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Protein

50S ribosomal protein L30

Gene

rpmD

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciEcoCyc:EG10888-MONOMER.
ECOL316407:JW3264-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L30UniRule annotation
Gene namesi
Name:rpmDUniRule annotation
Ordered Locus Names:b3302, JW3264
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10888. rpmD.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 595850S ribosomal protein L30PRO_0000104590Add
BLAST

Proteomic databases

PaxDbiP0AG51.
PRIDEiP0AG51.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit.

Protein-protein interaction databases

DIPiDIP-35970N.
IntActiP0AG51. 3 interactions.
STRINGi511145.b3302.

Structurei

Secondary structure

1
59
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 96Combined sources
Beta strandi13 – 153Combined sources
Helixi18 – 2710Combined sources
Beta strandi31 – 333Combined sources
Beta strandi35 – 395Combined sources
Helixi42 – 509Combined sources
Helixi51 – 544Combined sources
Beta strandi55 – 584Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ML5electron microscopy14.00x1-59[»]
2J28electron microscopy8.00Y2-59[»]
2RDOelectron microscopy9.10Y2-59[»]
3BBXelectron microscopy10.00Y2-59[»]
3J5Lelectron microscopy6.60Z2-59[»]
3J7Zelectron microscopy3.90Z1-59[»]
3J9Yelectron microscopy3.90Z1-59[»]
4CSUelectron microscopy5.5022-59[»]
4U1UX-ray2.95BZ/DZ2-59[»]
4U1VX-ray3.00BZ/DZ2-59[»]
4U20X-ray2.90BZ/DZ2-59[»]
4U24X-ray2.90BZ/DZ2-59[»]
4U25X-ray2.90BZ/DZ2-59[»]
4U26X-ray2.80BZ/DZ2-59[»]
4U27X-ray2.80BZ/DZ2-59[»]
4UY8electron microscopy3.80Z2-59[»]
4V47electron microscopy12.30AX2-59[»]
4V48electron microscopy11.50AX2-59[»]
4V4HX-ray3.46BY/DY1-59[»]
4V4QX-ray3.46BY/DY2-59[»]
4V4Velectron microscopy15.00BX4-59[»]
4V4Welectron microscopy15.00BX4-59[»]
4V50X-ray3.22BZ/DZ2-59[»]
4V52X-ray3.21BY/DY2-59[»]
4V53X-ray3.54BY/DY2-59[»]
4V54X-ray3.30BY/DY2-59[»]
4V55X-ray4.00BY/DY2-59[»]
4V56X-ray3.93BY/DY2-59[»]
4V57X-ray3.50BY/DY2-59[»]
4V5BX-ray3.74AY/CY2-59[»]
4V5Helectron microscopy5.80B22-59[»]
4V5YX-ray4.45BY/DY2-59[»]
4V64X-ray3.50BY/DY2-59[»]
4V65electron microscopy9.00BR1-59[»]
4V66electron microscopy9.00BR1-59[»]
4V69electron microscopy6.70BZ2-59[»]
4V6CX-ray3.19BZ/DZ1-59[»]
4V6DX-ray3.81BZ/DZ1-59[»]
4V6EX-ray3.71BZ/DZ1-59[»]
4V6Kelectron microscopy8.25Aa1-59[»]
4V6Lelectron microscopy13.20Ba1-59[»]
4V6Melectron microscopy7.10BZ2-59[»]
4V6Nelectron microscopy12.10A12-59[»]
4V6Oelectron microscopy14.70B12-59[»]
4V6Pelectron microscopy13.50B12-59[»]
4V6Qelectron microscopy11.50B12-59[»]
4V6Relectron microscopy11.50B12-59[»]
4V6Selectron microscopy13.10A12-59[»]
4V6Telectron microscopy8.30BZ2-59[»]
4V6Velectron microscopy9.80B32-59[»]
4V6Yelectron microscopy12.00BZ1-59[»]
4V6Zelectron microscopy12.00BZ1-59[»]
4V70electron microscopy17.00BZ1-59[»]
4V71electron microscopy20.00BZ1-59[»]
4V72electron microscopy13.00BZ1-59[»]
4V73electron microscopy15.00BZ1-59[»]
4V74electron microscopy17.00BZ1-59[»]
4V75electron microscopy12.00BZ1-59[»]
4V76electron microscopy17.00BZ1-59[»]
4V77electron microscopy17.00BZ1-59[»]
4V78electron microscopy20.00BZ1-59[»]
4V79electron microscopy15.00BZ1-59[»]
4V7Aelectron microscopy9.00BZ1-59[»]
4V7Belectron microscopy6.80BZ1-59[»]
4V7Celectron microscopy7.60B22-59[»]
4V7Delectron microscopy7.60A32-59[»]
4V7Ielectron microscopy9.60AZ1-59[»]
4V7SX-ray3.25BZ/DZ2-59[»]
4V7TX-ray3.19BZ/DZ2-59[»]
4V7UX-ray3.10BZ/DZ2-59[»]
4V7VX-ray3.29BZ/DZ2-59[»]
4V85X-ray3.2031-59[»]
4V89X-ray3.70B31-59[»]
4V9CX-ray3.30BZ/DZ1-59[»]
4V9DX-ray3.00CZ/DZ2-59[»]
4V9OX-ray2.90AZ/CZ/EZ/GZ1-59[»]
4V9PX-ray2.90AZ/CZ/EZ/GZ1-59[»]
4WF1X-ray3.09BZ/DZ2-59[»]
4WWWX-ray3.10RZ/YZ2-59[»]
4YBBX-ray2.10C0/D02-59[»]
5AFIelectron microscopy2.90Z1-59[»]
5AKAelectron microscopy5.70Y2-59[»]
ProteinModelPortaliP0AG51.
SMRiP0AG51. Positions 2-59.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AG51.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L30P family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1841.
HOGENOMiHOG000039916.
InParanoidiP0AG51.
KOiK02907.
OMAiIRTVAHL.
OrthoDBiEOG6BGP7P.
PhylomeDBiP0AG51.

Family and domain databases

Gene3Di3.30.1390.20. 1 hit.
HAMAPiMF_01371_B. Ribosomal_L30_B.
InterProiIPR005996. Ribosomal_L30_bac-type.
IPR018038. Ribosomal_L30_CS.
IPR016082. Ribosomal_L30_ferredoxin-like.
[Graphical view]
PfamiPF00327. Ribosomal_L30. 1 hit.
[Graphical view]
PIRSFiPIRSF002211. Ribosomal_L30_bac-type. 1 hit.
SUPFAMiSSF55129. SSF55129. 1 hit.
TIGRFAMsiTIGR01308. rpmD_bact. 1 hit.
PROSITEiPS00634. RIBOSOMAL_L30. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AG51-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKTIKITQT RSAIGRLPKH KATLLGLGLR RIGHTVERED TPAIRGMINA

VSFMVKVEE
Length:59
Mass (Da):6,542
Last modified:January 23, 2007 - v2
Checksum:i08F427BBB6F820A4
GO

Mass spectrometryi

Molecular mass is 6410.3 Da from positions 2 - 59. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01563 Genomic DNA. Translation: CAA25723.1.
U18997 Genomic DNA. Translation: AAA58099.1.
U00096 Genomic DNA. Translation: AAC76327.1.
AP009048 Genomic DNA. Translation: BAE77989.1.
PIRiA65123. R5EC30.
RefSeqiNP_417761.1. NC_000913.3.
WP_001140433.1. NZ_CP010445.1.

Genome annotation databases

EnsemblBacteriaiAAC76327; AAC76327; b3302.
BAE77989; BAE77989; BAE77989.
GeneIDi947797.
KEGGieco:b3302.
PATRICi32122036. VBIEscCol129921_3395.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01563 Genomic DNA. Translation: CAA25723.1.
U18997 Genomic DNA. Translation: AAA58099.1.
U00096 Genomic DNA. Translation: AAC76327.1.
AP009048 Genomic DNA. Translation: BAE77989.1.
PIRiA65123. R5EC30.
RefSeqiNP_417761.1. NC_000913.3.
WP_001140433.1. NZ_CP010445.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ML5electron microscopy14.00x1-59[»]
2J28electron microscopy8.00Y2-59[»]
2RDOelectron microscopy9.10Y2-59[»]
3BBXelectron microscopy10.00Y2-59[»]
3J5Lelectron microscopy6.60Z2-59[»]
3J7Zelectron microscopy3.90Z1-59[»]
3J9Yelectron microscopy3.90Z1-59[»]
4CSUelectron microscopy5.5022-59[»]
4U1UX-ray2.95BZ/DZ2-59[»]
4U1VX-ray3.00BZ/DZ2-59[»]
4U20X-ray2.90BZ/DZ2-59[»]
4U24X-ray2.90BZ/DZ2-59[»]
4U25X-ray2.90BZ/DZ2-59[»]
4U26X-ray2.80BZ/DZ2-59[»]
4U27X-ray2.80BZ/DZ2-59[»]
4UY8electron microscopy3.80Z2-59[»]
4V47electron microscopy12.30AX2-59[»]
4V48electron microscopy11.50AX2-59[»]
4V4HX-ray3.46BY/DY1-59[»]
4V4QX-ray3.46BY/DY2-59[»]
4V4Velectron microscopy15.00BX4-59[»]
4V4Welectron microscopy15.00BX4-59[»]
4V50X-ray3.22BZ/DZ2-59[»]
4V52X-ray3.21BY/DY2-59[»]
4V53X-ray3.54BY/DY2-59[»]
4V54X-ray3.30BY/DY2-59[»]
4V55X-ray4.00BY/DY2-59[»]
4V56X-ray3.93BY/DY2-59[»]
4V57X-ray3.50BY/DY2-59[»]
4V5BX-ray3.74AY/CY2-59[»]
4V5Helectron microscopy5.80B22-59[»]
4V5YX-ray4.45BY/DY2-59[»]
4V64X-ray3.50BY/DY2-59[»]
4V65electron microscopy9.00BR1-59[»]
4V66electron microscopy9.00BR1-59[»]
4V69electron microscopy6.70BZ2-59[»]
4V6CX-ray3.19BZ/DZ1-59[»]
4V6DX-ray3.81BZ/DZ1-59[»]
4V6EX-ray3.71BZ/DZ1-59[»]
4V6Kelectron microscopy8.25Aa1-59[»]
4V6Lelectron microscopy13.20Ba1-59[»]
4V6Melectron microscopy7.10BZ2-59[»]
4V6Nelectron microscopy12.10A12-59[»]
4V6Oelectron microscopy14.70B12-59[»]
4V6Pelectron microscopy13.50B12-59[»]
4V6Qelectron microscopy11.50B12-59[»]
4V6Relectron microscopy11.50B12-59[»]
4V6Selectron microscopy13.10A12-59[»]
4V6Telectron microscopy8.30BZ2-59[»]
4V6Velectron microscopy9.80B32-59[»]
4V6Yelectron microscopy12.00BZ1-59[»]
4V6Zelectron microscopy12.00BZ1-59[»]
4V70electron microscopy17.00BZ1-59[»]
4V71electron microscopy20.00BZ1-59[»]
4V72electron microscopy13.00BZ1-59[»]
4V73electron microscopy15.00BZ1-59[»]
4V74electron microscopy17.00BZ1-59[»]
4V75electron microscopy12.00BZ1-59[»]
4V76electron microscopy17.00BZ1-59[»]
4V77electron microscopy17.00BZ1-59[»]
4V78electron microscopy20.00BZ1-59[»]
4V79electron microscopy15.00BZ1-59[»]
4V7Aelectron microscopy9.00BZ1-59[»]
4V7Belectron microscopy6.80BZ1-59[»]
4V7Celectron microscopy7.60B22-59[»]
4V7Delectron microscopy7.60A32-59[»]
4V7Ielectron microscopy9.60AZ1-59[»]
4V7SX-ray3.25BZ/DZ2-59[»]
4V7TX-ray3.19BZ/DZ2-59[»]
4V7UX-ray3.10BZ/DZ2-59[»]
4V7VX-ray3.29BZ/DZ2-59[»]
4V85X-ray3.2031-59[»]
4V89X-ray3.70B31-59[»]
4V9CX-ray3.30BZ/DZ1-59[»]
4V9DX-ray3.00CZ/DZ2-59[»]
4V9OX-ray2.90AZ/CZ/EZ/GZ1-59[»]
4V9PX-ray2.90AZ/CZ/EZ/GZ1-59[»]
4WF1X-ray3.09BZ/DZ2-59[»]
4WWWX-ray3.10RZ/YZ2-59[»]
4YBBX-ray2.10C0/D02-59[»]
5AFIelectron microscopy2.90Z1-59[»]
5AKAelectron microscopy5.70Y2-59[»]
ProteinModelPortaliP0AG51.
SMRiP0AG51. Positions 2-59.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-35970N.
IntActiP0AG51. 3 interactions.
STRINGi511145.b3302.

