Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

50S ribosomal protein L22

Gene

rplV

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

Functioni

This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.1 Publication
The globular domain of the protein is one of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that penetrates into the center of the 70S ribosome where it lines the wall of the exit tunnel. Removal of most of this hairpin (residues 85-95) does not prevent its incorporation into 70S ribosomes. Two of the hairpin residues (91 and 93) seem to be involved in translation elongation arrest of the SecM protein, as their replacement by larger amino acids alleviates the arrest.2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Biological processi

Antibiotic resistance

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10882-MONOMER.
ECOL316407:JW3277-MONOMER.
MetaCyc:EG10882-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L22
Gene namesi
Name:rplV
Synonyms:eryB
Ordered Locus Names:b3315, JW3277
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10882. rplV.

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi82 – 99Missing : Incorporated into ribosomes in vivo, but is easily removed by a salt wash. 1 PublicationAdd BLAST18
Mutagenesisi85 – 95Missing : Incorporates into ribosomes in vivo. 1 PublicationAdd BLAST11
Mutagenesisi91G → A, D or S: Abolishes translation elongation arrest of SecM. 1 Publication1
Mutagenesisi93A → S, T or V: Abolishes translation elongation arrest of SecM. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001251531 – 11050S ribosomal protein L22Add BLAST110

Proteomic databases

EPDiP61175.
PaxDbiP61175.
PRIDEiP61175.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit.

Binary interactionsi

WithEntry#Exp.IntActNotes
ubiGP179932EBI-542255,EBI-559367

Protein-protein interaction databases

DIPiDIP-35983N.
IntActiP61175. 128 interactors.
MINTiMINT-1253134.
STRINGi511145.b3315.

