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Protein

50S ribosomal protein L33

Gene

rpmG

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

Functioni

Miscellaneous

Surface exposed on the 50S subunit.

GO - Molecular functioni

  • structural constituent of ribosome Source: CAFA
  • tRNA binding Source: UniProtKB-KW

GO - Biological processi

  • response to antibiotic Source: EcoCyc
  • ribosomal large subunit assembly Source: CAFA
  • translation Source: InterPro

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein, RNA-binding, tRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10891-MONOMER.
MetaCyc:EG10891-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L33
Alternative name(s):
Large ribosomal subunit protein bL331 Publication
Gene namesi
Name:rpmG
Ordered Locus Names:b3636, JW3611
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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: CAFA

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001701582 – 5550S ribosomal protein L33Add BLAST54

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-methylalanine1 Publication1

Keywords - PTMi

Methylation

Proteomic databases

PaxDbiP0A7N9.
PRIDEiP0A7N9.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit (PubMed:786732, PubMed:10094780, PubMed:12809609, PubMed:16272117, PubMed:25310980, PubMed:24844575, PubMed:27934701, PubMed:27906160, PubMed:27906161). Cross-links to the P and E site tRNAs (PubMed:8524654).10 Publications

Protein-protein interaction databases

BioGridi4260822. 250 interactors.
DIPiDIP-35968N.
IntActiP0A7N9. 53 interactors.
MINTiMINT-1234559.
STRINGi316385.ECDH10B_3818.

Structurei

Secondary structure

155
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 17Combined sources11
Beta strandi20 – 25Combined sources6
Turni27 – 29Combined sources3
Beta strandi35 – 40Combined sources6
Turni41 – 44Combined sources4
Beta strandi45 – 53Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5H5Uelectron microscopy3.00c2-55[»]
5IQRelectron microscopy3.00c1-55[»]
5IT8X-ray3.12C2/D24-54[»]
5J5BX-ray2.80C2/D24-54[»]
5J7LX-ray3.00C2/D24-54[»]
5J88X-ray3.32C2/D24-54[»]
5J8AX-ray3.10C2/D24-54[»]
5J91X-ray2.96C2/D24-54[»]
5JC9X-ray3.03C2/D24-54[»]
5JTEelectron microscopy3.60B11-55[»]
5JU8electron microscopy3.60B11-55[»]
5KCRelectron microscopy3.60161-55[»]
5KCSelectron microscopy3.90161-55[»]
5KPSelectron microscopy3.9031-55[»]
5KPVelectron microscopy4.1021-55[»]
5KPWelectron microscopy3.9021-55[»]
5KPXelectron microscopy3.9021-55[»]
5L3Pelectron microscopy3.7061-55[»]
5LZAelectron microscopy3.6014-53[»]
5LZBelectron microscopy5.3014-53[»]
5LZCelectron microscopy4.8014-53[»]
5LZDelectron microscopy3.4014-53[»]
5LZEelectron microscopy3.5014-53[»]
5LZFelectron microscopy4.6014-53[»]
5MDVelectron microscopy2.97c1-55[»]
5MDWelectron microscopy3.06c1-55[»]
5MDYelectron microscopy3.35c1-55[»]
5MDZelectron microscopy3.10c1-55[»]
5MGPelectron microscopy3.1014-53[»]
5NCOelectron microscopy4.80c4-54[»]
5NP6electron microscopy3.60z4-53[»]
5U4Ielectron microscopy3.5021-55[»]
5U9Felectron microscopy3.20311-55[»]
5U9Gelectron microscopy3.20311-55[»]
5UYKelectron microscopy3.90314-53[»]
5UYLelectron microscopy3.60314-53[»]
5UYMelectron microscopy3.20314-53[»]
5UYNelectron microscopy4.00314-53[»]
5UYPelectron microscopy3.90314-53[»]
5UYQelectron microscopy3.80314-53[»]
ProteinModelPortaliP0A7N9.
SMRiP0A7N9.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7N9.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

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

Family and domain databases

HAMAPiMF_00294. Ribosomal_L33. 1 hit.
InterProiView protein in InterPro
IPR001705. Ribosomal_L33.
IPR018264. Ribosomal_L33_CS.
IPR011332. Ribosomal_zn-bd.
PfamiView protein in Pfam
PF00471. Ribosomal_L33. 1 hit.
SUPFAMiSSF57829. SSF57829. 1 hit.
TIGRFAMsiTIGR01023. rpmG_bact. 1 hit.
PROSITEiView protein in PROSITE
PS00582. RIBOSOMAL_L33. 1 hit.

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)DescriptionActionsGraphical viewLength
Sequence conflicti48 – 49IY → YI AA sequence (PubMed:786732).Curated2

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.
PATRICifig|1411691.4.peg.3070.

Similar proteinsi

Entry informationi

Entry nameiRL33_ECOLI
AccessioniPrimary (citable) accession number: P0A7N9
Secondary accession number(s): P02436, Q2M7V0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: August 30, 2017
This is version 129 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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