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P0ADY3 (RL14_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 88. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
50S ribosomal protein L14
Gene names
Name:rplN
Ordered Locus Names:b3310, JW3272
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length123 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This protein binds directly to 23S ribosomal RNA. In the E.coli 70S ribosome (Ref.11) 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. 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 (Ref.12) L14 and L19 interact and together make contact with the 16S rRNA in bridges B5 and B8. Ref.9

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. Ref.9

Subunit structure

Part of the 50S ribosomal subunit. Contacts L19 (Ref.7 and Ref.12). 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. Ref.11

Sequence similarities

Belongs to the ribosomal protein L14P family.

Mass spectrometry

Molecular mass is 13540.2 Da from positions 1 - 123. Determined by MALDI. Ref.8

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12312350S ribosomal protein L14 HAMAP-Rule MF_01367
PRO_0000128540

Experimental info

Mutagenesis971T → A: Reduced RsfS binding. Ref.9
Mutagenesis981R → A: Reduced RsfS binding. Ref.9
Mutagenesis1141K → A: Reduced RsfS binding. Ref.9
Mutagenesis1171S → A: No change in RsfS binding. Ref.9
Sequence conflict631Missing AA sequence Ref.1
Sequence conflict841C → S AA sequence Ref.1
Sequence conflict90 – 912NS → TD AA sequence Ref.1
Sequence conflict971Missing AA sequence Ref.1
Sequence conflict1151I → L AA sequence Ref.1
Sequence conflict1231Missing AA sequence Ref.1

Secondary structure

.............................. 123
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0ADY3 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: 192ACB1623979510

FASTA12313,541
        10         20         30         40         50         60 
MIQEQTMLNV ADNSGARRVM CIKVLGGSHR RYAGVGDIIK ITIKEAIPRG KVKKGDVLKA 

        70         80         90        100        110        120 
VVVRTKKGVR RPDGSVIRFD GNACVLLNNN SEQPIGTRIF GPVTRELRSE KFMKIISLAP 