Chemistry

ChEMBLiCHEMBL2363135.

Proteomic databases

PaxDbiP0AG51.
PRIDEiP0AG51.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76327; AAC76327; b3302.
BAE77989; BAE77989; BAE77989.
GeneIDi947797.
KEGGieco:b3302.
PATRICi32122036. VBIEscCol129921_3395.

Organism-specific databases

EchoBASEiEB0881.
EcoGeneiEG10888. rpmD.

Phylogenomic databases

eggNOGiCOG1841.
HOGENOMiHOG000039916.
InParanoidiP0AG51.
KOiK02907.
OMAiIRTVAHL.
OrthoDBiEOG6BGP7P.
PhylomeDBiP0AG51.

Enzyme and pathway databases

BioCyciEcoCyc:EG10888-MONOMER.
ECOL316407:JW3264-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AG51.
PROiP0AG51.

Family and domain databases

Gene3Di3.30.1390.20. 1 hit.
HAMAPiMF_01371_B. Ribosomal_L30_B.
InterProiIPR005996. Ribosomal_L30_bac-type.
IPR018038. Ribosomal_L30_CS.
IPR016082. Ribosomal_L30_ferredoxin-like.
[Graphical view]
PfamiPF00327. Ribosomal_L30. 1 hit.
[Graphical view]
PIRSFiPIRSF002211. Ribosomal_L30_bac-type. 1 hit.
SUPFAMiSSF55129. SSF55129. 1 hit.
TIGRFAMsiTIGR01308. rpmD_bact. 1 hit.
PROSITEiPS00634. RIBOSOMAL_L30. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The spc ribosomal protein operon of Escherichia coli: sequence and cotranscription of the ribosomal protein genes and a protein export gene."
    Cerretti D.P., Dean D., Davis G.R., Bedwell D.M., Nomura M.
    Nucleic Acids Res. 11:2599-2616(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "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.
  4. "The primary structure of protein L30 from Escherichia coli ribosomes."
    Ritter E., Wittmann-Liebold B.
    FEBS Lett. 60:153-155(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-59.
    Strain: K.
  5. "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.
  6. "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.
  7. "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.
  8. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.
  9. "Molecular basis for the ribosome functioning as an L-tryptophan sensor."
    Bischoff L., Berninghausen O., Beckmann R.
    Cell Rep. 9:469-475(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF 2-59 IN TNAC-STALLED 50S RIBOSOMAL SUBUNIT.
    Strain: K12 / A19 / KC6.

Entry informationi

Entry nameiRL30_ECOLI
AccessioniPrimary (citable) accession number: P0AG51
Secondary accession number(s): P02430, Q2M6W7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

This protein is located near the guanosine triphosphatase center of the 50S subunit.

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

External Data

Dasty 3

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 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.