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Protein

50S ribosomal protein L33

Gene

rpmG

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

Functioni

GO - Molecular functioni

  1. structural constituent of ribosome Source: GO_Central
  2. tRNA binding Source: UniProtKB-KW

GO - Biological processi

  1. translation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, tRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10891-MONOMER.
ECOL316407:JW3611-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L33
Gene namesi
Name:rpmG
Ordered Locus Names:b3636, JW3611
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10891. rpmG.

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 – 555450S ribosomal protein L33PRO_0000170158Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-methylalanine1 Publication

Keywords - PTMi

Methylation

Proteomic databases

PaxDbiP0A7N9.
PRIDEiP0A7N9.

Expressioni

Gene expression databases

GenevestigatoriP0A7N9.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Cross-links to the P and E site tRNAs.

Protein-protein interaction databases

DIPiDIP-35968N.
IntActiP0A7N9. 53 interactions.
MINTiMINT-1234559.
STRINGi511145.b3636.

Structurei

Secondary structure

1
55
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 1711Combined sources
Beta strandi20 – 256Combined sources
Turni27 – 293Combined sources
Beta strandi36 – 405Combined sources
Turni41 – 444Combined sources
Beta strandi45 – 506Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1P85electron microscopy12.3012-55[»]
1P86electron microscopy11.5012-55[»]
1VS6X-ray3.4611-55[»]
1VS8X-ray3.4611-55[»]
1VT2X-ray3.3011-55[»]
2AW4X-ray3.4612-55[»]
2AWBX-ray3.4612-55[»]
2GYAelectron microscopy15.0012-53[»]
2GYCelectron microscopy15.0012-53[»]
2I2TX-ray3.2212-55[»]
2I2VX-ray3.2212-55[»]
2J28electron microscopy8.0012-55[»]
2QAMX-ray3.2112-55[»]
2QAOX-ray3.2112-55[»]
2QBAX-ray3.5412-55[»]
2QBCX-ray3.5412-55[»]
2QBEX-ray3.3012-55[»]
2QBGX-ray3.3012-55[»]
2QBIX-ray4.0012-55[»]
2QBKX-ray4.0012-55[»]
2QOVX-ray3.9312-55[»]
2QOXX-ray3.9312-55[»]
2QOZX-ray3.5012-55[»]
2QP1X-ray3.5012-55[»]
2RDOelectron microscopy9.1012-55[»]
2VHMX-ray3.7412-55[»]
2VHNX-ray3.7412-55[»]
2WWQelectron microscopy5.8044-53[»]
2Z4LX-ray4.4512-55[»]
2Z4NX-ray4.4512-55[»]
3BBXelectron microscopy10.0012-55[»]
3DF2X-ray3.5012-54[»]
3DF4X-ray3.5012-54[»]
3E1Belectron microscopy-U2-55[»]
3E1Delectron microscopy-U2-55[»]
3FIKelectron microscopy6.7014-53[»]
3I1NX-ray3.1911-55[»]
3I1PX-ray3.1911-55[»]
3I1RX-ray3.8111-55[»]
3I1TX-ray3.8111-55[»]
3I20X-ray3.7111-55[»]
3I22X-ray3.7111-55[»]
3IZTelectron microscopy-d1-55[»]
3IZUelectron microscopy-d1-55[»]
3J01electron microscopy-12-55[»]
3J0Telectron microscopy12.1042-55[»]
3J0Welectron microscopy14.7042-55[»]
3J0Yelectron microscopy13.5042-55[»]
3J11electron microscopy13.1042-55[»]
3J12electron microscopy11.5042-55[»]
3J14electron microscopy11.5042-55[»]
3J19electron microscopy8.3014-53[»]
3J37electron microscopy9.8062-55[»]
3J4Xelectron microscopy12.0014-53[»]
3J50electron microscopy20.0014-53[»]
3J51electron microscopy17.0014-53[»]
3J52electron microscopy12.0014-53[»]
3J54electron microscopy13.0014-53[»]
3J56electron microscopy15.0014-53[»]
3J58electron microscopy17.0014-53[»]
3J5Aelectron microscopy12.0014-53[»]
3J5Celectron microscopy17.0014-53[»]
3J5Eelectron microscopy17.0014-53[»]
3J5Gelectron microscopy20.0014-53[»]
3J5Ielectron microscopy15.0014-53[»]
3J5Kelectron microscopy9.0014-53[»]
3J5Lelectron microscopy6.6014-53[»]
3J5Oelectron microscopy6.8011-55[»]
3J5Selectron microscopy7.50H4-53[»]
3J5Uelectron microscopy7.6042-55[»]
3J5Welectron microscopy7.6052-55[»]
3J7Zelectron microscopy3.9011-55[»]
3KCRelectron microscopy-11-55[»]
3OASX-ray3.2514-53[»]
3OATX-ray3.2514-53[»]
3OFCX-ray3.1914-53[»]
3OFDX-ray3.1914-53[»]
3OFQX-ray3.1014-53[»]
3OFRX-ray3.1014-53[»]
3OFZX-ray3.2914-53[»]
3OG0X-ray3.2914-53[»]
3ORBX-ray3.3011-55[»]
3R8SX-ray3.0014-53[»]
3R8TX-ray3.0014-53[»]
3SGFX-ray3.2051-55[»]
3UOSX-ray3.7051-55[»]
4CSUelectron microscopy5.5042-55[»]
4GARX-ray3.3011-55[»]
4GAUX-ray3.3011-55[»]
4KIXX-ray2.9011-55[»]
4KIZX-ray2.9011-55[»]
4KJ1X-ray2.9011-55[»]
4KJ3X-ray2.9011-55[»]
4KJ5X-ray2.9011-55[»]
4KJ7X-ray2.9011-55[»]
4KJ9X-ray2.9011-55[»]
4KJBX-ray2.9011-55[»]
4PEBX-ray2.9514-53[»]
4PECX-ray2.9514-53[»]
4TOMX-ray3.0014-53[»]
4TOOX-ray3.0014-53[»]
4TOVX-ray2.9014-53[»]
4TOXX-ray2.9014-53[»]
4TP1X-ray2.9014-53[»]
4TP3X-ray2.9014-53[»]
4TP5X-ray2.9014-53[»]
4TP7X-ray2.9014-53[»]
4TP9X-ray2.8014-53[»]
4TPBX-ray2.8014-53[»]
4TPDX-ray2.8014-53[»]
4TPFX-ray2.8014-53[»]
4WAPX-ray3.0914-53[»]
4WARX-ray3.0914-53[»]
DisProtiDP00143.
ProteinModelPortaliP0A7N9.
SMRiP0A7N9. Positions 2-53.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7N9.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L33P family.Curated

