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P60438 (RL3_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 112. 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 L3
Gene names
Name:rplC
Ordered Locus Names:b3320, JW3282
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length209 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

One of two assembly initiator proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. HAMAP-Rule MF_01325_B

Subunit structure

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

Post-translational modification

Methylated by PrmB By similarity. Ref.1 Ref.11

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.10

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 20920950S ribosomal protein L3 HAMAP-Rule MF_01325_B
PRO_0000077098

Amino acid modifications

Modified residue381N6-succinyllysine Ref.12
Modified residue1501N5-methylglutamine Ref.1

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P60438 [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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, METHYLATION AT GLN-150.
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] [Europe PMC] [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 277:1453-1462(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]"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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: ASSEMBLY MAP OF THE 50S SUBUNIT.
Strain: K12.
[9]"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.
[10]"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.
[11]"The hemK gene in Escherichia coli encodes the N(5)-glutamine methyltransferase that modifies peptide release factors."
Heurgue-Hamard V., Champ S., Engstroem A., Ehrenberg M., Buckingham R.H.
EMBO J. 21:769-778(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION BY PRMB.
Strain: K12.
[12]"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-38.
Strain: K12.
[13]"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).
Strain: MRE-600.
[14]"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
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.
RefSeqNP_417779.1. NC_000913.3.
YP_492112.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ML5electron microscopy14.00e2-209[»]
1P85electron microscopy12.30B1-209[»]
1P86electron microscopy11.50B1-209[»]
1VS6X-ray3.46D1-209[»]
1VS8X-ray3.46D1-209[»]
1VT2X-ray3.30D1-209[»]
2AW4X-ray3.46D1-209[»]
2AWBX-ray3.46D1-209[»]
2GYAelectron microscopy15.00B1-209[»]
2GYCelectron microscopy15.00B1-209[»]
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[»]
2WWQelectron microscopy5.80D1-209[»]
2Z4LX-ray4.45D1-209[»]
2Z4NX-ray4.45D1-209[»]
3BBXelectron microscopy10.00D1-209[»]
3DF2X-ray3.50D1-209[»]
3DF4X-ray3.50D1-209[»]
3E1Belectron microscopy-Y1-209[»]
3E1Delectron microscopy-Y1-209[»]
3FIKelectron microscopy6.70D1-209[»]
3I1NX-ray3.19D1-209[»]
3I1PX-ray3.19D1-209[»]
3I1RX-ray3.81D1-209[»]
3I1TX-ray3.81D1-209[»]
3I20X-ray3.71D1-209[»]
3I22X-ray3.71D1-209[»]
3IZTelectron microscopy-E1-209[»]
3IZUelectron microscopy-E1-209[»]
3J01electron microscopy-D1-209[»]
3J0Telectron microscopy12.10E1-209[»]
3J0Welectron microscopy14.70E1-209[»]
3J0Yelectron microscopy13.50E1-209[»]
3J11electron microscopy13.10E1-209[»]
3J12electron microscopy11.50E1-209[»]
3J14electron microscopy11.50E1-209[»]
3J19electron microscopy8.30D1-209[»]
3J37electron microscopy9.80E1-209[»]
3J4Xelectron microscopy12.00D1-209[»]
3J50electron microscopy20.00D1-209[»]
3J51electron microscopy17.00D1-209[»]
3J52electron microscopy12.00D1-209[»]
3J54electron microscopy13.00D1-209[»]
3J56electron microscopy15.00D1-209[»]
3J58electron microscopy17.00D1-209[»]
3J5Aelectron microscopy12.00D1-209[»]
3J5Celectron microscopy17.00D1-209[»]
3J5Eelectron microscopy17.00D1-209[»]
3J5Gelectron microscopy20.00D1-209[»]
3J5Ielectron microscopy15.00D1-209[»]
3J5Kelectron microscopy9.00D1-209[»]
3J5Lelectron microscopy6.60D1-209[»]
3J5Oelectron microscopy6.80D1-209[»]
3J5Uelectron microscopy7.60E1-209[»]
3J5Welectron microscopy7.60E1-209[»]
3KCRelectron microscopy-D1-209[»]
3OASX-ray3.25D1-209[»]
3OATX-ray3.25D1-209[»]
3OFCX-ray3.19D1-209[»]
3OFDX-ray3.19D1-209[»]
3OFQX-ray3.10D1-209[»]
3OFRX-ray3.10D1-209[»]
3OFZX-ray3.29D1-209[»]
3OG0X-ray3.29D1-209[»]
3ORBX-ray3.30D1-209[»]
3R8SX-ray3.00D1-209[»]
3R8TX-ray3.00D1-209[»]
3SGFX-ray3.20D1-209[»]
3UOSX-ray3.70D1-209[»]
4GARX-ray3.30D1-209[»]
4GAUX-ray3.30D1-209[»]
4KIXX-ray2.90D1-209[»]
4KIZX-ray2.90D1-209[»]
4KJ1X-ray2.90D1-209[»]
4KJ3X-ray2.90D1-209[»]
4KJ5X-ray2.90D1-209[»]
4KJ7X-ray2.90D1-209[»]
4KJ9X-ray2.90D1-209[»]
4KJBX-ray2.90D1-209[»]
ProteinModelPortalP60438.
SMRP60438. Positions 1-209.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10744N.
IntActP60438. 144 interactions.
MINTMINT-1302843.
STRING511145.b3320.

Chemistry

ChEMBLCHEMBL2363135.

Proteomic databases

PaxDbP60438.
PRIDEP60438.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76345; AAC76345; b3320.
BAE77971; BAE77971; BAE77971.
GeneID12932298.
947817.
KEGGecj:Y75_p3856.
eco:b3320.
PATRIC32122072. VBIEscCol129921_3413.

Organism-specific databases

EchoBASEEB0859.
EcoGeneEG10866. rplC.

Phylogenomic databases

eggNOGCOG0087.
HOGENOMHOG000100368.
KOK02906.
OMASMQDATH.
OrthoDBEOG6WDSMH.
PhylomeDBP60438.

Enzyme and pathway databases

BioCycEcoCyc:EG10866-MONOMER.
ECOL316407:JW3282-MONOMER.

Gene expression databases

GenevestigatorP60438.

Family and domain databases

HAMAPMF_01325_B. Ribosomal_L3_B.
InterProIPR000597. Ribosomal_L3.
IPR019927. Ribosomal_L3_bac/org-type.
IPR019926. Ribosomal_L3_CS.
IPR009000. Transl_B-barrel.
[Graphical view]
PANTHERPTHR11229. PTHR11229. 1 hit.
PfamPF00297. Ribosomal_L3. 1 hit.
[Graphical view]
SUPFAMSSF50447. SSF50447. 1 hit.
TIGRFAMsTIGR03625. L3_bact. 1 hit.
PROSITEPS00474. RIBOSOMAL_L3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP60438.
PROP60438.

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: May 14, 2014
This is version 112 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