EVL 

« Hide

References

« Hide 'large scale' references
[1]"Primary structure of protein L14 isolated from Escherichia coli ribosomes."
Morinaga T., Funatsu G., Funatsu M., Wittmann-Liebold B., Wittmann H.G.
FEBS Lett. 91:74-77(1978) [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]"DNA sequences of promoter regions for the str and spc ribosomal protein operons in E. coli."
Post L.E., Arfsten A.E., Reusser F., Nomura M.
Cell 15:215-229(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
Strain: K12.
[6]"Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by cross-linking studies."
Urlaub H., Kruft V., Bischof O., Mueller E.-C., Wittmann-Liebold B.
EMBO J. 14:4578-4588(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 24-28, CROSS-LINKING TO RRNA.
Strain: MRE-600.
[7]"Comparative cross-linking study on the 50S ribosomal subunit from Escherichia coli."
Walleczek J., Martin T., Redl B., Stoeffler-Meilicke M., Stoeffler G.
Biochemistry 28:4099-4105(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: CROSS-LINKING TO L19.
[8]"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.
[9]"RsfA (YbeB) proteins are conserved ribosomal silencing factors."
Hauser R., Pech M., Kijek J., Yamamoto H., Titz B., Naeve F., Tovchigrechko A., Yamamoto K., Szaflarski W., Takeuchi N., Stellberger T., Diefenbacher M.E., Nierhaus K.H., Uetz P.
PLoS Genet. 8:E1002815-E1002815(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RSFS, MUTAGENESIS OF THR-97; ARG-98; LYS-114 AND SER-117.
Strain: K12 / MG1655 / ATCC 47076.
[10]"The 3D arrangement of the 23 S and 5 S rRNA in the Escherichia coli 50 S ribosomal subunit based on a cryo-electron microscopic reconstruction at 7.5 A resolution."
Mueller F., Sommer I., Baranov P., Matadeen R., Stoldt M., Woehnert J., Goerlach M., van Heel M., Brimacombe R.
J. Mol. Biol. 298:35-59(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING.
[11]"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), INTERSUBUNIT BRIDGE FORMATION.
[12]"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: 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.
PIRR5EC14. A65124.
RefSeqNP_417769.1. NC_000913.3.
YP_492122.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ML5electron microscopy14.00n1-122[»]
1P85electron microscopy12.30I1-123[»]
1P86electron microscopy11.50I1-123[»]
1VS6X-ray3.46K1-123[»]
1VS8X-ray3.46K1-123[»]
1VT2X-ray3.30K1-123[»]
2AW4X-ray3.46K1-123[»]
2AWBX-ray3.46K1-123[»]
2GYAelectron microscopy15.00I2-123[»]
2GYCelectron microscopy15.00I2-123[»]
2I2TX-ray3.22K1-123[»]
2I2VX-ray3.22K1-123[»]
2J28electron microscopy8.00K2-122[»]
2QAMX-ray3.21K1-123[»]
2QAOX-ray3.21K1-123[»]
2QBAX-ray3.54K1-123[»]
2QBCX-ray3.54K1-123[»]
2QBEX-ray3.30K1-123[»]
2QBGX-ray3.30K1-123[»]
2QBIX-ray4.00K1-123[»]
2QBKX-ray4.00K1-123[»]
2QOVX-ray3.93K1-123[»]
2QOXX-ray3.93K1-123[»]
2QOZX-ray3.50K1-123[»]
2QP1X-ray3.50K1-123[»]
2RDOelectron microscopy9.10K1-123[»]
2WWQelectron microscopy5.80K1-121[»]
2Z4LX-ray4.45K1-123[»]
2Z4NX-ray4.45K1-123[»]
3BBXelectron microscopy10.00K1-123[»]
3E1Belectron microscopy-D1-123[»]
3E1Delectron microscopy-D1-123[»]
3FIKelectron microscopy6.70K2-122[»]
3I1NX-ray3.19K1-123[»]
3I1PX-ray3.19K1-123[»]
3I1RX-ray3.81K1-123[»]
3I1TX-ray3.81K1-123[»]
3I20X-ray3.71K1-123[»]
3I22X-ray3.71K1-123[»]
3IY9electron microscopy14.10K2-122[»]
3IZTelectron microscopy-L1-123[»]
3IZUelectron microscopy-L1-123[»]
3IZZelectron microscopy10.80G2-122[»]
3J01electron microscopy-K1-123[»]
3J0Telectron microscopy12.10M1-123[»]
3J0Welectron microscopy14.70M1-123[»]
3J0Yelectron microscopy13.50M1-123[»]
3J11electron microscopy13.10M1-123[»]
3J12electron microscopy11.50M1-123[»]
3J14electron microscopy11.50M1-123[»]
3J19electron microscopy8.30K1-122[»]
3J37electron microscopy9.80O1-123[»]
3J4Xelectron microscopy12.00K1-122[»]
3J50electron microscopy20.00K1-122[»]
3J51electron microscopy17.00K1-122[»]
3J52electron microscopy12.00K1-122[»]
3J54electron microscopy13.00K1-122[»]
3J56electron microscopy15.00K1-122[»]
3J58electron microscopy17.00K1-122[»]
3J5Aelectron microscopy12.00K1-122[»]
3J5Celectron microscopy17.00K1-122[»]
3J5Eelectron microscopy17.00K1-122[»]
3J5Gelectron microscopy20.00K1-122[»]
3J5Ielectron microscopy15.00K1-122[»]
3J5Kelectron microscopy9.00K1-122[»]
3J5Lelectron microscopy6.60K1-122[»]
3J5Oelectron microscopy6.80K1-123[»]
3J5Uelectron microscopy7.60M1-123[»]
3J5Welectron microscopy7.60N1-123[»]
3KCRelectron microscopy-K1-123[»]
3OASX-ray3.25K1-122[»]
3OATX-ray3.25K1-122[»]
3OFCX-ray3.19K1-122[»]
3OFDX-ray3.19K1-122[»]
3OFQX-ray3.10K1-122[»]
3OFRX-ray3.10K1-122[»]
3OFZX-ray3.29K1-122[»]
3OG0X-ray3.29K1-122[»]
3ORBX-ray3.30K1-123[»]
3R8SX-ray3.00K1-122[»]
3R8TX-ray3.00K1-122[»]
3SGFX-ray3.20O1-123[»]
3UOSX-ray3.70O1-123[»]
487Delectron microscopy7.50M1-122[»]
4GARX-ray3.30K1-123[»]
4GAUX-ray3.30K1-123[»]
4KIXX-ray2.90K1-123[»]
4KIZX-ray2.90K1-123[»]
4KJ1X-ray2.90K1-123[»]
4KJ3X-ray2.90K1-123[»]
4KJ5X-ray2.90K1-123[»]
4KJ7X-ray2.90K1-123[»]
4KJ9X-ray2.90K1-123[»]
4KJBX-ray2.90K1-123[»]
ProteinModelPortalP0ADY3.
SMRP0ADY3. Positions 2-123.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid852121. 1 interaction.
DIPDIP-35798N.
IntActP0ADY3. 49 interactions.
MINTMINT-1304553.
STRING511145.b3310.

Chemistry

ChEMBLCHEMBL2363135.

Proteomic databases

PaxDbP0ADY3.
PRIDEP0ADY3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76335; AAC76335; b3310.
BAE77981; BAE77981; BAE77981.
GeneID12934392.
947809.
KEGGecj:Y75_p3866.
eco:b3310.
PATRIC32122052. VBIEscCol129921_3403.

Organism-specific databases

EchoBASEEB0868.
EcoGeneEG10875. rplN.

Phylogenomic databases

eggNOGCOG0093.
HOGENOMHOG000183702.
KOK02874.
OMAELRNDKF.
OrthoDBEOG6GBMJ6.
PhylomeDBP0ADY3.

Enzyme and pathway databases

BioCycEcoCyc:EG10875-MONOMER.
ECOL316407:JW3272-MONOMER.

Gene expression databases

GenevestigatorP0ADY3.

Family and domain databases

Gene3D2.40.150.20. 1 hit.
HAMAPMF_01367. Ribosomal_L14.
InterProIPR005745. Ribosomal_L14_bac-type.
IPR019972. Ribosomal_L14_CS.
IPR023571. Ribosomal_L14_dom.
IPR000218. Ribosomal_L14b/L23e.
[Graphical view]
PANTHERPTHR11761. PTHR11761. 1 hit.
PfamPF00238. Ribosomal_L14. 1 hit.
[Graphical view]
SUPFAMSSF50193. SSF50193. 1 hit.
TIGRFAMsTIGR01067. rplN_bact. 1 hit.
PROSITEPS00049. RIBOSOMAL_L14. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0ADY3.
PROP0ADY3.

Entry information

Entry nameRL14_ECOLI
AccessionPrimary (citable) accession number: P0ADY3
Secondary accession number(s): P02411, Q2M6X5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1988
Last modified: June 11, 2014
This is version 88 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