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P0A7N9 (RL33_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
50S ribosomal protein L33
Gene names
Name:rpmG
Ordered Locus Names:b3636, JW3611
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length55 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Subunit structure

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

Miscellaneous

Surface exposed on the 50S subunit.

Sequence similarities

Belongs to the ribosomal protein L33P family.

Mass spectrometry

Molecular mass is 6254.1 Da from positions 2 - 55. Determined by MALDI. Ref.7

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 555450S ribosomal protein L33 HAMAP-Rule MF_00294
PRO_0000170158

Amino acid modifications

Modified residue21N-methylalanine HAMAP-Rule MF_00294

Experimental info

Sequence conflict48 – 492IY → YI AA sequence Ref.5

Secondary structure

........... 55
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A7N9 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 31681CC3DAC0C5D6

FASTA556,372
        10         20         30         40         50 
MAKGIREKIK LVSSAGTGHF YTTTKNKRTK PEKLELKKFD PVVRQHVIYK EAKIK 

« Hide

References

« Hide 'large scale' references
[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]"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 277:1453-1462(1997) [PubMed] [Europe PMC] [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] [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.
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]"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] [Europe PMC] [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
J01677 Genomic DNA. Translation: AAA74100.1.
L10328 Genomic DNA. Translation: AAA61989.1.
U00096 Genomic DNA. Translation: AAC76660.1.
AP009048 Genomic DNA. Translation: BAE77656.1.
PIRR5EC33. S42444.
RefSeqNP_418093.1. NC_000913.3.
YP_491797.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
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[»]
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[»]
DisProtDP00143.
ProteinModelPortalP0A7N9.
SMRP0A7N9. Positions 2-53.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-35968N.
IntActP0A7N9. 53 interactions.
MINTMINT-1234559.
STRING511145.b3636.

Chemistry

ChEMBLCHEMBL2363135.

Proteomic databases

PaxDbP0A7N9.
PRIDEP0A7N9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76660; AAC76660; b3636.
BAE77656; BAE77656; BAE77656.
GeneID12931828.
946318.
KEGGecj:Y75_p3538.
eco:b3636.
PATRIC32122759. VBIEscCol129921_3756.

Organism-specific databases

EchoBASEEB0884.
EcoGeneEG10891. rpmG.

Phylogenomic databases

eggNOGCOG0267.
HOGENOMHOG000004839.
KOK02913.
OMAVIYREAK.
OrthoDBEOG60KNBM.
PhylomeDBP0A7N9.

Enzyme and pathway databases

BioCycEcoCyc:EG10891-MONOMER.
ECOL316407:JW3611-MONOMER.

Gene expression databases

GenevestigatorP0A7N9.

Family and domain databases

HAMAPMF_00294. Ribosomal_L33.
InterProIPR001705. Ribosomal_L33.
IPR018264. Ribosomal_L33_CS.
IPR011332. Ribosomal_zn-bd.
[Graphical view]
PfamPF00471. Ribosomal_L33. 1 hit.
[Graphical view]
SUPFAMSSF57829. SSF57829. 1 hit.
TIGRFAMsTIGR01023. rpmG_bact. 1 hit.
PROSITEPS00582. RIBOSOMAL_L33. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A7N9.
PROP0A7N9.

Entry information

Entry nameRL33_ECOLI
AccessionPrimary (citable) accession number: P0A7N9
Secondary accession number(s): P02436, Q2M7V0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

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