50S ribosomal protein L3 - Escherichia coli (strain K12)

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P60438 (RL3_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 92. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
50S ribosomal protein L3

Gene names

Name:	rplC
Ordered Locus Names:	b3320, JW3282

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	209 AA.
Sequence status	Complete.
Protein existence	Evidence 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_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.10
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

Ontologies

Keywords
Ligand	RNA-binding rRNA-binding
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Methylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	translation Inferred from electronic annotation. Source: InterPro
Cellular component	ribosome Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	rRNA binding Inferred from electronic annotation. Source: UniProtKB-KW structural constituent of ribosome Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 209

209

50S ribosomal protein L3 HAMAP MF_01325_B

PRO_0000077098

Amino acid modifications

Modified residue

150

N5-methylglutamine Ref.1

Secondary structure

209

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P60438 [UniParc].

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

FASTA

209

22,244

        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' referencesShow '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, 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: 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]	"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: 11847124] [Abstract] Cited for: METHYLATION BY PRMB. Strain: K12.
[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: 12809609] [Abstract] Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS). Strain: MRE-600.
[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: 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

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.

PIR

R5EC3. A02757.

RefSeq

NP_417779.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1P85	electron microscopy	12.30	B	1-209	[»]
1P86	electron microscopy	11.50	B	1-209	[»]
1VS6	X-ray	3.46	D	1-209	[»]
1VS8	X-ray	3.46	D	1-209	[»]
1VT2	X-ray	3.30	D	1-209	[»]
2AW4	X-ray	3.46	D	1-209	[»]
2AWB	X-ray	3.46	D	1-209	[»]
2GYA	electron microscopy	15.00	B	1-209	[»]
2GYC	electron microscopy	15.00	B	1-209	[»]
2I2T	X-ray	3.22	D	1-209	[»]
2I2V	X-ray	3.22	D	1-209	[»]
2J28	electron microscopy	8.00	D	1-209	[»]
2QAM	X-ray	3.21	D	1-209	[»]
2QAO	X-ray	3.21	D	1-209	[»]
2QBA	X-ray	3.54	D	1-209	[»]
2QBC	X-ray	3.54	D	1-209	[»]
2QBE	X-ray	3.30	D	1-209	[»]
2QBG	X-ray	3.30	D	1-209	[»]
2QBI	X-ray	4.00	D	1-209	[»]
2QBK	X-ray	4.00	D	1-209	[»]
2QOV	X-ray	3.93	D	1-209	[»]
2QOX	X-ray	3.93	D	1-209	[»]
2QOZ	X-ray	3.50	D	1-209	[»]
2QP1	X-ray	3.50	D	1-209	[»]
2RDO	electron microscopy	9.10	D	1-209	[»]
2VHM	X-ray	3.74	D	1-209	[»]
2VHN	X-ray	3.74	D	1-209	[»]
2WWQ	electron microscopy	5.80	D	1-209	[»]
2Z4L	X-ray	4.45	D	1-209	[»]
2Z4N	X-ray	4.45	D	1-209	[»]
3BBX	electron microscopy	10.00	D	1-209	[»]
3DF2	X-ray	3.50	D	1-209	[»]
3DF4	X-ray	3.50	D	1-209	[»]
3E1B	electron microscopy	-	Y	1-209	[»]
3E1D	electron microscopy	-	Y	1-209	[»]
3FIK	electron microscopy	6.70	D	1-209	[»]
3I1N	X-ray	3.19	D	1-209	[»]
3I1P	X-ray	3.19	D	1-209	[»]
3I1R	X-ray	3.81	D	1-209	[»]
3I1T	X-ray	3.81	D	1-209	[»]
3I20	X-ray	3.71	D	1-209	[»]
3I22	X-ray	3.71	D	1-209	[»]
3IZT	electron microscopy	-	E	1-209	[»]
3IZU	electron microscopy	-	E	1-209	[»]
3J01	electron microscopy	-	D	1-209	[»]
3KCR	electron microscopy	-	D	1-209	[»]
3OAS	X-ray	3.25	D	1-209	[»]
3OAT	X-ray	3.25	D	1-209	[»]
3OFC	X-ray	3.19	D	1-209	[»]
3OFD	X-ray	3.19	D	1-209	[»]
3OFQ	X-ray	3.10	D	1-209	[»]
3OFR	X-ray	3.10	D	1-209	[»]
3OFZ	X-ray	3.29	D	1-209	[»]
3OG0	X-ray	3.29	D	1-209	[»]
3ORB	X-ray	3.30	D	1-209	[»]
3R8S	X-ray	3.00	D	1-209	[»]
3R8T	X-ray	3.00	D	1-209	[»]

ProteinModelPortal

P60438.

SMR

P60438. Positions 1-209.

ModBase

Search...

Protein-protein interaction databases

IntAct

P60438. 144 interactions.

MINT

MINT-1302843.

2D gel databases

ECO2DBASE

I023.0. 6TH EDITION.

Proteomic databases

PRIDE

P60438.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000001875; EBESCP00000001875; EBESCG00000001541.
EBESCT00000014527; EBESCP00000013818; EBESCG00000013588.

GeneID

947817.

GenomeReviews

Gene locus JW3282 in contig AP009048_GR.
Gene locus b3320 in contig U00096_GR.

KEGG

ecj:JW3282.
eco:b3320.

PATRIC

32122072. VBIEscCol129921_3413.

Organism-specific databases

EchoBASE

EB0859.

EcoGene

EG10866. rplC.

Phylogenomic databases

eggNOG

COG0087.

GeneTree

EBGT00050000011222.

HOGENOM

HBG734653.

OMA

VGMTRLF.

PhylomeDB

P60438.

ProtClustDB

PRK00001.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10866-MONOMER.

Gene expression databases

Genevestigator

P60438.

Family and domain databases

HAMAP

MF_01325_B. Ribosomal_L3_B.
[Tree]

InterPro

IPR000597. Ribosomal_L3.
IPR019927. Ribosomal_L3_bac/org-type.
IPR019926. Ribosomal_L3_CS.
IPR009000. Transl_elong_init/rib_B-barrel.
[Graphical view]

K02906.

PANTHER

PTHR11229. PTHR11229. 1 hit.

Pfam

PF00297. Ribosomal_L3. 1 hit.
[Graphical view]

SUPFAM

SSF50447. Translat_factor. 1 hit.

TIGRFAMs

TIGR03625. L3_bact. 1 hit.

PROSITE

PS00474. RIBOSOMAL_L3. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

RL3_ECOLI

Accession

Primary (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:	January 25, 2012
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Ribosomal proteins

Ribosomal proteins families and list of entries

Escherichia coli

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents