFVRA → CSTSTSFALNC in AAA16413 (Ref. 6) Curated9

Mass spectrometryi

Molecular mass is 10693.4 Da from positions 1 - 94. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13326 Genomic DNA. Translation: BAA02585.1.
U00008 Genomic DNA. Translation: AAA16413.1.
U00096 Genomic DNA. Translation: AAC75246.1.
AP009048 Genomic DNA. Translation: BAE76650.1.
PIRiS16002. R5EC25.
RefSeqiNP_416690.1. NC_000913.3.
WP_000494183.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75246; AAC75246; b2185.
BAE76650; BAE76650; BAE76650.
GeneIDi945618.
KEGGiecj:JW2173.
eco:b2185.
PATRICi32119725. VBIEscCol129921_2273.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13326 Genomic DNA. Translation: BAA02585.1.
U00008 Genomic DNA. Translation: AAA16413.1.
U00096 Genomic DNA. Translation: AAC75246.1.
AP009048 Genomic DNA. Translation: BAE76650.1.
PIRiS16002. R5EC25.
RefSeqiNP_416690.1. NC_000913.3.
WP_000494183.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B75NMR-A1-94[»]
1D6KNMR-A1-94[»]
1DFUX-ray1.80P1-94[»]
1ML5electron microscopy14.00v1-94[»]
2J28electron microscopy8.00V1-94[»]
2RDOelectron microscopy9.10V1-94[»]
3BBXelectron microscopy10.00V1-94[»]
3J5Lelectron microscopy6.60V1-94[»]
3J7Zelectron microscopy3.90V1-94[»]
3J8Gelectron microscopy5.00W1-94[»]
3J9Yelectron microscopy3.90V1-94[»]
3J9Zelectron microscopy3.60LT1-94[»]
3JA1electron microscopy3.60LX1-94[»]
3JBUelectron microscopy3.64w1-94[»]
3JBVelectron microscopy3.32w1-94[»]
3JCDelectron microscopy3.70V1-94[»]
3JCEelectron microscopy3.20V1-94[»]
3JCJelectron microscopy3.70U1-94[»]
3JCNelectron microscopy4.60V1-94[»]
487Delectron microscopy7.50N1-94[»]
4CSUelectron microscopy5.50W1-94[»]
4U1UX-ray2.95BV/DV1-94[»]
4U1VX-ray3.00BV/DV1-94[»]
4U20X-ray2.90BV/DV1-94[»]
4U24X-ray2.90BV/DV1-94[»]
4U25X-ray2.90BV/DV1-94[»]
4U26X-ray2.80BV/DV1-94[»]
4U27X-ray2.80BV/DV1-94[»]
4UY8electron microscopy3.8081-94[»]
4V47electron microscopy12.30AT1-94[»]
4V48electron microscopy11.50AT1-94[»]
4V4HX-ray3.46BV/DV1-94[»]
4V4QX-ray3.46BV/DV1-94[»]
4V4Velectron microscopy15.00BT1-94[»]
4V4Welectron microscopy15.00BT1-94[»]
4V50X-ray3.22BV/DV1-94[»]
4V52X-ray3.21BV/DV1-94[»]
4V53X-ray3.54BV/DV1-94[»]
4V54X-ray3.30BV/DV1-94[»]
4V55X-ray4.00BV/DV1-94[»]
4V56X-ray3.93BV/DV1-94[»]
4V57X-ray3.50BV/DV1-94[»]
4V5BX-ray3.74AV/CV1-94[»]
4V5Helectron microscopy5.80BW1-94[»]
4V5YX-ray4.45BV/DV1-94[»]
4V64X-ray3.50BV/DV1-94[»]
4V65electron microscopy9.00BC1-94[»]
4V66electron microscopy9.00BC1-94[»]
4V69electron microscopy6.70BV1-94[»]
4V6CX-ray3.19BV/DV1-94[»]
4V6DX-ray3.81BV/DV1-94[»]
4V6EX-ray3.71BV/DV1-94[»]
4V6Kelectron microscopy8.25AW1-94[»]
4V6Lelectron microscopy13.20BW1-94[»]
4V6Melectron microscopy7.10BV1-94[»]
4V6Nelectron microscopy12.10AX1-94[»]
4V6Oelectron microscopy14.70BX1-94[»]
4V6Pelectron microscopy13.50BX1-94[»]
4V6Qelectron microscopy11.50BX1-94[»]
4V6Relectron microscopy11.50BX1-94[»]
4V6Selectron microscopy13.10AX1-94[»]
4V6Telectron microscopy8.30BV1-94[»]
4V6Velectron microscopy9.80BZ1-94[»]
4V6Yelectron microscopy12.00BV1-94[»]
4V6Zelectron microscopy12.00BV1-94[»]
4V70electron microscopy17.00BV1-94[»]
4V71electron microscopy20.00BV1-94[»]
4V72electron microscopy13.00BV1-94[»]
4V73electron microscopy15.00BV1-94[»]
4V74electron microscopy17.00BV1-94[»]
4V75electron microscopy12.00BV1-94[»]
4V76electron microscopy17.00BV1-94[»]
4V77electron microscopy17.00BV1-94[»]
4V78electron microscopy20.00BV1-94[»]
4V79electron microscopy15.00BV1-94[»]
4V7Aelectron microscopy9.00BV1-94[»]
4V7Belectron microscopy6.80BV1-94[»]
4V7Celectron microscopy7.60BX1-94[»]
4V7Delectron microscopy7.60AY1-94[»]
4V7Ielectron microscopy9.60AV1-94[»]
4V7SX-ray3.25BV/DV1-94[»]
4V7TX-ray3.19BV/DV1-94[»]
4V7UX-ray3.10BV/DV1-94[»]
4V7VX-ray3.29BV/DV1-94[»]
4V85X-ray3.20Z1-94[»]
4V89X-ray3.70BZ1-94[»]
4V9CX-ray3.30BV/DV1-94[»]
4V9DX-ray3.00CV/DV1-94[»]
4V9OX-ray2.90AV/CV/EV/GV1-94[»]
4V9PX-ray2.90AV/CV/EV/GV1-94[»]
4WF1X-ray3.09BV/DV1-94[»]
4WOIX-ray3.00BV/CV1-94[»]
4WWWX-ray3.10RV/YV1-94[»]
4YBBX-ray2.10CW/DW1-94[»]
5ADYelectron microscopy4.50V1-94[»]
5AFIelectron microscopy2.90V1-94[»]
5AKAelectron microscopy5.70V1-94[»]
5GADelectron microscopy3.70W1-94[»]
5GAEelectron microscopy3.33W1-94[»]
5GAFelectron microscopy4.30W1-94[»]
5GAGelectron microscopy3.80W1-94[»]
5GAHelectron microscopy3.80W1-94[»]
5IQRelectron microscopy3.00V1-94[»]
5IT8X-ray3.12CW/DW1-94[»]
5J5BX-ray2.80CW/DW1-94[»]
5J7LX-ray3.00CW/DW1-94[»]
5J88X-ray3.32CW/DW1-94[»]
5J8AX-ray3.10CW/DW1-94[»]
5J91X-ray2.96CW/DW1-94[»]
5JC9X-ray3.03CW/DW1-94[»]
5JTEelectron microscopy3.60BV1-94[»]
5JU8electron microscopy3.60BV1-94[»]
5KCRelectron microscopy3.601Z1-94[»]
5KCSelectron microscopy3.901Z1-94[»]
5KPSelectron microscopy3.90V1-94[»]
5KPVelectron microscopy4.10U1-94[»]
5KPWelectron microscopy3.90U1-94[»]
5KPXelectron microscopy3.90U1-94[»]
5L3Pelectron microscopy3.70Z1-94[»]
ProteinModelPortaliP68919.
SMRiP68919.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-35885N.
IntActiP68919. 13 interactors.
MINTiMINT-1261165.
STRINGi511145.b2185.

2D gel databases

SWISS-2DPAGEP68919.

Proteomic databases

EPDiP68919.
PaxDbiP68919.
PRIDEiP68919.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75246; AAC75246; b2185.
BAE76650; BAE76650; BAE76650.
GeneIDi945618.
KEGGiecj:JW2173.
eco:b2185.
PATRICi32119725. VBIEscCol129921_2273.

Organism-specific databases

EchoBASEiEB0878.
EcoGeneiEG10885. rplY.

Phylogenomic databases

eggNOGiENOG4105KW6. Bacteria.
COG1825. LUCA.
HOGENOMiHOG000277629.
KOiK02897.
OMAiHAGKFPA.
PhylomeDBiP68919.

Enzyme and pathway databases

BioCyciEcoCyc:EG10885-MONOMER.
ECOL316407:JW2173-MONOMER.
MetaCyc:EG10885-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP68919.
PROiP68919.

Family and domain databases

CDDicd00495. Ribosomal_L25_TL5_CTC. 1 hit.
Gene3Di2.40.240.10. 1 hit.
HAMAPiMF_01336. Ribosomal_L25. 1 hit.
InterProiIPR020056. Rbsml_L25/Gln-tRNA_synth_b-brl.
IPR029751. Ribosomal_L25.
IPR011035. Ribosomal_L25/Gln-tRNA_synth.
IPR020055. Ribosomal_L25_short.
[Graphical view]
PfamiPF01386. Ribosomal_L25p. 1 hit.
[Graphical view]
ProDomiPD012503. Ribosomal_L25. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF50715. SSF50715. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRL25_ECOLI
AccessioniPrimary (citable) accession number: P68919
Secondary accession number(s): P02426, Q2MAQ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 30, 2016
This is version 121 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.