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Protein

50S ribosomal protein L14

Gene

rplN

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

Functioni

This protein binds directly to 23S ribosomal RNA. In the E.coli 70S ribosome it has been modeled to make two contacts with the 16S rRNA of the 30S subunit, forming part of bridges B5 and B8, connecting the 2 subunits (PubMed:12809609). Although the protein undergoes significant rotation during the transition from an initiation to and EF-G bound state, the bridges remain stable. In the 3.5 A resolved structures L14 and L19 interact and together make contact with the 16S rRNA in bridges B5 and B8 (PubMed:16272117).3 Publications
Can also interact with RsfS, in this case bridge B8 probably cannot form, and the 30S and 50S ribosomal subunits do not associate, which represses translation.1 Publication

GO - Molecular functioni

  • large ribosomal subunit rRNA binding Source: EcoCyc
  • structural constituent of ribosome Source: GO_Central

GO - Biological processi

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10875-MONOMER.
MetaCyc:EG10875-MONOMER.

Protein family/group databases

MoonProtiP0ADY3.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L14UniRule annotation
Alternative name(s):
Large ribosomal subunit protein uL141 Publication
Gene namesi
Name:rplNUniRule annotation
Ordered Locus Names:b3310, JW3272
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10875. rplN.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • cytosolic large ribosomal subunit Source: EcoCyc

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi97T → A: Reduced RsfS binding. 1 Publication1
Mutagenesisi98R → A: Reduced RsfS binding. 1 Publication1
Mutagenesisi114K → A: Reduced RsfS binding. 1 Publication1
Mutagenesisi117S → A: No change in RsfS binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001285401 – 12350S ribosomal protein L14Add BLAST123

Proteomic databases

PaxDbiP0ADY3.
PRIDEiP0ADY3.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit (PubMed:352727, PubMed:7556101, PubMed:2665813, PubMed:10094780, PubMed:10756104, PubMed:12809609, PubMed:16272117, PubMed:25310980, PubMed:24844575, PubMed:27934701, PubMed:27906160, PubMed:27906161). Contacts L19 (PubMed:2665813, PubMed:16272117). Forms two bridges to the 30S subunit in the 70S ribosome, contacting the 16S rRNA. Can also contact RsfS, which then probably inhibits ribosomal subunit association.12 Publications

Protein-protein interaction databases

BioGridi852121. 1 interactor.
DIPiDIP-35798N.
IntActiP0ADY3. 53 interactors.
MINTiMINT-1304553.
STRINGi316385.ECDH10B_3485.

