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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

GO - Biological processi

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
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10891. rpmG.

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2363135.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 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

EPDiP0A7N9.
PaxDbiP0A7N9.
PRIDEiP0A7N9.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Cross-links to the P and E site tRNAs.1 Publication

Protein-protein interaction databases

BioGridi4260822. 234 interactions.
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
2J28electron microscopy8.0012-55[»]
2RDOelectron microscopy9.1012-55[»]
3BBXelectron microscopy10.0012-55[»]
3J5Lelectron microscopy6.6014-53[»]
3J5Selectron microscopy7.50H4-53[»]
3J7Zelectron microscopy3.9011-55[»]
3J9Yelectron microscopy3.9011-55[»]
3J9Zelectron microscopy3.60L22-55[»]
3JA1electron microscopy3.60L42-55[»]
3JBUelectron microscopy3.6441-55[»]
3JBVelectron microscopy3.3241-55[»]
3JCDelectron microscopy3.7011-55[»]
3JCEelectron microscopy3.2011-55[»]
3JCJelectron microscopy3.70a1-55[»]
3JCNelectron microscopy4.6011-55[»]
4CSUelectron microscopy5.5042-55[»]
4U1UX-ray2.95B1/D14-53[»]
4U1VX-ray3.00B1/D14-53[»]
4U20X-ray2.90B1/D14-53[»]
4U24X-ray2.90B1/D14-53[»]
4U25X-ray2.90B1/D14-53[»]
4U26X-ray2.80B1/D14-53[»]
4U27X-ray2.80B1/D14-53[»]
4UY8electron microscopy3.8014-53[»]
4V47electron microscopy12.30A12-55[»]
4V48electron microscopy11.50A12-55[»]
4V4HX-ray3.46B1/D11-55[»]
4V4QX-ray3.46B1/D12-55[»]
4V4Velectron microscopy15.00B12-53[»]
4V4Welectron microscopy15.00B12-53[»]
4V50X-ray3.22B1/D12-55[»]
4V52X-ray3.21B1/D12-55[»]
4V53X-ray3.54B1/D12-55[»]
4V54X-ray3.30B1/D12-55[»]
4V55X-ray4.00B1/D12-55[»]
4V56X-ray3.93B1/D12-55[»]
4V57X-ray3.50B1/D12-55[»]
4V5BX-ray3.74A1/C12-55[»]
4V5Helectron microscopy5.80B44-53[»]
4V5YX-ray4.45B1/D12-55[»]
4V64X-ray3.50B1/D12-55[»]
4V65electron microscopy9.00BU2-55[»]
4V66electron microscopy9.00BU2-55[»]
4V69electron microscopy6.70B14-53[»]
4V6CX-ray3.19B1/D11-55[»]
4V6DX-ray3.81B1/D11-55[»]
4V6EX-ray3.71B1/D11-55[»]
4V6Kelectron microscopy8.25Ad1-55[»]
4V6Lelectron microscopy13.20Bd1-55[»]
4V6Melectron microscopy7.10B12-55[»]
4V6Nelectron microscopy12.10A42-55[»]
4V6Oelectron microscopy14.70B42-55[»]
4V6Pelectron microscopy13.50B42-55[»]
4V6Qelectron microscopy11.50B42-55[»]
4V6Relectron microscopy11.50B42-55[»]
4V6Selectron microscopy13.10A42-55[»]
4V6Telectron microscopy8.30B14-53[»]
4V6Velectron microscopy9.80B62-55[»]
4V6Yelectron microscopy12.00B14-53[»]
4V6Zelectron microscopy12.00B14-53[»]
4V70electron microscopy17.00B14-53[»]
4V71electron microscopy20.00B14-53[»]
4V72electron microscopy13.00B14-53[»]
4V73electron microscopy15.00B14-53[»]
4V74electron microscopy17.00B14-53[»]
4V75electron microscopy12.00B14-53[»]
4V76electron microscopy17.00B14-53[»]
4V77electron microscopy17.00B14-53[»]
4V78electron microscopy20.00B14-53[»]
4V79electron microscopy15.00B14-53[»]
4V7Aelectron microscopy9.00B14-53[»]
4V7Belectron microscopy6.80B11-55[»]
4V7Celectron microscopy7.60B42-55[»]
4V7Delectron microscopy7.60A52-55[»]
4V7Ielectron microscopy9.60A11-55[»]
4V7SX-ray3.25B1/D14-53[»]
4V7TX-ray3.19B1/D14-53[»]
4V7UX-ray3.10B1/D14-53[»]
4V7VX-ray3.29B1/D14-53[»]
4V85X-ray3.2051-55[»]
4V89X-ray3.70B51-55[»]
4V9CX-ray3.30B1/D11-55[»]
4V9DX-ray3.00C1/D14-53[»]
4V9OX-ray2.90A1/C1/E1/G11-55[»]
4V9PX-ray2.90A1/C1/E1/G11-55[»]
4WF1X-ray3.09B1/D14-53[»]
4WOIX-ray3.00B1/C11-55[»]
4WWWX-ray3.10R1/Y14-53[»]
4YBBX-ray2.10C2/D24-54[»]
5ADYelectron microscopy4.5011-55[»]
5AFIelectron microscopy2.9011-55[»]
5AKAelectron microscopy5.7012-55[»]
5GADelectron microscopy3.70c1-55[»]
5GAEelectron microscopy3.33c1-55[»]
5GAFelectron microscopy4.30c4-54[»]
5GAGelectron microscopy3.80c1-55[»]
5GAHelectron microscopy3.80c1-55[»]
5IQRelectron microscopy3.00c1-55[»]
DisProtiDP00143.
ProteinModelPortaliP0A7N9.
SMRiP0A7N9. Positions 4-53.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7N9.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L33P family.Curated