Phylogenomic databases

eggNOGiCOG0267.
HOGENOMiHOG000004839.
InParanoidiP0A7N9.
KOiK02913.
OMAiHVLYKET.
OrthoDBiEOG60KNBM.
PhylomeDBiP0A7N9.

Family and domain databases

HAMAPiMF_00294. Ribosomal_L33.
InterProiIPR001705. Ribosomal_L33.
IPR018264. Ribosomal_L33_CS.
IPR011332. Ribosomal_zn-bd.
[Graphical view]
PfamiPF00471. Ribosomal_L33. 1 hit.
[Graphical view]
SUPFAMiSSF57829. SSF57829. 1 hit.
TIGRFAMsiTIGR01023. rpmG_bact. 1 hit.
PROSITEiPS00582. RIBOSOMAL_L33. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0A7N9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAKGIREKIK LVSSAGTGHF YTTTKNKRTK PEKLELKKFD PVVRQHVIYK

EAKIK
Length:55
Mass (Da):6,372
Last modified:January 23, 2007 - v2
Checksum:i31681CC3DAC0C5D6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 492IY → YI AA sequence (PubMed:786732)Curated

Mass spectrometryi

Molecular mass is 6254.1 Da from positions 2 - 55. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01677 Genomic DNA. Translation: AAA74100.1.
L10328 Genomic DNA. Translation: AAA61989.1.
U00096 Genomic DNA. Translation: AAC76660.1.
AP009048 Genomic DNA. Translation: BAE77656.1.
PIRiS42444. R5EC33.
RefSeqiNP_418093.1. NC_000913.3.
YP_491797.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76660; AAC76660; b3636.
BAE77656; BAE77656; BAE77656.
GeneIDi12931828.
946318.
KEGGiecj:Y75_p3538.
eco:b3636.
PATRICi32122759. VBIEscCol129921_3756.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01677 Genomic DNA. Translation: AAA74100.1.
L10328 Genomic DNA. Translation: AAA61989.1.
U00096 Genomic DNA. Translation: AAC76660.1.
AP009048 Genomic DNA. Translation: BAE77656.1.
PIRiS42444. R5EC33.
RefSeqiNP_418093.1. NC_000913.3.
YP_491797.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1P85electron microscopy12.3012-55[»]
1P86electron microscopy11.5012-55[»]
1VS6X-ray3.4611-55[»]
1VS8X-ray3.4611-55[»]
1VT2X-ray3.3011-55[»]
2AW4X-ray3.4612-55[»]
2AWBX-ray3.4612-55[»]
2GYAelectron microscopy15.0012-53[»]
2GYCelectron microscopy15.0012-53[»]
2I2TX-ray3.2212-55[»]
2I2VX-ray3.2212-55[»]
2J28electron microscopy8.0012-55[»]
2QAMX-ray3.2112-55[»]
2QAOX-ray3.2112-55[»]
2QBAX-ray3.5412-55[»]
2QBCX-ray3.5412-55[»]
2QBEX-ray3.3012-55[»]
2QBGX-ray3.3012-55[»]
2QBIX-ray4.0012-55[»]
2QBKX-ray4.0012-55[»]
2QOVX-ray3.9312-55[»]
2QOXX-ray3.9312-55[»]
2QOZX-ray3.5012-55[»]
2QP1X-ray3.5012-55[»]
2RDOelectron microscopy9.1012-55[»]
2VHMX-ray3.7412-55[»]
2VHNX-ray3.7412-55[»]
2WWQelectron microscopy5.8044-53[»]
2Z4LX-ray4.4512-55[»]
2Z4NX-ray4.4512-55[»]