Structurei

Secondary structure

1110
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 12Combined sources10
Helixi14 – 24Combined sources11
Beta strandi25 – 27Combined sources3
Helixi29 – 37Combined sources9
Helixi42 – 60Combined sources19
Beta strandi62 – 64Combined sources3
Helixi66 – 68Combined sources3
Beta strandi70 – 78Combined sources9
Beta strandi82 – 87Combined sources6
Helixi89 – 91Combined sources3
Beta strandi93 – 98Combined sources6
Beta strandi101 – 108Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2J28electron microscopy8.00S1-110[»]
2RDOelectron microscopy9.10S1-110[»]
3BBXelectron microscopy10.00S1-110[»]
3J5Lelectron microscopy6.60S1-110[»]
3J7Zelectron microscopy3.90S1-110[»]
3J8Gelectron microscopy5.00S1-110[»]
3J9Yelectron microscopy3.90S1-110[»]
3J9Zelectron microscopy3.60LQ1-110[»]
3JA1electron microscopy3.60LU1-110[»]
3JBUelectron microscopy3.64s1-110[»]
3JBVelectron microscopy3.32s1-110[»]
3JCDelectron microscopy3.70S1-110[»]
3JCEelectron microscopy3.20S1-110[»]
3JCJelectron microscopy3.70R1-110[»]
3JCNelectron microscopy4.60S1-110[»]
4CSUelectron microscopy5.50S1-110[»]
4U1UX-ray2.95BS/DS1-110[»]
4U1VX-ray3.00BS/DS1-110[»]
4U20X-ray2.90BS/DS1-110[»]
4U24X-ray2.90BS/DS1-110[»]
4U25X-ray2.90BS/DS1-110[»]
4U26X-ray2.80BS/DS1-110[»]
4U27X-ray2.80BS/DS1-110[»]
4UY8electron microscopy3.80S1-110[»]
4V47electron microscopy12.30AQ1-110[»]
4V48electron microscopy11.50AQ1-110[»]
4V4HX-ray3.46BS/DS1-110[»]
4V4QX-ray3.46BS/DS1-110[»]
4V4Velectron microscopy15.00BQ5-110[»]
4V4Welectron microscopy15.00BQ5-110[»]
4V50X-ray3.22BS/DS1-110[»]
4V52X-ray3.21BS/DS1-110[»]
4V53X-ray3.54BS/DS1-110[»]
4V54X-ray3.30BS/DS1-110[»]
4V55X-ray4.00BS/DS1-110[»]
4V56X-ray3.93BS/DS1-110[»]
4V57X-ray3.50BS/DS1-110[»]
4V5BX-ray3.74AS/CS1-110[»]
4V5Helectron microscopy5.80BS1-110[»]
4V5YX-ray4.45BS/DS1-110[»]
4V64X-ray3.50BS/DS1-110[»]
4V65electron microscopy9.00BL1-110[»]
4V66electron microscopy9.00BL1-110[»]
4V69electron microscopy6.70BS1-110[»]
4V6CX-ray3.19BS/DS1-110[»]
4V6DX-ray3.81BS/DS1-110[»]
4V6EX-ray3.71BS/DS1-110[»]
4V6Kelectron microscopy8.25AT1-110[»]
4V6Lelectron microscopy13.20BT1-110[»]
4V6Melectron microscopy7.10BS1-110[»]
4V6Nelectron microscopy12.10AU1-110[»]
4V6Oelectron microscopy14.70BU1-110[»]
4V6Pelectron microscopy13.50BU1-110[»]
4V6Qelectron microscopy11.50BU1-110[»]
4V6Relectron microscopy11.50BU1-110[»]
4V6Selectron microscopy13.10AU1-110[»]
4V6Telectron microscopy8.30BS1-110[»]
4V6Velectron microscopy9.80BW1-110[»]
4V6Yelectron microscopy12.00BS1-110[»]
4V6Zelectron microscopy12.00BS1-110[»]
4V70electron microscopy17.00BS1-110[»]
4V71electron microscopy20.00BS1-110[»]
4V72electron microscopy13.00BS1-110[»]
4V73electron microscopy15.00BS1-110[»]
4V74electron microscopy17.00BS1-110[»]
4V75electron microscopy12.00BS1-110[»]
4V76electron microscopy17.00BS1-110[»]
4V77electron microscopy17.00BS1-110[»]
4V78electron microscopy20.00BS1-110[»]
4V79electron microscopy15.00BS1-110[»]
4V7Aelectron microscopy9.00BS1-110[»]
4V7Belectron microscopy6.80BS1-110[»]
4V7Celectron microscopy7.60BU1-110[»]
4V7Delectron microscopy7.60AV1-110[»]
4V7Ielectron microscopy9.60AS1-110[»]
4V7SX-ray3.25BS/DS1-110[»]
4V7TX-ray3.19BS/DS1-110[»]
4V7UX-ray3.10BS/DS1-110[»]
4V7VX-ray3.29BS/DS1-110[»]
4V85X-ray3.20W1-110[»]
4V89X-ray3.70BW1-110[»]
4V9CX-ray3.30BS/DS1-110[»]
4V9DX-ray3.00CS/DS1-110[»]
4V9OX-ray2.90AS/CS/ES/GS1-110[»]
4V9PX-ray2.90AS/CS/ES/GS1-110[»]
4WF1X-ray3.09BS/DS1-110[»]
4WOIX-ray3.00BS/CS1-110[»]
4WWWX-ray3.10RS/YS1-110[»]
4YBBX-ray2.10CT/DT1-110[»]
5ADYelectron microscopy4.50S1-110[»]
5AFIelectron microscopy2.90S1-110[»]
5AKAelectron microscopy5.70S1-110[»]
5GADelectron microscopy3.70T1-110[»]
5GAEelectron microscopy3.33T1-110[»]
5GAFelectron microscopy4.30T1-110[»]
5GAGelectron microscopy3.80T1-110[»]
5GAHelectron microscopy3.80T1-110[»]
5IQRelectron microscopy3.00S1-110[»]
5IT8X-ray3.12CT/DT1-110[»]
5J5BX-ray2.80CT/DT1-110[»]
5J7LX-ray3.00CT/DT1-110[»]
5J88X-ray3.32CT/DT1-110[»]
5J8AX-ray3.10CT/DT1-110[»]
5J91X-ray2.96CT/DT1-110[»]
5JC9X-ray3.03CT/DT1-110[»]
5JTEelectron microscopy3.60BS1-110[»]
5JU8electron microscopy3.60BS1-110[»]
5KCRelectron microscopy3.601W1-110[»]
5KCSelectron microscopy3.901W1-110[»]
5KPSelectron microscopy3.90S1-110[»]
5KPVelectron microscopy4.10R1-110[»]
5KPWelectron microscopy3.90R1-110[»]
5KPXelectron microscopy3.90R1-110[»]
5L3Pelectron microscopy3.70W1-110[»]
ProteinModelPortaliP61175.
SMRiP61175.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61175.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L22P family.Curated

Phylogenomic databases

eggNOGiCOG0091. LUCA.
HOGENOMiHOG000205046.
InParanoidiP61175.
KOiK02890.
OMAiVAILEHM.
PhylomeDBiP61175.

Family and domain databases

CDDicd00336. Ribosomal_L22. 1 hit.
Gene3Di3.90.470.10. 1 hit.
HAMAPiMF_01331_B. Ribosomal_L22_B. 1 hit.
InterProiIPR001063. Ribosomal_L22.
IPR018260. Ribosomal_L22/L17_CS.
IPR005727. Ribosomal_L22_bac/chlpt-type.
[Graphical view]
PANTHERiPTHR13501. PTHR13501. 1 hit.
PfamiPF00237. Ribosomal_L22. 1 hit.
[Graphical view]
SUPFAMiSSF54843. SSF54843. 1 hit.
TIGRFAMsiTIGR01044. rplV_bact. 1 hit.
PROSITEiPS00464. RIBOSOMAL_L22. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P61175-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METIAKHRHA RSSAQKVRLV ADLIRGKKVS QALDILTYTN KKAAVLVKKV
60 70 80 90 100
LESAIANAEH NDGADIDDLK VTKIFVDEGP SMKRIMPRAK GRADRILKRT
110
SHITVVVSDR
Length:110
Mass (Da):12,226
Last modified:July 21, 1986 - v1
Checksum:iF0E0C6982772277C
GO