Phylogenomic databases

eggNOGiCOG0267. LUCA.
HOGENOMiHOG000004839.
InParanoidiP0A7N9.
KOiK02913.
OMAiARKHVLY.
PhylomeDBiP0A7N9.

Family and domain databases

HAMAPiMF_00294. Ribosomal_L33. 1 hit.
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.
WP_001051798.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76660; AAC76660; b3636.
BAE77656; BAE77656; BAE77656.
GeneIDi8913847.
946318.
KEGGiecj:JW3611.
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.
WP_001051798.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J28electron microscopy8.0012-55[»]
2RDOelectron microscopy9.1012-55[»]
3BBXelectron microscopy10.0012-55[»]
3J5Lelectron microscopy6.6014-53[»]
3J5Selectron microscopy7.50H4-53[»]
3J7Zelectron microscopy3.9011-55[»]
3J9Yelectron microscopy3.9011-55[»]
3J9Zelectron microscopy3.60L22-55[»]
3JA1electron microscopy3.60L42-55[»]
3JBUelectron microscopy3.6441-55[»]
3JBVelectron microscopy3.3241-55[»]
3JCDelectron microscopy3.7011-55[»]
3JCEelectron microscopy3.2011-55[»]
3JCJelectron microscopy3.70a1-55[»]
3JCNelectron microscopy4.6011-55[»]
4CSUelectron microscopy5.5042-55[»]
4U1UX-ray2.95B1/D14-53[»]
4U1VX-ray3.00B1/D14-53[»]
4U20X-ray2.90B1/D14-53[»]
4U24X-ray2.90B1/D14-53[»]
4U25X-ray2.90B1/D14-53[»]
4U26X-ray2.80B1/D14-53[»]
4U27X-ray2.80B1/D14-53[»]
4UY8electron microscopy3.8014-53[»]
4V47electron microscopy12.30A12-55[»]
4V48electron microscopy11.50A12-55[»]
4V4HX-ray3.46B1/D11-55[»]
4V4QX-ray3.46B1/D12-55[»]
4V4Velectron microscopy15.00B12-53[»]
4V4Welectron microscopy15.00B12-53[»]
4V50X-ray3.22B1/D12-55[»]
4V52X-ray3.21B1/D12-55[»]
4V53X-ray3.54B1/D12-55[»]
4V54X-ray3.30B1/D12-55[»]
4V55X-ray4.00B1/D12-55[»]
4V56X-ray3.93B1/D12-55[»]
4V57X-ray3.50B1/D12-55[»]
4V5BX-ray3.74A1/C12-55[»]
4V5Helectron microscopy5.80B44-53[»]
4V5YX-ray4.45B1/D12-55[»]
4V64X-ray3.50B1/D12-55[»]
4V65electron microscopy9.00BU2-55[»]
4V66electron microscopy9.00BU2-55[»]
4V69electron microscopy6.70B14-53[»]
4V6CX-ray3.19B1/D11-55[»]
4V6DX-ray3.81B1/D11-55[»]
4V6EX-ray3.71B1/D11-55[»]
4V6Kelectron microscopy8.25Ad1-55[»]
4V6Lelectron microscopy13.20Bd1-55[»]
4V6Melectron microscopy7.10B12-55[»]
4V6Nelectron microscopy12.10A42-55[»]
4V6Oelectron microscopy14.70B42-55[»]
4V6Pelectron microscopy13.50B42-55[»]
4V6Qelectron microscopy11.50B42-55[»]
4V6Relectron microscopy11.50B42-55[»]
4V6Selectron microscopy13.10A42-55[»]
4V6Telectron microscopy8.30B14-53[»]
4V6Velectron microscopy9.80B62-55[»]
4V6Yelectron microscopy12.00B14-53[»]
