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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

  1. structural constituent of ribosome Source: InterPro

GO - Biological processi

  1. translation Source: UniProtKB-HAMAP
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: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10888. rpmD.

Subcellular locationi

GO - Cellular componenti

  1. 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.

Expressioni

Gene expression databases

GenevestigatoriP0AG51.

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[»]
1P85electron microscopy12.30X2-59[»]
1P86electron microscopy11.50X2-59[»]
1VS6X-ray3.46Y1-59[»]
1VS8X-ray3.46Y1-59[»]
1VT2X-ray3.30Z1-59[»]
2AW4X-ray3.46Y2-59[»]
2AWBX-ray3.46Y2-59[»]
2GYAelectron microscopy15.00X4-59[»]
2GYCelectron microscopy15.00X4-59[»]
2I2TX-ray3.22Z2-59[»]
2I2VX-ray3.22Z2-59[»]
2J28electron microscopy8.00Y2-59[»]
2QAMX-ray3.21Y2-59[»]
2QAOX-ray3.21Y2-59[»]
2QBAX-ray3.54Y2-59[»]
2QBCX-ray3.54Y2-59[»]
2QBEX-ray3.30Y2-59[»]
2QBGX-ray3.30Y2-59[»]
2QBIX-ray4.00Y2-59[»]
2QBKX-ray4.00Y2-59[»]
2QOVX-ray3.93Y2-59[»]
2QOXX-ray3.93Y2-59[»]
2QOZX-ray3.50Y2-59[»]
2QP1X-ray3.50Y2-59[»]
2RDOelectron microscopy9.10Y2-59[»]
2WWQelectron microscopy5.8022-59[»]
2Z4LX-ray4.45Y2-59[»]
2Z4NX-ray4.45Y2-59[»]
3BBXelectron microscopy10.00Y2-59[»]
3E1Belectron microscopy-R1-59[»]
3E1Delectron microscopy-R1-59[»]
3FIKelectron microscopy6.70Z2-59[»]
3I1NX-ray3.19Z1-59[»]
3I1PX-ray3.19Z1-59[»]
3I1RX-ray3.81Z1-59[»]
3I1TX-ray3.81Z1-59[»]
3I20X-ray3.71Z1-59[»]
3I22X-ray3.71Z1-59[»]
3IZTelectron microscopy-a1-59[»]
3IZUelectron microscopy-a1-59[»]
3J01electron microscopy-Z2-59[»]
3J0Telectron microscopy12.1012-59[»]
3J0Welectron microscopy14.7012-59[»]
3J0Yelectron microscopy13.5012-59[»]
3J11electron microscopy13.1012-59[»]
3J12electron microscopy11.5012-59[»]
3J14electron microscopy11.5012-59[»]
3J19electron microscopy8.30Z2-59[»]
3J37electron microscopy9.8032-59[»]
3J4Xelectron microscopy12.00Z1-59[»]
3J50electron microscopy20.00Z1-59[»]
3J51electron microscopy17.00Z1-59[»]
3J52electron microscopy12.00Z1-59[»]
3J54electron microscopy13.00Z1-59[»]
3J56electron microscopy15.00Z1-59[»]
3J58electron microscopy17.00Z1-59[»]
3J5Aelectron microscopy12.00Z1-59[»]
3J5Celectron microscopy17.00Z1-59[»]
3J5Eelectron microscopy17.00Z1-59[»]
3J5Gelectron microscopy20.00Z1-59[»]
3J5Ielectron microscopy15.00Z1-59[»]
3J5Kelectron microscopy9.00Z1-59[»]
3J5Lelectron microscopy6.60Z2-59[»]
3J5Oelectron microscopy6.80Z1-59[»]
3J5Uelectron microscopy7.6022-59[»]
