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P0A7L0 (RL1_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 94. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
50S ribosomal protein L1
Gene names
Name:rplA
Ordered Locus Names:b3984, JW3947
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length234 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

One of the primary rRNA binding proteins, it binds very close to the 3'-end of the 23S rRNA. Forms part of the L1 stalk. It is often not seen in high-resolution crystal structures, but can be seen in cryo_EM and 3D reconstruction models. These indicate that the distal end of the stalk moves by approximately 20 angstroms (Ref.16). This stalk movement is thought to be coupled to movement of deacylated tRNA into and out of the E site, and thus to participate in tRNA translocation (Ref.16). Contacts the P and E site tRNAs. HAMAP-Rule MF_01318_B

Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA. HAMAP-Rule MF_01318_B

Subunit structure

Part of the 50S ribosomal subunit. Cross-links to the P and E site tRNAs. Ref.9

Sequence similarities

Belongs to the ribosomal protein L1P family.

Mass spectrometry

Molecular mass is 24598.9 Da from positions 2 - 234. Determined by MALDI. Ref.13

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5 Ref.7
Chain2 – 23423350S ribosomal protein L1 HAMAP-Rule MF_01318_B
PRO_0000125654

Amino acid modifications

Modified residue1051N6-succinyllysine Ref.15
Modified residue1541N6-succinyllysine Ref.15
Modified residue1861N6-succinyllysine Ref.15
Modified residue1971N6-succinyllysine Ref.15

Experimental info

Sequence conflict121R → I AA sequence Ref.7

Secondary structure

............................................ 234
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A7L0 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: D751704B34748D53

FASTA23424,730
        10         20         30         40         50         60 
MAKLTKRMRV IREKVDATKQ YDINEAIALL KELATAKFVE SVDVAVNLGI DARKSDQNVR 

        70         80         90        100        110        120 
GATVLPHGTG RSVRVAVFTQ GANAEAAKAA GAELVGMEDL ADQIKKGEMN FDVVIASPDA 

       130        140        150        160        170        180 
MRVVGQLGQV LGPRGLMPNP KVGTVTPNVA EAVKNAKAGQ VRYRNDKNGI IHTTIGKVDF 

       190        200        210        220        230 
DADKLKENLE ALLVALKKAK PTQAKGVYIK KVSISTTMGA GVAVDQAGLS ASVN 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the ribosomal protein gene cluster adjacent to the gene for RNA polymerase subunit beta in Escherichia coli."
Post L.E., Strycharz G.D., Nomura M., Lewis H., Dennis P.P.
Proc. Natl. Acad. Sci. U.S.A. 76:1697-1701(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[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]"The primary structure of protein L1 from the large ribosomal subunit of Escherichia coli."
Brauer D., Oechsner I.
FEBS Lett. 96:317-321(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-234.
Strain: K.
[6]Erratum
Brauer D., Oechsner I.
FEBS Lett. 98:411-411(1979)
[7]"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Link A.J., Robison K., Church G.M.
Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-13.
Strain: K12 / EMG2.
[8]"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 199-203, CROSS-LINKING TO RRNA.
Strain: MRE-600.
[9]"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.
[10]"Translational regulation of the L11 ribosomal protein operon of Escherichia coli: mutations that define the target site for repression by L1."
Thomas M.S., Nomura M.
Nucleic Acids Res. 15:3085-3096(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: MECHANISM OF TRANSLATION REGULATION.
Strain: K12 / MC1061 / ATCC 53338 / DSM 7140.
[11]"The ribosomal neighbourhood of the central fold of tRNA: cross-links from position 47 of tRNA located at the A, P or E site."
Osswald M., Doering T., Brimacombe R.
Nucleic Acids Res. 23:4635-4641(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CROSS-LINKING TO THE TRNA CENTRAL FOLD.
Strain: MRE-600.
[12]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[13]"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.
[14]"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.
Strain: MRE-600.
[15]"Identification of lysine succinylation as a new post-translational modification."
Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y.
Nat. Chem. Biol. 7:58-63(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION AT LYS-105; LYS-154; LYS-186 AND LYS-197.
Strain: K12.
[16]"Locking and unlocking of ribosomal motions."
Valle M., Zavialov A., Sengupta J., Rawat U., Ehrenberg M., Frank J.
Cell 114:123-134(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING OF RIBOSOMAL COMPLEXES IMPLYING THE INVOLVEMENT OF THE L1 STALK IN TRANSLOCATION OF TRNAS FROM THE P TO E SITE.
[17]"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: LOCALIZATION IN THE 3.5 ANGSTROM RIBOSOMAL STRUCTURES AND DISCUSSION OF ITS MOVEMENT.
Strain: MRE-600.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V00339 Genomic DNA. Translation: CAA23622.1.
U00006 Genomic DNA. Translation: AAC43082.1.
U00096 Genomic DNA. Translation: AAC76958.1.
AP009048 Genomic DNA. Translation: BAE77336.1.
PIRR5EC1. S12573.
RefSeqNP_418411.1. NC_000913.3.
YP_491477.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EG0electron microscopy11.50N1-229[»]
1ML5electron microscopy14.00c2-229[»]
2GYAelectron microscopy15.0026-227[»]
2GYCelectron microscopy15.0026-227[»]
2RDOelectron microscopy9.1092-234[»]
2WWQelectron microscopy5.8051-234[»]
3E1Belectron microscopy9.00Z131-224[»]
3E1Delectron microscopy9.00Z131-224[»]
3FIKelectron microscopy6.7051-234[»]
3IZTelectron microscopy-C1-234[»]
3IZUelectron microscopy-C1-234[»]
3J01electron microscopy-51-234[»]
3J0Telectron microscopy12.10C1-234[»]
3J0Welectron microscopy14.70C1-234[»]
3J0Yelectron microscopy13.50C1-234[»]
3J11electron microscopy13.10C1-234[»]
3J12electron microscopy11.50C1-234[»]
3J14electron microscopy11.50C1-234[»]
3J37electron microscopy9.80C1-234[»]
3J46electron microscopy10.1051-234[»]
3J4Xelectron microscopy12.0051-234[»]
3J50electron microscopy20.0051-234[»]
3J51electron microscopy17.0051-234[»]
3J52electron microscopy12.0051-234[»]
3J54electron microscopy13.0051-234[»]
3J56electron microscopy15.0051-234[»]
3J58electron microscopy17.0051-234[»]
3J5Aelectron microscopy12.0051-234[»]
3J5Celectron microscopy17.0051-234[»]
3J5Eelectron microscopy17.0051-234[»]
3J5Gelectron microscopy20.0051-234[»]
3J5Ielectron microscopy15.0051-234[»]
3J5Kelectron microscopy9.0051-234[»]
3J5Selectron microscopy7.50F1-234[»]
3J5Uelectron microscopy7.60C2-234[»]
3J5Welectron microscopy7.60C2-234[»]
3KCRelectron microscopy-51-234[»]
487Delectron microscopy7.50H29-201[»]
ProteinModelPortalP0A7L0.
SMRP0A7L0. Positions 1-234.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-35746N.
IntActP0A7L0. 125 interactions.
MINTMINT-1268287.
STRING511145.b3984.

Chemistry

ChEMBLCHEMBL2363135.

2D gel databases

SWISS-2DPAGEP0A7L0.

Proteomic databases

PaxDbP0A7L0.
PRIDEP0A7L0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76958; AAC76958; b3984.
BAE77336; BAE77336; BAE77336.
GeneID12930515.
948483.
KEGGecj:Y75_p3213.
eco:b3984.
PATRIC32123489. VBIEscCol129921_4097.

Organism-specific databases

EchoBASEEB0857.
EcoGeneEG10864. rplA.

Phylogenomic databases

eggNOGCOG0081.
HOGENOMHOG000207015.
KOK02863.
OMAVDSTKQY.
OrthoDBEOG6FBX2G.
PhylomeDBP0A7L0.

Enzyme and pathway databases

BioCycEcoCyc:EG10864-MONOMER.
ECOL316407:JW3947-MONOMER.

Gene expression databases

GenevestigatorP0A7L0.

Family and domain databases

Gene3D3.30.190.20. 2 hits.
3.40.50.790. 1 hit.
HAMAPMF_01318_B. Ribosomal_L1_B.
InterProIPR005878. Ribosom_L1_bac-type.
IPR002143. Ribosomal_L1.
IPR023674. Ribosomal_L1-like.
IPR028364. Ribosomal_L1/biogenesis.
IPR016094. Ribosomal_L1_2-a/b-sand.
IPR016095. Ribosomal_L1_3-a/b-sand.
IPR023673. Ribosomal_L1_CS.
[Graphical view]
PfamPF00687. Ribosomal_L1. 1 hit.
[Graphical view]
PIRSFPIRSF002155. Ribosomal_L1. 1 hit.
SUPFAMSSF56808. SSF56808. 1 hit.
TIGRFAMsTIGR01169. rplA_bact. 1 hit.
PROSITEPS01199. RIBOSOMAL_L1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A7L0.
PROP0A7L0.

Entry information

Entry nameRL1_ECOLI
AccessionPrimary (citable) accession number: P0A7L0
Secondary accession number(s): P02384, Q2M8S0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 94 of the entry and version 2 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