4V6Zelectron microscopy12.00B14-53[»]
4V70electron microscopy17.00B14-53[»]
4V71electron microscopy20.00B14-53[»]
4V72electron microscopy13.00B14-53[»]
4V73electron microscopy15.00B14-53[»]
4V74electron microscopy17.00B14-53[»]
4V75electron microscopy12.00B14-53[»]
4V76electron microscopy17.00B14-53[»]
4V77electron microscopy17.00B14-53[»]
4V78electron microscopy20.00B14-53[»]
4V79electron microscopy15.00B14-53[»]
4V7Aelectron microscopy9.00B14-53[»]
4V7Belectron microscopy6.80B11-55[»]
4V7Celectron microscopy7.60B42-55[»]
4V7Delectron microscopy7.60A52-55[»]
4V7Ielectron microscopy9.60A11-55[»]
4V7SX-ray3.25B1/D14-53[»]
4V7TX-ray3.19B1/D14-53[»]
4V7UX-ray3.10B1/D14-53[»]
4V7VX-ray3.29B1/D14-53[»]
4V85X-ray3.2051-55[»]
4V89X-ray3.70B51-55[»]
4V9CX-ray3.30B1/D11-55[»]
4V9DX-ray3.00C1/D14-53[»]
4V9OX-ray2.90A1/C1/E1/G11-55[»]
4V9PX-ray2.90A1/C1/E1/G11-55[»]
4WF1X-ray3.09B1/D14-53[»]
4WOIX-ray3.00B1/C11-55[»]
4WWWX-ray3.10R1/Y14-53[»]
4YBBX-ray2.10C2/D24-54[»]
5ADYelectron microscopy4.5011-55[»]
5AFIelectron microscopy2.9011-55[»]
5AKAelectron microscopy5.7012-55[»]
5GADelectron microscopy3.70c1-55[»]
5GAEelectron microscopy3.33c1-55[»]
5GAFelectron microscopy4.30c4-54[»]
5GAGelectron microscopy3.80c1-55[»]
5GAHelectron microscopy3.80c1-55[»]
5IQRelectron microscopy3.00c1-55[»]
DisProtiDP00143.
ProteinModelPortaliP0A7N9.
SMRiP0A7N9. Positions 4-53.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260822. 234 interactions.
DIPiDIP-35968N.
IntActiP0A7N9. 53 interactions.
MINTiMINT-1234559.
STRINGi511145.b3636.

Chemistry

ChEMBLiCHEMBL2363135.

Proteomic databases

EPDiP0A7N9.
PaxDbiP0A7N9.
PRIDEiP0A7N9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76660; AAC76660; b3636.
BAE77656; BAE77656; BAE77656.
GeneIDi8913847.
946318.
KEGGiecj:JW3611.
eco:b3636.
PATRICi32122759. VBIEscCol129921_3756.

Organism-specific databases

EchoBASEiEB0884.
EcoGeneiEG10891. rpmG.

Phylogenomic databases

eggNOGiCOG0267. LUCA.
HOGENOMiHOG000004839.
InParanoidiP0A7N9.
KOiK02913.
OMAiARKHVLY.
PhylomeDBiP0A7N9.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0A7N9.
PROiP0A7N9.

Family and domain databases

HAMAPiMF_00294. Ribosomal_L33. 1 hit.
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...

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 7, 2016
This is version 118 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

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 one 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.