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Reviewed, UniProtKB/Swiss-Prot P60438 (RL3_ECOLI)

Last modified June 16, 2009. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    50S ribosomal protein L3
Gene names
Name: rplC
Ordered Locus Names: b3320, JW3282
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length209 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

One of two assembly inititator proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. HAMAP MF_01325

Subunit structure

Part of the 50S ribosomal subunit. Forms a cluster with proteins L14 and L19. Ref.8

Sequence similarities

Belongs to the ribosomal protein L3P family.

Mass spectrometry

Molecular mass is 22257.2 Da from positions 1 - 209. Determined by MALDI. Ref.9

Binary interactions

With

Entry

#Exp.

IntAct

Notes

mcbRP761141EBI-542200,EBI-560824

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 20920950S ribosomal protein L3 HAMAP MF_01325
PRO_0000077098

Amino acid modifications

Modified residue1501N5-methylglutamine HAMAP MF_01325

Secondary structure

................... 209
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P60438-1 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: EA8E10EDD2C0A8FD

FASTA20922,244
        10         20         30         40         50         60 
MIGLVGKKVG MTRIFTEDGV SIPVTVIEVE ANRVTQVKDL ANDGYRAIQV TTGAKKANRV 

        70         80         90        100        110        120 
TKPEAGHFAK AGVEAGRGLW EFRLAEGEEF TVGQSISVEL FADVKKVDVT GTSKGKGFAG 

       130        140        150        160        170        180 
TVKRWNFRTQ DATHGNSLSH RVPGSIGQNQ TPGKVFKGKK MAGQMGNERV TVQSLDVVRV 

       190        200 
DAERNLLLVK GAVPGATGSD LIVKPAVKA 

« Hide

References

« Hide 'large scale' references
[1]"The primary structure of ribosomal protein L3 from Escherichia coli 70 S ribosomes."
Muranova T.A., Muranov A.V., Markova L.F., Ovchinnikov Y.A.
FEBS Lett. 96:301-305(1978) [PubMed: 365579] [Abstract]
Cited for: PROTEIN SEQUENCE.
Strain: MRE-600.
[2]"Structure of the Escherichia coli S10 ribosomal protein operon."
Zurawski G., Zurawski S.M.
Nucleic Acids Res. 13:4521-4526(1985) [PubMed: 3892488] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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 277:1453-1474(1997) [PubMed: 9278503] [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: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Regulation of the S10 ribosomal protein operon in E. coli: nucleotide sequence at the start of the operon."
Olins P.O., Nomura M.
Cell 26:205-211(1981) [PubMed: 7037196] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-80.
[6]"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: 9298646] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-12.
Strain: K12 / EMG2.
[7]"Initiator proteins for the assembly of the 50S subunit from Escherichia coli ribosomes."
Nowotny V., Nierhaus K.H.
Proc. Natl. Acad. Sci. U.S.A. 79:7238-7242(1982) [PubMed: 6760192] [Abstract]
Cited for: IDENTIFICATION AS AN ASSEMBLY INITIATOR PROTEIN.
[8]"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: 3298242] [Abstract]
Cited for: ASSEMBLY MAP OF THE 50S SUBUNIT.
Strain: K12.
[9]"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: 10094780] [Abstract]
Cited for: MASS SPECTROMETRY.
Strain: K12 / ATCC 25404 / DSM 5698 / NCIMB 11290.
[10]"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: 12809609] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS).
Strain: MRE-600.
[11]"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: 16272117] [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

X02613 Genomic DNA. Translation: CAA26460.1.
U18997 Genomic DNA. Translation: AAA58117.1.
U00096 Genomic DNA. Translation: AAC76345.1.
AP009048 Genomic DNA. Translation: BAE77971.1.
V00344 Genomic DNA. Translation: CAA23634.1.
PIRR5EC3. A02757.
RefSeqAP_004470.1.
NP_417779.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1P85electron microscopy12.30B1-209[»]
1P86electron microscopy11.50B1-209[»]
1VS6X-ray3.46D1-209[»]
1VS8X-ray3.46D1-209[»]
2AW4X-ray3.46D1-209[»]
2AWBX-ray3.46D1-209[»]
2GYAelectron microscopy2.00B1-209[»]
2GYCelectron microscopy2.00B1-209[»]
2I2TX-ray3.22D1-209[»]
2I2VX-ray3.22D1-209[»]
2J28electron microscopy8.00D1-209[»]
2QAMX-ray3.21D1-209[»]
2QAOX-ray3.21D1-209[»]
2QBAX-ray3.54D1-209[»]
2QBCX-ray3.54D1-209[»]
2QBEX-ray3.30D1-209[»]
2QBGX-ray3.30D1-209[»]
2QBIX-ray4.00D1-209[»]
2QBKX-ray4.00D1-209[»]
2QOVX-ray3.93D1-209[»]
2QOXX-ray3.93D1-209[»]
2QOZX-ray3.50D1-209[»]
2QP1X-ray3.50D1-209[»]
2RDOelectron microscopy9.10D1-209[»]
2VHMX-ray3.74D1-209[»]
2VHNX-ray3.74D1-209[»]
2Z4LX-ray4.45D1-209[»]
2Z4NX-ray4.45D1-209[»]
3BBXelectron microscopy10.00D1-209[»]
3DF2X-ray3.50D1-209[»]
3DF4X-ray3.50D1-209[»]
3FIKelectron microscopy-D1-209[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP60438. 144 interactions.

2-D gel databases

ECO2DBASEI023.0. 6TH EDITION.

Genome annotation databases

GeneID947817.
GenomeReviewsGene locus JW3282 in contig AP009048_GR.
Gene locus b3320 in contig U00096_GR.
KEGGecj:JW3282.
eco:b3320.

Organism-specific databases

EchoBASEEB0859.
EcoGeneEG10866. rplC.
CMRSearch...

Phylogenomic databases

HOGENOMP60438.
OMAP60438. AEFRVSE.

Enzyme and pathway databases

BioCycEcoCyc:EG10866-MON.

Family and domain databases

HAMAPMF_01325.
[Tree]
InterProIPR000597. Ribosomal_L3.
IPR019927. Ribosomal_L3_bac/org-type.
IPR019926. Ribosomal_L3_CS.
[Graphical view]
PfamPF00297. Ribosomal_L3. 1 hit.
[Graphical view]
ProDomPD001374. Ribosomal_L3. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR03625. L3_bact. 1 hit.
PROSITEPS00474. RIBOSOMAL_L3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRL3_ECOLI
AccessionPrimary (citable) accession number: P60438
Secondary accession number(s): P02386, Q2M6Y5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 16, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Ribosomal proteins

Ribosomal proteins families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents