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Protein

50S ribosomal protein L3

Gene

rplC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10866-MONOMER.
ECOL316407:JW3282-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L3
Gene namesi
Name:rplC
Ordered Locus Names:b3320, JW3282
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10866. rplC.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • cytosolic large ribosomal subunit Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2363135.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 20920950S ribosomal protein L3PRO_0000077098Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei38 – 381N6-succinyllysine1 Publication
Modified residuei150 – 1501N5-methylglutamine1 Publication

Post-translational modificationi

Methylated by PrmB.1 Publication

Keywords - PTMi

Methylation

Proteomic databases

EPDiP60438.
PaxDbiP60438.
PRIDEiP60438.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-10744N.
IntActiP60438. 144 interactions.
MINTiMINT-1302843.
STRINGi511145.b3320.

Structurei

Secondary structure

1
209
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 1512Combined sources
Turni17 – 193Combined sources
Beta strandi21 – 288Combined sources
Beta strandi32 – 387Combined sources
Turni40 – 434Combined sources
Beta strandi47 – 537Combined sources
Helixi57 – 593Combined sources
Helixi62 – 7110Combined sources
Beta strandi77 – 837Combined sources
Turni91 – 933Combined sources
Helixi98 – 1014Combined sources
Turni102 – 1043Combined sources
Beta strandi106 – 1127Combined sources
Beta strandi115 – 1195Combined sources
Helixi121 – 1255Combined sources
Beta strandi132 – 1354Combined sources
Beta strandi136 – 1383Combined sources
Beta strandi140 – 1423Combined sources
Turni150 – 1523Combined sources
Helixi155 – 1573Combined sources
Beta strandi163 – 18119Combined sources
Helixi182 – 1843Combined sources
Beta strandi186 – 1916Combined sources
Beta strandi194 – 1963Combined sources
Beta strandi199 – 2057Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ML5electron microscopy14.00e2-209[»]
2J28electron microscopy8.00D1-209[»]
2RDOelectron microscopy9.10D1-209[»]
3BBXelectron microscopy10.00D1-209[»]
3J5Lelectron microscopy6.60D1-209[»]
3J7Zelectron microscopy3.90D1-209[»]
3J8Gelectron microscopy5.00D1-209[»]
3J9Yelectron microscopy3.90D1-209[»]
3J9Zelectron microscopy3.60LX1-209[»]
3JA1electron microscopy3.60LE1-209[»]
3JBUelectron microscopy3.64d1-209[»]
3JBVelectron microscopy3.32d1-209[»]
3JCDelectron microscopy3.70D1-209[»]
3JCEelectron microscopy3.20D1-209[»]
3JCJelectron microscopy3.70C1-209[»]
3JCNelectron microscopy4.60D1-209[»]
4CSUelectron microscopy5.50D1-209[»]
4U1UX-ray2.95BD/DD1-209[»]
4U1VX-ray3.00BD/DD1-209[»]
4U20X-ray2.90BD/DD1-209[»]
4U24X-ray2.90BD/DD1-209[»]
4U25X-ray2.90BD/DD1-209[»]
4U26X-ray2.80BD/DD1-209[»]
4U27X-ray2.80BD/DD1-209[»]
4UY8electron microscopy3.80D1-209[»]
4V47electron microscopy12.30AB1-209[»]
4V48electron microscopy11.50AB1-209[»]
4V4HX-ray3.46BD/DD1-209[»]
4V4QX-ray3.46BD/DD1-209[»]
4V4Velectron microscopy15.00BB1-209[»]
4V4Welectron microscopy15.00BB1-209[»]
4V50X-ray3.22BD/DD1-209[»]
4V52X-ray3.21BD/DD1-209[»]
4V53X-ray3.54BD/DD1-209[»]
4V54X-ray3.30BD/DD1-209[»]
4V55X-ray4.00BD/DD1-209[»]
4V56X-ray3.93BD/DD1-209[»]
4V57X-ray3.50BD/DD1-209[»]
4V5BX-ray3.74AD/CD1-209[»]
4V5Helectron microscopy5.80BD1-209[»]
4V5YX-ray4.45BD/DD1-209[»]
4V64X-ray3.50BD/DD1-209[»]
4V65electron microscopy9.00BY1-209[»]
4V66electron microscopy9.00BY1-209[»]
4V69electron microscopy6.70BD1-209[»]
4V6CX-ray3.19BD/DD1-209[»]
4V6DX-ray3.81BD/DD1-209[»]
4V6EX-ray3.71BD/DD1-209[»]
4V6Kelectron microscopy8.25AE1-209[»]
4V6Lelectron microscopy13.20BE1-209[»]
4V6Melectron microscopy7.10BD1-209[»]
4V6Nelectron microscopy12.10AE1-209[»]
4V6Oelectron microscopy14.70BE1-209[»]
4V6Pelectron microscopy13.50BE1-209[»]
4V6Qelectron microscopy11.50BE1-209[»]
4V6Relectron microscopy11.50BE1-209[»]
4V6Selectron microscopy13.10AE1-209[»]
4V6Telectron microscopy8.30BD1-209[»]
4V6Velectron microscopy9.80BE1-209[»]
4V6Yelectron microscopy12.00BD1-209[»]
4V6Zelectron microscopy12.00BD1-209[»]
4V70electron microscopy17.00BD1-209[»]
4V71electron microscopy20.00BD1-209[»]
4V72electron microscopy13.00BD1-209[»]
4V73electron microscopy15.00BD1-209[»]
4V74electron microscopy17.00BD1-209[»]
4V75electron microscopy12.00BD1-209[»]
4V76electron microscopy17.00BD1-209[»]
4V77electron microscopy17.00BD1-209[»]
4V78electron microscopy20.00BD1-209[»]
4V79electron microscopy15.00BD1-209[»]
4V7Aelectron microscopy9.00BD1-209[»]
4V7Belectron microscopy6.80BD1-209[»]
4V7Celectron microscopy7.60BE1-209[»]
4V7Delectron microscopy7.60AE1-209[»]
4V7Ielectron microscopy9.60AD1-209[»]
4V7SX-ray3.25BD/DD1-209[»]
4V7TX-ray3.19BD/DD1-209[»]
4V7UX-ray3.10BD/DD1-209[»]
4V7VX-ray3.29BD/DD1-209[»]
4V85X-ray3.20D1-209[»]
4V89X-ray3.70BD1-209[»]
4V9CX-ray3.30BD/DD1-209[»]
4V9DX-ray3.00CD/DD1-209[»]
4V9OX-ray2.90AD/CD/ED/GD1-209[»]
4V9PX-ray2.90AD/CD/ED/GD1-209[»]
4WF1X-ray3.09BD/DD1-209[»]
4WOIX-ray3.00BD/CD1-209[»]
4WWWX-ray3.10RD/YD1-209[»]
4YBBX-ray2.10CD/DD1-209[»]
5ADYelectron microscopy4.50D1-209[»]
5AFIelectron microscopy2.90D1-209[»]
5AKAelectron microscopy5.70D1-209[»]
5GADelectron microscopy3.70D1-209[»]
5GAEelectron microscopy3.33D1-209[»]
5GAFelectron microscopy4.30D1-209[»]
5GAGelectron microscopy3.80D1-209[»]
5GAHelectron microscopy3.80D1-209[»]
5IQRelectron microscopy3.00C1-209[»]
ProteinModelPortaliP60438.
SMRiP60438. Positions 1-209.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60438.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L3P family.Curated