3BBXelectron microscopy10.0012-55[»]
3DF2X-ray3.5012-54[»]
3DF4X-ray3.5012-54[»]
3E1Belectron microscopy-U2-55[»]
3E1Delectron microscopy-U2-55[»]
3FIKelectron microscopy6.7014-53[»]
3I1NX-ray3.1911-55[»]
3I1PX-ray3.1911-55[»]
3I1RX-ray3.8111-55[»]
3I1TX-ray3.8111-55[»]
3I20X-ray3.7111-55[»]
3I22X-ray3.7111-55[»]
3IZTelectron microscopy-d1-55[»]
3IZUelectron microscopy-d1-55[»]
3J01electron microscopy-12-55[»]
3J0Telectron microscopy12.1042-55[»]
3J0Welectron microscopy14.7042-55[»]
3J0Yelectron microscopy13.5042-55[»]
3J11electron microscopy13.1042-55[»]
3J12electron microscopy11.5042-55[»]
3J14electron microscopy11.5042-55[»]
3J19electron microscopy8.3014-53[»]
3J37electron microscopy9.8062-55[»]
3J4Xelectron microscopy12.0014-53[»]
3J50electron microscopy20.0014-53[»]
3J51electron microscopy17.0014-53[»]
3J52electron microscopy12.0014-53[»]
3J54electron microscopy13.0014-53[»]
3J56electron microscopy15.0014-53[»]
3J58electron microscopy17.0014-53[»]
3J5Aelectron microscopy12.0014-53[»]
3J5Celectron microscopy17.0014-53[»]
3J5Eelectron microscopy17.0014-53[»]
3J5Gelectron microscopy20.0014-53[»]
3J5Ielectron microscopy15.0014-53[»]
3J5Kelectron microscopy9.0014-53[»]
3J5Lelectron microscopy6.6014-53[»]
3J5Oelectron microscopy6.8011-55[»]
3J5Selectron microscopy7.50H4-53[»]
3J5Uelectron microscopy7.6042-55[»]
3J5Welectron microscopy7.6052-55[»]
3J7Zelectron microscopy3.9011-55[»]
3KCRelectron microscopy-11-55[»]
3OASX-ray3.2514-53[»]
3OATX-ray3.2514-53[»]
3OFCX-ray3.1914-53[»]
3OFDX-ray3.1914-53[»]
3OFQX-ray3.1014-53[»]
3OFRX-ray3.1014-53[»]
3OFZX-ray3.2914-53[»]
3OG0X-ray3.2914-53[»]
3ORBX-ray3.3011-55[»]
3R8SX-ray3.0014-53[»]
3R8TX-ray3.0014-53[»]
3SGFX-ray3.2051-55[»]
3UOSX-ray3.7051-55[»]
4CSUelectron microscopy5.5042-55[»]
4GARX-ray3.3011-55[»]
4GAUX-ray3.3011-55[»]
4KIXX-ray2.9011-55[»]
4KIZX-ray2.9011-55[»]
4KJ1X-ray2.9011-55[»]
4KJ3X-ray2.9011-55[»]
4KJ5X-ray2.9011-55[»]
4KJ7X-ray2.9011-55[»]
4KJ9X-ray2.9011-55[»]
4KJBX-ray2.9011-55[»]
4PEBX-ray2.9514-53[»]
4PECX-ray2.9514-53[»]
4TOMX-ray3.0014-53[»]
4TOOX-ray3.0014-53[»]
4TOVX-ray2.9014-53[»]
4TOXX-ray2.9014-53[»]
4TP1X-ray2.9014-53[»]
4TP3X-ray2.9014-53[»]
4TP5X-ray2.9014-53[»]
4TP7X-ray2.9014-53[»]
4TP9X-ray2.8014-53[»]
4TPBX-ray2.8014-53[»]
4TPDX-ray2.8014-53[»]
4TPFX-ray2.8014-53[»]
4WAPX-ray3.0914-53[»]
4WARX-ray3.0914-53[»]
DisProtiDP00143.
ProteinModelPortaliP0A7N9.
SMRiP0A7N9. Positions 2-53.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-35968N.
IntActiP0A7N9. 53 interactions.
MINTiMINT-1234559.
STRINGi511145.b3636.

Chemistry

ChEMBLiCHEMBL2363135.

Proteomic databases

PaxDbiP0A7N9.
PRIDEiP0A7N9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76660; AAC76660; b3636.
BAE77656; BAE77656; BAE77656.
GeneIDi12931828.
946318.
KEGGiecj:Y75_p3538.
eco:b3636.
PATRICi32122759. VBIEscCol129921_3756.

Organism-specific databases

EchoBASEiEB0884.
EcoGeneiEG10891. rpmG.

Phylogenomic databases

eggNOGiCOG0267.
HOGENOMiHOG000004839.
InParanoidiP0A7N9.
KOiK02913.
OMAiHVLYKET.
OrthoDBiEOG60KNBM.
PhylomeDBiP0A7N9.

Enzyme and pathway databases

BioCyciEcoCyc:EG10891-MONOMER.
ECOL316407:JW3611-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A7N9.
PROiP0A7N9.

Gene expression databases

GenevestigatoriP0A7N9.

Family and domain databases

HAMAPiMF_00294. Ribosomal_L33.
InterProiIPR001705. Ribosomal_L33.
IPR018264. Ribosomal_L33_CS.
IPR011332. Ribosomal_zn-bd.
[Graphical view]
PfamiPF00471. Ribosomal_L33. 1 hit.
[Graphical view]
SUPFAMiSSF57829. SSF57829. 1 hit.
TIGRFAMsiTIGR01023. rpmG_bact. 1 hit.
PROSITEiPS00582. RIBOSOMAL_L33. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and the nucleotide sequence of the genes for Escherichia coli ribosomal proteins L28 (rpmB) and L33 (rpmG)."
    Lee J.S., An G., Friesen J.D., Isono K.
    Mol. Gen. Genet. 184:218-223(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication."
    Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.
    Genomics 16:551-561(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. 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. "Primary structure of protein L33 from the large subunit of the Escherichia coli ribosome."
    Wittmann-Liebold B., Pannenbecker R.
    FEBS Lett. 68:115-118(1976) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-55, METHYLATION AT ALA-2.
    Strain: K.
  6. "The ribosomal neighbourhood of the central fold of tRNA: cross-links from position 47 of tRNA located at the A, P or E site."
    Osswald M., Doering T., Brimacombe R.
    Nucleic Acids Res. 23:4635-4641(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: CROSS-LINKING TO THE TRNA CENTRAL FOLD.
    Strain: MRE-600.
  7. "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.
  8. "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.
  9. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.

Entry informationi

Entry nameiRL33_ECOLI
AccessioniPrimary (citable) accession number: P0A7N9
Secondary accession number(s): P02436, Q2M7V0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: February 4, 2015
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Surface exposed on 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.