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P0A7N9

- RL33_ECOLI

UniProt

P0A7N9 - RL33_ECOLI

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Protein
50S ribosomal protein L33
Gene
rpmG, b3636, JW3611
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

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

GO - Biological processi

  1. translation Source: InterPro
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 L33UniRule annotation
PRO_0000170158Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-methylalanineUniRule annotation

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

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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[»]
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[»]
DisProtiDP00143.
ProteinModelPortaliP0A7N9.
SMRiP0A7N9. Positions 2-53.

Miscellaneous databases

EvolutionaryTraceiP0A7N9.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0267.
HOGENOMiHOG000004839.
KOiK02913.
OMAiVIYREAK.
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

MAKGIREKIK LVSSAGTGHF YTTTKNKRTK PEKLELKKFD PVVRQHVIYK   50
EAKIK 55
Length:55
Mass (Da):6,372
Last modified:January 23, 2007 - v2
Checksum:i31681CC3DAC0C5D6
GO

Mass spectrometryi

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 492IY → YI AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi S42444. R5EC33.
RefSeqi NP_418093.1. NC_000913.3.
YP_491797.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1P85 electron microscopy 12.30 1 2-55 [» ]
1P86 electron microscopy 11.50 1 2-55 [» ]
1VS6 X-ray 3.46 1 1-55 [» ]
1VS8 X-ray 3.46 1 1-55 [» ]
1VT2 X-ray 3.30 1 1-55 [» ]
2AW4 X-ray 3.46 1 2-55 [» ]
2AWB X-ray 3.46 1 2-55 [» ]
2GYA electron microscopy 15.00 1 2-53 [» ]
2GYC electron microscopy 15.00 1 2-53 [» ]
2I2T X-ray 3.22 1 2-55 [» ]
2I2V X-ray 3.22 1 2-55 [» ]
2J28 electron microscopy 8.00 1 2-55 [» ]
2QAM X-ray 3.21 1 2-55 [» ]
2QAO X-ray 3.21 1 2-55 [» ]
2QBA X-ray 3.54 1 2-55 [» ]
2QBC X-ray 3.54 1 2-55 [» ]
2QBE X-ray 3.30 1 2-55 [» ]
2QBG X-ray 3.30 1 2-55 [» ]
2QBI X-ray 4.00 1 2-55 [» ]
2QBK X-ray 4.00 1 2-55 [» ]
2QOV X-ray 3.93 1 2-55 [» ]
2QOX X-ray 3.93 1 2-55 [» ]
2QOZ X-ray 3.50 1 2-55 [» ]
2QP1 X-ray 3.50 1 2-55 [» ]
2RDO electron microscopy 9.10 1 2-55 [» ]
2VHM X-ray 3.74 1 2-55 [» ]
2VHN X-ray 3.74 1 2-55 [» ]
2WWQ electron microscopy 5.80 4 4-53 [» ]
2Z4L X-ray 4.45 1 2-55 [» ]
2Z4N X-ray 4.45 1 2-55 [» ]
3BBX electron microscopy 10.00 1 2-55 [» ]
3DF2 X-ray 3.50 1 2-54 [» ]
3DF4 X-ray 3.50 1 2-54 [» ]
3E1B electron microscopy - U 2-55 [» ]
3E1D electron microscopy - U 2-55 [» ]
3FIK electron microscopy 6.70 1 4-53 [» ]
3I1N X-ray 3.19 1 1-55 [» ]
3I1P X-ray 3.19 1 1-55 [» ]
3I1R X-ray 3.81 1 1-55 [» ]
3I1T X-ray 3.81 1 1-55 [» ]
3I20 X-ray 3.71 1 1-55 [» ]
3I22 X-ray 3.71 1 1-55 [» ]
3IZT electron microscopy - d 1-55 [» ]
3IZU electron microscopy - d 1-55 [» ]
3J01 electron microscopy - 1 2-55 [» ]
3J0T electron microscopy 12.10 4 2-55 [» ]
3J0W electron microscopy 14.70 4 2-55 [» ]
3J0Y electron microscopy 13.50 4 2-55 [» ]
3J11 electron microscopy 13.10 4 2-55 [» ]
3J12 electron microscopy 11.50 4 2-55 [» ]
3J14 electron microscopy 11.50 4 2-55 [» ]
3J19 electron microscopy 8.30 1 4-53 [» ]
3J37 electron microscopy 9.80 6 2-55 [» ]
3J4X electron microscopy 12.00 1 4-53 [» ]
3J50 electron microscopy 20.00 1 4-53 [» ]
3J51 electron microscopy 17.00 1 4-53 [» ]
3J52 electron microscopy 12.00 1 4-53 [» ]
3J54 electron microscopy 13.00 1 4-53 [» ]
3J56 electron microscopy 15.00 1 4-53 [» ]
3J58 electron microscopy 17.00 1 4-53 [» ]
3J5A electron microscopy 12.00 1 4-53 [» ]
3J5C electron microscopy 17.00 1 4-53 [» ]
3J5E electron microscopy 17.00 1 4-53 [» ]
3J5G electron microscopy 20.00 1 4-53 [» ]
3J5I electron microscopy 15.00 1 4-53 [» ]
3J5K electron microscopy 9.00 1 4-53 [» ]
3J5L electron microscopy 6.60 1 4-53 [» ]
3J5O electron microscopy 6.80 1 1-55 [» ]
3J5S electron microscopy 7.50 H 4-53 [» ]
3J5U electron microscopy 7.60 4 2-55 [» ]
3J5W electron microscopy 7.60 5 2-55 [» ]
3KCR electron microscopy - 1 1-55 [» ]
3OAS X-ray 3.25 1 4-53 [» ]
3OAT X-ray 3.25 1 4-53 [» ]
3OFC X-ray 3.19 1 4-53 [» ]
3OFD X-ray 3.19 1 4-53 [» ]
3OFQ X-ray 3.10 1 4-53 [» ]
3OFR X-ray 3.10 1 4-53 [» ]
3OFZ X-ray 3.29 1 4-53 [» ]
3OG0 X-ray 3.29 1 4-53 [» ]
3ORB X-ray 3.30 1 1-55 [» ]
3R8S X-ray 3.00 1 4-53 [» ]
3R8T X-ray 3.00 1 4-53 [» ]
3SGF X-ray 3.20 5 1-55 [» ]
3UOS X-ray 3.70 5 1-55 [» ]
4CSU electron microscopy 5.50 4 2-55 [» ]
4GAR X-ray 3.30 1 1-55 [» ]
4GAU X-ray 3.30 1 1-55 [» ]
4KIX X-ray 2.90 1 1-55 [» ]
4KIZ X-ray 2.90 1 1-55 [» ]
4KJ1 X-ray 2.90 1 1-55 [» ]
4KJ3 X-ray 2.90 1 1-55 [» ]
4KJ5 X-ray 2.90 1 1-55 [» ]
4KJ7 X-ray 2.90 1 1-55 [» ]
4KJ9 X-ray 2.90 1 1-55 [» ]
4KJB X-ray 2.90 1 1-55 [» ]
DisProti DP00143.
ProteinModelPortali P0A7N9.
SMRi P0A7N9. Positions 2-53.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-35968N.
IntActi P0A7N9. 53 interactions.
MINTi MINT-1234559.
STRINGi 511145.b3636.