Phylogenomic databases

eggNOGiENOG4105EEE. Bacteria.
COG0087. LUCA.
HOGENOMiHOG000100368.
InParanoidiP60438.
KOiK02906.
OMAiKRMAGRY.
PhylomeDBiP60438.

Family and domain databases

HAMAPiMF_01325_B. Ribosomal_L3_B. 1 hit.
InterProiIPR000597. Ribosomal_L3.
IPR019927. Ribosomal_L3_bac/org-type.
IPR019926. Ribosomal_L3_CS.
IPR009000. Transl_B-barrel.
[Graphical view]
PANTHERiPTHR11229. PTHR11229. 1 hit.
PfamiPF00297. Ribosomal_L3. 1 hit.
[Graphical view]
SUPFAMiSSF50447. SSF50447. 1 hit.
TIGRFAMsiTIGR03625. L3_bact. 1 hit.
PROSITEiPS00474. RIBOSOMAL_L3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P60438-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIGLVGKKVG MTRIFTEDGV SIPVTVIEVE ANRVTQVKDL ANDGYRAIQV
60 70 80 90 100
TTGAKKANRV TKPEAGHFAK AGVEAGRGLW EFRLAEGEEF TVGQSISVEL
110 120 130 140 150
FADVKKVDVT GTSKGKGFAG TVKRWNFRTQ DATHGNSLSH RVPGSIGQNQ
160 170 180 190 200
TPGKVFKGKK MAGQMGNERV TVQSLDVVRV DAERNLLLVK GAVPGATGSD