Structurei

Secondary structure

1123
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 10Combined sources4
Beta strandi12 – 24Combined sources13
Beta strandi38 – 46Combined sources9
Beta strandi57 – 62Combined sources6
Beta strandi76 – 81Combined sources6
Beta strandi83 – 87Combined sources5
Beta strandi89 – 91Combined sources3
Helixi105 – 107Combined sources3
Turni110 – 112Combined sources3
Helixi113 – 118Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ML5electron microscopy14.00n1-122[»]
2J28electron microscopy8.00K2-122[»]
2RDOelectron microscopy9.10K1-123[»]
3BBXelectron microscopy10.00K1-123[»]
3IY9electron microscopy14.10K2-122[»]
3IZZelectron microscopy10.80G2-122[»]
3J5Lelectron microscopy6.60K1-122[»]
3J7Zelectron microscopy3.90K1-123[»]
3J8Gelectron microscopy5.00K1-123[»]
3J9Yelectron microscopy3.90K1-123[»]
3J9Zelectron microscopy3.60LG1-123[»]
3JA1electron microscopy3.60LM1-123[»]
3JBUelectron microscopy3.64k1-123[»]
3JBVelectron microscopy3.32k1-123[»]
3JCDelectron microscopy3.70K1-123[»]
3JCEelectron microscopy3.20K1-123[»]
3JCJelectron microscopy3.70J1-123[»]
3JCNelectron microscopy4.60K1-123[»]
487Delectron microscopy7.50M1-122[»]
4CSUelectron microscopy5.50K1-123[»]
4U1UX-ray2.95BK/DK1-122[»]
4U1VX-ray3.00BK/DK1-122[»]
4U20X-ray2.90BK/DK1-122[»]
4U24X-ray2.90BK/DK1-122[»]
4U25X-ray2.90BK/DK1-122[»]
4U26X-ray2.80BK/DK1-122[»]
4U27X-ray2.80BK/DK1-122[»]
4UY8electron microscopy3.80K1-122[»]
4V47electron microscopy12.30AI1-123[»]
4V48electron microscopy11.50AI1-123[»]
4V4HX-ray3.46BK/DK1-123[»]
4V4QX-ray3.46BK/DK1-123[»]
4V4Velectron microscopy15.00BI2-123[»]
4V4Welectron microscopy15.00BI2-123[»]
4V50X-ray3.22BK/DK1-123[»]
4V52X-ray3.21BK/DK1-123[»]
4V53X-ray3.54BK/DK1-123[»]
4V54X-ray3.30BK/DK1-123[»]
4V55X-ray4.00BK/DK1-123[»]
4V56X-ray3.93BK/DK1-123[»]
4V57X-ray3.50BK/DK1-123[»]
4V5BX-ray3.74AK/CK1-123[»]
4V5Helectron microscopy5.80BK1-121[»]
4V5YX-ray4.45BK/DK1-123[»]
4V64X-ray3.50BK/DK1-123[»]
4V65electron microscopy9.00BD1-123[»]
4V66electron microscopy9.00BD1-123[»]
4V69electron microscopy6.70BK2-122[»]
4V6CX-ray3.19BK/DK1-123[»]
4V6DX-ray3.81BK/DK1-123[»]
4V6EX-ray3.71BK/DK1-123[»]
4V6Kelectron microscopy8.25AL1-123[»]
4V6Lelectron microscopy13.20BL1-123[»]
4V6Melectron microscopy7.10BK1-123[»]
4V6Nelectron microscopy12.10AM1-123[»]
4V6Oelectron microscopy14.70BM1-123[»]
4V6Pelectron microscopy13.50BM1-123[»]
4V6Qelectron microscopy11.50BM1-123[»]
4V6Relectron microscopy11.50BM1-123[»]
4V6Selectron microscopy13.10AM1-123[»]
4V6Telectron microscopy8.30BK1-122[»]
4V6Velectron microscopy9.80BO1-123[»]
4V6Yelectron microscopy12.00BK1-122[»]
4V6Zelectron microscopy12.00BK1-122[»]
4V70electron microscopy17.00BK1-122[»]
4V71electron microscopy20.00BK1-122[»]
4V72electron microscopy13.00BK1-122[»]
4V73electron microscopy15.00BK1-122[»]
4V74electron microscopy17.00BK1-122[»]
4V75electron microscopy12.00BK1-122[»]
4V76electron microscopy17.00BK1-122[»]
4V77electron microscopy17.00BK1-122[»]
4V78electron microscopy20.00BK1-122[»]
4V79electron microscopy15.00BK1-122[»]
4V7Aelectron microscopy9.00BK1-122[»]
4V7Belectron microscopy6.80BK1-123[»]
4V7Celectron microscopy7.60BM1-123[»]
4V7Delectron microscopy7.60AN1-123[»]
4V7Ielectron microscopy9.60AK1-123[»]
4V7SX-ray3.25BK/DK1-122[»]
4V7TX-ray3.19BK/DK1-122[»]
4V7UX-ray3.10BK/DK1-122[»]
4V7VX-ray3.29BK/DK1-122[»]
4V85X-ray3.20O1-123[»]
4V89X-ray3.70BO1-123[»]
4V9CX-ray3.30BK/DK1-123[»]
4V9DX-ray3.00CK/DK1-122[»]
4V9OX-ray2.90AK/CK/EK/GK1-123[»]
4V9PX-ray2.90AK/CK/EK/GK1-123[»]
4WF1X-ray3.09BK/DK1-122[»]
4WOIX-ray3.00BK/CK1-123[»]
4WWWX-ray3.10RK/YK1-122[»]
4YBBX-ray2.10CL/DL1-123[»]
5ADYelectron microscopy4.50K1-123[»]
5AFIelectron microscopy2.90K1-123[»]
5AKAelectron microscopy5.70K1-123[»]
5GADelectron microscopy3.70L1-123[»]
5GAEelectron microscopy3.33L1-123[»]
5GAFelectron microscopy4.30L1-123[»]
5GAGelectron microscopy3.80L1-123[»]
5GAHelectron microscopy3.80L1-123[»]
5H5Uelectron microscopy3.00L1-123[»]
5IQRelectron microscopy3.00K1-123[»]
5IT8X-ray3.12CL/DL1-123[»]
5J5BX-ray2.80CL/DL1-123[»]
5J7LX-ray3.00CL/DL1-123[»]
5J88X-ray3.32CL/DL1-123[»]
5J8AX-ray3.10CL/DL1-123[»]
5J91X-ray2.96CL/DL1-123[»]
5JC9X-ray3.03CL/DL1-123[»]
5JTEelectron microscopy3.60BK1-123[»]
5JU8electron microscopy3.60BK1-123[»]
5KCRelectron microscopy3.601O1-123[»]
5KCSelectron microscopy3.901O1-123[»]
5KPSelectron microscopy3.90K1-123[»]
5KPVelectron microscopy4.10J1-123[»]
5KPWelectron microscopy3.90J1-123[»]
5KPXelectron microscopy3.90J1-123[»]
5L3Pelectron microscopy3.70O1-123[»]
5LZAelectron microscopy3.60K1-122[»]
5LZBelectron microscopy5.30K1-122[»]
5LZCelectron microscopy4.80K1-122[»]
5LZDelectron microscopy3.40K1-122[»]
5LZEelectron microscopy3.50K1-122[»]
5LZFelectron microscopy4.60K1-122[»]
5MDVelectron microscopy2.97K1-123[»]
5MDWelectron microscopy3.06K1-123[»]
5MDYelectron microscopy3.35K1-123[»]
5MDZelectron microscopy3.10K1-123[»]
5MGPelectron microscopy3.10K1-122[»]
5NCOelectron microscopy4.80L1-123[»]
5NP6electron microscopy3.60i1-122[»]
5NWYelectron microscopy2.93X1-123[»]
5O2Relectron microscopy3.40K1-122[»]
5U4Ielectron microscopy3.50L1-123[»]
5U9Felectron microscopy3.20131-123[»]
5U9Gelectron microscopy3.20131-123[»]
5UYKelectron microscopy3.90131-122[»]
5UYLelectron microscopy3.60131-122[»]
5UYMelectron microscopy3.20131-122[»]
5UYNelectron microscopy4.00131-122[»]
5UYPelectron microscopy3.90131-122[»]
5UYQelectron microscopy3.80131-122[»]
ProteinModelPortaliP0ADY3.
SMRiP0ADY3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ADY3.