3J5Welectron microscopy7.6032-59[»]
3J7Zelectron microscopy3.90Z1-59[»]
3KCRelectron microscopy-Z1-59[»]
3OASX-ray3.25Z2-59[»]
3OATX-ray3.25Z2-59[»]
3OFCX-ray3.19Z2-59[»]
3OFDX-ray3.19Z2-59[»]
3OFQX-ray3.10Z2-59[»]
3OFRX-ray3.10Z2-59[»]
3OFZX-ray3.29Z2-59[»]
3OG0X-ray3.29Z2-59[»]
3ORBX-ray3.30Z1-59[»]
3R8SX-ray3.00Z2-59[»]
3R8TX-ray3.00Z2-59[»]
3SGFX-ray3.2031-59[»]
3UOSX-ray3.7031-59[»]
4CSUelectron microscopy5.5022-59[»]
4GARX-ray3.30Z1-59[»]
4GAUX-ray3.30Z1-59[»]
4KIXX-ray2.90Z1-59[»]
4KIZX-ray2.90Z1-59[»]
4KJ1X-ray2.90Z1-59[»]
4KJ3X-ray2.90Z1-59[»]
4KJ5X-ray2.90Z1-59[»]
4KJ7X-ray2.90Z1-59[»]
4KJ9X-ray2.90Z1-59[»]
4KJBX-ray2.90Z1-59[»]
4PEBX-ray2.95Z2-59[»]
4PECX-ray2.95Z2-59[»]
4TOMX-ray3.00Z2-59[»]
4TOOX-ray3.00Z2-59[»]
4TOVX-ray2.90Z2-59[»]
4TOXX-ray2.90Z2-59[»]
4TP1X-ray2.90Z2-59[»]
4TP3X-ray2.90Z2-59[»]
4TP5X-ray2.90Z2-59[»]
4TP7X-ray2.90Z2-59[»]
4TP9X-ray2.80Z2-59[»]
4TPBX-ray2.80Z2-59[»]
4TPDX-ray2.80Z2-59[»]
4TPFX-ray2.80Z2-59[»]
4WAPX-ray3.09Z2-59[»]
4WARX-ray3.09Z2-59[»]
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.
OMAiQNHRDTL.
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.
YP_492130.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76327; AAC76327; b3302.
BAE77989; BAE77989; BAE77989.
GeneIDi12934448.
947797.
KEGGiecj:Y75_p3874.
eco: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.
YP_492130.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ML5electron microscopy14.00x1-59[»]
1P85electron microscopy12.30X2-59[»]
1P86electron microscopy11.50X2-59[»]
1VS6X-ray3.46Y1-59[»]
1VS8X-ray3.46Y1-59[»]
1VT2X-ray3.30Z1-59[»]
2AW4X-ray3.46Y2-59[»]
2AWBX-ray3.46Y2-59[»]
2GYAelectron microscopy15.00X4-59[»]
2GYCelectron microscopy15.00X4-59[»]
2I2TX-ray3.22Z2-59[»]
2I2VX-ray3.22Z2-59[»]
2J28electron microscopy8.00Y2-59[»]
2QAMX-ray3.21Y2-59[»]
2QAOX-ray3.21Y2-59[»]
2QBAX-ray3.54Y2-59[»]
2QBCX-ray3.54Y2-59[»]
2QBEX-ray3.30Y2-59[»]
2QBGX-ray3.30Y2-59[»]
2QBIX-ray4.00Y2-59[»]
2QBKX-ray4.00Y2-59[»]
2QOVX-ray3.93Y2-59[»]
2QOXX-ray3.93Y2-59[»]
2QOZX-ray3.50Y2-59[»]
2QP1X-ray3.50Y2-59[»]
2RDOelectron microscopy9.10Y2-59[»]
2WWQelectron microscopy5.8022-59[»]
2Z4LX-ray4.45Y2-59[»]
2Z4NX-ray4.45Y2-59[»]
3BBXelectron microscopy10.00Y2-59[»]
3E1Belectron microscopy-R1-59[»]
3E1Delectron microscopy-R1-59[»]
3FIKelectron microscopy6.70Z2-59[»]
3I1NX-ray3.19Z1-59[»]
3I1PX-ray3.19Z1-59[»]
3I1RX-ray3.81Z1-59[»]
3I1TX-ray3.81Z1-59[»]
3I20X-ray3.71Z1-59[»]
3I22X-ray3.71Z1-59[»]
3IZTelectron microscopy-a1-59[»]
3IZUelectron microscopy-a1-59[»]
3J01electron microscopy-Z2-59[»]
3J0Telectron microscopy12.1012-59[»]
3J0Welectron microscopy14.7012-59[»]
3J0Yelectron microscopy13.5012-59[»]
3J11electron microscopy13.1012-59[»]
3J12electron microscopy11.5012-59[»]
3J14electron microscopy11.5012-59[»]
3J19electron microscopy8.30Z2-59[»]
3J37electron microscopy9.8032-59[»]
3J4Xelectron microscopy12.00Z1-59[»]
3J50electron microscopy20.00Z1-59[»]
3J51electron microscopy17.00Z1-59[»]
3J52electron microscopy12.00Z1-59[»]
3J54electron microscopy13.00Z1-59[»]
3J56electron microscopy15.00Z1-59[»]
3J58electron microscopy17.00Z1-59[»]
3J5Aelectron microscopy12.00Z1-59[»]
3J5Celectron microscopy17.00Z1-59[»]
3J5Eelectron microscopy17.00Z1-59[»]
3J5Gelectron microscopy20.00Z1-59[»]
3J5Ielectron microscopy15.00Z1-59[»]
3J5Kelectron microscopy9.00Z1-59[»]
3J5Lelectron microscopy6.60Z2-59[»]
3J5Oelectron microscopy6.80Z1-59[»]
3J5Uelectron microscopy7.6022-59[»]
3J5Welectron microscopy7.6032-59[»]
3J7Zelectron microscopy3.90Z1-59[»]
3KCRelectron microscopy-Z1-59[»]
3OASX-ray3.25Z2-59[»]
3OATX-ray3.25Z2-59[»]
3OFCX-ray3.19Z2-59[»]
3OFDX-ray3.19Z2-59[»]
3OFQX-ray3.10Z2-59[»]
3OFRX-ray3.10Z2-59[»]
3OFZX-ray3.29Z2-59[»]
3OG0X-ray3.29Z2-59[»]
3ORBX-ray3.30Z1-59[»]
3R8SX-ray3.00Z2-59[»]
3R8TX-ray3.00Z2-59[»]
3SGFX-ray3.2031-59[»]
3UOSX-ray3.7031-59[»]
4CSUelectron microscopy5.5022-59[»]
4GARX-ray3.30Z1-59[»]
4GAUX-ray3.30Z1-59[»]
4KIXX-ray2.90Z1-59[»]
4KIZX-ray2.90Z1-59[»]
4KJ1X-ray2.90Z1-59[»]
4KJ3X-ray2.90Z1-59[»]
4KJ5X-ray2.90Z1-59[»]
4KJ7X-ray2.90Z1-59[»]
4KJ9X-ray2.90Z1-59[»]
4KJBX-ray2.90Z1-59[»]
4PEBX-ray2.95Z2-59[»]
4PECX-ray2.95Z2-59[»]
4TOMX-ray3.00Z2-59[»]
4TOOX-ray3.00Z2-59[»]
4TOVX-ray2.90Z2-59[»]
4TOXX-ray2.90Z2-59[»]
4TP1X-ray2.90Z2-59[»]
4TP3X-ray2.90Z2-59[»]
4TP5X-ray2.90Z2-59[»]
4TP7X-ray2.90Z2-59[»]
4TP9X-ray2.80Z2-59[»]
4TPBX-ray2.80Z2-59[»]
4TPDX-ray2.80Z2-59[»]
4TPFX-ray2.80Z2-59[»]
4WAPX-ray3.09Z2-59[»]
4WARX-ray3.09Z2-59[»]
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.
GeneIDi12934448.
947797.
KEGGiecj:Y75_p3874.
eco:b3302.
PATRICi32122036. VBIEscCol129921_3395.

Organism-specific databases

EchoBASEiEB0881.
EcoGeneiEG10888. rpmD.

Phylogenomic databases

eggNOGiCOG1841.
HOGENOMiHOG000039916.
InParanoidiP0AG51.
KOiK02907.
OMAiQNHRDTL.
OrthoDBiEOG6BGP7P.
PhylomeDBiP0AG51.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0AG51.
PROiP0AG51.

Gene expression databases

GenevestigatoriP0AG51.

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.

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: February 4, 2015
This is version 95 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.