LIVKPAVKA
Length:209
Mass (Da):22,244
Last modified:July 21, 1986 - v1
Checksum:iEA8E10EDD2C0A8FD
GO

Mass spectrometryi

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA02757. R5EC3.
RefSeqiNP_417779.1. NC_000913.3.
WP_000579833.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76345; AAC76345; b3320.
BAE77971; BAE77971; BAE77971.
GeneIDi947817.
KEGGiecj:JW3282.
eco:b3320.
PATRICi32122072. VBIEscCol129921_3413.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA02757. R5EC3.
RefSeqiNP_417779.1. NC_000913.3.
WP_000579833.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ML5electron microscopy14.00e2-209[»]
2J28electron microscopy8.00D1-209[»]
2RDOelectron microscopy9.10D1-209[»]
3BBXelectron microscopy10.00D1-209[»]
3J5Lelectron microscopy6.60D1-209[»]
3J7Zelectron microscopy3.90D1-209[»]
3J8Gelectron microscopy5.00D1-209[»]
3J9Yelectron microscopy3.90D1-209[»]
3J9Zelectron microscopy3.60LX1-209[»]
3JA1electron microscopy3.60LE1-209[»]
3JBUelectron microscopy3.64d1-209[»]
3JBVelectron microscopy3.32d1-209[»]
3JCDelectron microscopy3.70D1-209[»]
3JCEelectron microscopy3.20D1-209[»]
3JCJelectron microscopy3.70C1-209[»]
3JCNelectron microscopy4.60D1-209[»]
4CSUelectron microscopy5.50D1-209[»]
4U1UX-ray2.95BD/DD1-209[»]
4U1VX-ray3.00BD/DD1-209[»]
4U20X-ray2.90BD/DD1-209[»]
4U24X-ray2.90BD/DD1-209[»]
4U25X-ray2.90BD/DD1-209[»]
4U26X-ray2.80BD/DD1-209[»]
4U27X-ray2.80BD/DD1-209[»]
4UY8electron microscopy3.80D1-209[»]
4V47electron microscopy12.30AB1-209[»]
4V48electron microscopy11.50AB1-209[»]
4V4HX-ray3.46BD/DD1-209[»]
4V4QX-ray3.46BD/DD1-209[»]
4V4Velectron microscopy15.00BB1-209[»]
4V4Welectron microscopy15.00BB1-209[»]
4V50X-ray3.22BD/DD1-209[»]
4V52X-ray3.21BD/DD1-209[»]
4V53X-ray3.54BD/DD1-209[»]
4V54X-ray3.30BD/DD1-209[»]
4V55X-ray4.00BD/DD1-209[»]
4V56X-ray3.93BD/DD1-209[»]
4V57X-ray3.50BD/DD1-209[»]
4V5BX-ray3.74AD/CD1-209[»]
4V5Helectron microscopy5.80BD1-209[»]
4V5YX-ray4.45BD/DD1-209[»]
4V64X-ray3.50BD/DD1-209[»]
4V65electron microscopy9.00BY1-209[»]
4V66electron microscopy9.00BY1-209[»]
4V69electron microscopy6.70BD1-209[»]
4V6CX-ray3.19BD/DD1-209[»]
4V6DX-ray3.81BD/DD1-209[»]
4V6EX-ray3.71BD/DD1-209[»]
4V6Kelectron microscopy8.25AE1-209[»]
4V6Lelectron microscopy13.20BE1-209[»]
4V6Melectron microscopy7.10BD1-209[»]
4V6Nelectron microscopy12.10AE1-209[»]
4V6Oelectron microscopy14.70BE1-209[»]
4V6Pelectron microscopy13.50BE1-209[»]
4V6Qelectron microscopy11.50BE1-209[»]
4V6Relectron microscopy11.50BE1-209[»]
4V6Selectron microscopy13.10AE1-209[»]
4V6Telectron microscopy8.30BD1-209[»]
4V6Velectron microscopy9.80BE1-209[»]
4V6Yelectron microscopy12.00BD1-209[»]
4V6Zelectron microscopy12.00BD1-209[»]
4V70electron microscopy17.00BD1-209[»]
4V71electron microscopy20.00BD1-209[»]
4V72electron microscopy13.00BD1-209[»]
4V73electron microscopy15.00BD1-209[»]
4V74electron microscopy17.00BD1-209[»]
4V75electron microscopy12.00BD1-209[»]
4V76electron microscopy17.00BD1-209[»]
4V77electron microscopy17.00BD1-209[»]
4V78electron microscopy20.00BD1-209[»]
4V79electron microscopy15.00BD1-209[»]
4V7Aelectron microscopy9.00BD1-209[»]
4V7Belectron microscopy6.80BD1-209[»]
4V7Celectron microscopy7.60BE1-209[»]
4V7Delectron microscopy7.60AE1-209[»]
4V7Ielectron microscopy9.60AD1-209[»]
4V7SX-ray3.25BD/DD1-209[»]
4V7TX-ray3.19BD/DD1-209[»]
4V7UX-ray3.10BD/DD1-209[»]
4V7VX-ray3.29BD/DD1-209[»]
4V85X-ray3.20D1-209[»]
4V89X-ray3.70BD1-209[»]
4V9CX-ray3.30BD/DD1-209[»]
4V9DX-ray3.00CD/DD1-209[»]
4V9OX-ray2.90AD/CD/ED/GD1-209[»]
4V9PX-ray2.90AD/CD/ED/GD1-209[»]
4WF1X-ray3.09BD/DD1-209[»]
4WOIX-ray3.00BD/CD1-209[»]
4WWWX-ray3.10RD/YD1-209[»]
4YBBX-ray2.10CD/DD1-209[»]
5ADYelectron microscopy4.50D1-209[»]
5AFIelectron microscopy2.90D1-209[»]
5AKAelectron microscopy5.70D1-209[»]
5GADelectron microscopy3.70D1-209[»]
5GAEelectron microscopy3.33D1-209[»]
5GAFelectron microscopy4.30D1-209[»]
5GAGelectron microscopy3.80D1-209[»]
5GAHelectron microscopy3.80D1-209[»]
5IQRelectron microscopy3.00C1-209[»]
ProteinModelPortaliP60438.
SMRiP60438. Positions 1-209.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-10744N.
IntActiP60438. 144 interactions.
MINTiMINT-1302843.
STRINGi511145.b3320.

Chemistry

ChEMBLiCHEMBL2363135.

Proteomic databases

EPDiP60438.
PaxDbiP60438.
PRIDEiP60438.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76345; AAC76345; b3320.
BAE77971; BAE77971; BAE77971.
GeneIDi947817.
KEGGiecj:JW3282.
eco:b3320.
PATRICi32122072. VBIEscCol129921_3413.

Organism-specific databases

EchoBASEiEB0859.
EcoGeneiEG10866. rplC.

Phylogenomic databases

eggNOGiENOG4105EEE. Bacteria.
COG0087. LUCA.
HOGENOMiHOG000100368.
InParanoidiP60438.
KOiK02906.
OMAiKRMAGRY.
PhylomeDBiP60438.

Enzyme and pathway databases

BioCyciEcoCyc:EG10866-MONOMER.
ECOL316407:JW3282-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP60438.
PROiP60438.

Family and domain databases

HAMAPiMF_01325_B. Ribosomal_L3_B. 1 hit.
InterProiIPR000597. Ribosomal_L3.
IPR019927. Ribosomal_L3_bac/org-type.
IPR019926. Ribosomal_L3_CS.
IPR009000. Transl_B-barrel.
[Graphical view]
PANTHERiPTHR11229. PTHR11229. 1 hit.
PfamiPF00297. Ribosomal_L3. 1 hit.
[Graphical view]
SUPFAMiSSF50447. SSF50447. 1 hit.
TIGRFAMsiTIGR03625. L3_bact. 1 hit.
PROSITEiPS00474. RIBOSOMAL_L3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRL3_ECOLI
AccessioniPrimary (citable) accession number: P60438
Secondary accession number(s): P02386, Q2M6Y5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: September 7, 2016
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Ribosomal proteins
    Ribosomal proteins families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.