Family & Domainsi

Sequence similaritiesi

Belongs to the universal ribosomal protein uL14 family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108UNN. Bacteria.
COG0093. LUCA.
HOGENOMiHOG000183702.
InParanoidiP0ADY3.
KOiK02874.
PhylomeDBiP0ADY3.

Family and domain databases

Gene3Di2.40.150.20. 1 hit.
HAMAPiMF_01367. Ribosomal_L14. 1 hit.
InterProiView protein in InterPro
IPR000218. Ribosomal_L14P.
IPR005745. Ribosomal_L14P_bac-type.
IPR019972. Ribosomal_L14P_CS.
IPR036853. Ribosomal_L14P_sf.
PANTHERiPTHR11761. PTHR11761. 1 hit.
PfamiView protein in Pfam
PF00238. Ribosomal_L14. 1 hit.
SMARTiView protein in SMART
SM01374. Ribosomal_L14. 1 hit.
SUPFAMiSSF50193. SSF50193. 1 hit.
TIGRFAMsiTIGR01067. rplN_bact. 1 hit.
PROSITEiView protein in PROSITE
PS00049. RIBOSOMAL_L14. 1 hit.

Sequencei

Sequence statusi: Complete.

P0ADY3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIQEQTMLNV ADNSGARRVM CIKVLGGSHR RYAGVGDIIK ITIKEAIPRG
60 70 80 90 100
KVKKGDVLKA VVVRTKKGVR RPDGSVIRFD GNACVLLNNN SEQPIGTRIF
110 120
GPVTRELRSE KFMKIISLAP EVL
Length:123
Mass (Da):13,541
Last modified:April 1, 1988 - v1
Checksum:i192ACB1623979510
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti63Missing AA sequence (PubMed:352727).Curated1
Sequence conflicti84C → S AA sequence (PubMed:352727).Curated1
Sequence conflicti90 – 91NS → TD AA sequence (PubMed:352727).Curated2
Sequence conflicti97Missing AA sequence (PubMed:352727).Curated1
Sequence conflicti115I → L AA sequence (PubMed:352727).Curated1
Sequence conflicti123Missing AA sequence (PubMed:352727).Curated1

Mass spectrometryi

P0ADY3: Molecular mass is 13540.2 Da from positions 1 - 123. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01563 Genomic DNA. Translation: CAA25715.1.
U18997 Genomic DNA. Translation: AAA58107.1.
U00096 Genomic DNA. Translation: AAC76335.1.
AP009048 Genomic DNA. Translation: BAE77981.1.
V00357 Genomic DNA. Translation: CAA23653.1.
PIRiA65124. R5EC14.
RefSeqiNP_417769.1. NC_000913.3.
WP_000613955.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76335; AAC76335; b3310.
BAE77981; BAE77981; BAE77981.
GeneIDi947809.
KEGGiecj:JW3272.
eco:b3310.
PATRICifig|1411691.4.peg.3421.

Similar proteinsi

Entry informationi

Entry nameiRL14_ECOLI
AccessioniPrimary (citable) accession number: P0ADY3
Secondary accession number(s): P02411, Q2M6X5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1988
Last modified: October 25, 2017
This is version 118 of the entry and version 1 of the sequence. See 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