Chemistry

ChEMBLi CHEMBL2363135.

Proteomic databases

PaxDbi P0A7N9.
PRIDEi P0A7N9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76660 ; AAC76660 ; b3636 .
BAE77656 ; BAE77656 ; BAE77656 .
GeneIDi 12931828.
946318.
KEGGi ecj:Y75_p3538.
eco:b3636.
PATRICi 32122759. VBIEscCol129921_3756.

Organism-specific databases

EchoBASEi EB0884.
EcoGenei EG10891. rpmG.

Phylogenomic databases

eggNOGi COG0267.
HOGENOMi HOG000004839.
KOi K02913.
OMAi VIYREAK.
OrthoDBi EOG60KNBM.
PhylomeDBi P0A7N9.

Enzyme and pathway databases

BioCyci EcoCyc:EG10891-MONOMER.
ECOL316407:JW3611-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A7N9.
PROi P0A7N9.

Gene expression databases

Genevestigatori P0A7N9.

Family and domain databases

HAMAPi MF_00294. Ribosomal_L33.
InterProi IPR001705. Ribosomal_L33.
IPR018264. Ribosomal_L33_CS.
IPR011332. Ribosomal_zn-bd.
[Graphical view ]
Pfami PF00471. Ribosomal_L33. 1 hit.
[Graphical view ]
SUPFAMi SSF57829. SSF57829. 1 hit.
TIGRFAMsi TIGR01023. rpmG_bact. 1 hit.
PROSITEi PS00582. RIBOSOMAL_L33. 1 hit.
[Graphical view ]
ProtoNeti Search...

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.
    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: September 3, 2014
This is version 97 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