Mass spectrometryi

Molecular mass is 12225.3 Da from positions 1 - 110. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti8R → C in strain: SK1048; decreases translational rate, tRNA binding and subunit association at 44 degrees Celsius; does not alter 23S rRNA or L4 interactions; not erythromycin resistant. 1 Publication1
Natural varianti82 – 84Missing in strain: N281; confers erythromycin resistance; ribosomes bind erythromycin normally and have normal peptidyltransferase activity; 50S subunits assemble normally, even in the presence of drug; the protein is incorporated into ribosomes in vivo; abolishes translation elongation arrest of SecM. 2 Publications3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02613 Genomic DNA. Translation: CAA26465.1.
U18997 Genomic DNA. Translation: AAA58112.1.
U00096 Genomic DNA. Translation: AAC76340.1.
AP009048 Genomic DNA. Translation: BAE77976.1.
PIRiG23129. R5EC22.
RefSeqiNP_417774.1. NC_000913.3.
WP_000447529.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76340; AAC76340; b3315.
BAE77976; BAE77976; BAE77976.
GeneIDi5548826.
947813.
KEGGiecj:JW3277.
eco:b3315.
PATRICi32122062. VBIEscCol129921_3408.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02613 Genomic DNA. Translation: CAA26465.1.
U18997 Genomic DNA. Translation: AAA58112.1.
U00096 Genomic DNA. Translation: AAC76340.1.
AP009048 Genomic DNA. Translation: BAE77976.1.
PIRiG23129. R5EC22.
RefSeqiNP_417774.1. NC_000913.3.
WP_000447529.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2J28electron microscopy8.00S1-110[»]
2RDOelectron microscopy9.10S1-110[»]
3BBXelectron microscopy10.00S1-110[»]
3J5Lelectron microscopy6.60S1-110[»]
3J7Zelectron microscopy3.90S1-110[»]
3J8Gelectron microscopy5.00S1-110[»]
3J9Yelectron microscopy3.90S1-110[»]
3J9Zelectron microscopy3.60LQ1-110[»]
3JA1electron microscopy3.60LU1-110[»]
3JBUelectron microscopy3.64s1-110[»]
3JBVelectron microscopy3.32s1-110[»]
3JCDelectron microscopy3.70S1-110[»]
3JCEelectron microscopy3.20S1-110[»]
3JCJelectron microscopy3.70R1-110[»]
3JCNelectron microscopy4.60S1-110[»]
4CSUelectron microscopy5.50S1-110[»]
4U1UX-ray2.95BS/DS1-110[»]
4U1VX-ray3.00BS/DS1-110[»]
4U20X-ray2.90BS/DS1-110[»]
4U24X-ray2.90BS/DS1-110[»]
4U25X-ray2.90BS/DS1-110[»]
4U26X-ray2.80BS/DS1-110[»]
4U27X-ray2.80BS/DS1-110[»]
4UY8electron microscopy3.80S1-110[»]
4V47electron microscopy12.30AQ1-110[»]
4V48electron microscopy11.50AQ1-110[»]
4V4HX-ray3.46BS/DS1-110[»]
4V4QX-ray3.46BS/DS1-110[»]
4V4Velectron microscopy15.00BQ5-110[»]
4V4Welectron microscopy15.00BQ5-110[»]
4V50X-ray3.22BS/DS1-110[»]
4V52X-ray3.21BS/DS1-110[»]
4V53X-ray3.54BS/DS1-110[»]
4V54X-ray3.30BS/DS1-110[»]
4V55X-ray4.00BS/DS1-110[»]
4V56X-ray3.93BS/DS1-110[»]
4V57X-ray3.50BS/DS1-110[»]
4V5BX-ray3.74AS/CS1-110[»]
4V5Helectron microscopy5.80BS1-110[»]
4V5YX-ray4.45BS/DS1-110[»]
4V64X-ray3.50BS/DS1-110[»]
4V65electron microscopy9.00BL1-110[»]
4V66electron microscopy9.00BL1-110[»]
4V69electron microscopy6.70BS1-110[»]
4V6CX-ray3.19BS/DS1-110[»]
4V6DX-ray3.81BS/DS1-110[»]
4V6EX-ray3.71BS/DS1-110[»]
4V6Kelectron microscopy8.25AT1-110[»]
4V6Lelectron microscopy13.20BT1-110[»]
4V6Melectron microscopy7.10BS1-110[»]
4V6Nelectron microscopy12.10AU1-110[»]
4V6Oelectron microscopy14.70BU1-110[»]
4V6Pelectron microscopy13.50BU1-110[»]
4V6Qelectron microscopy11.50BU1-110[»]
4V6Relectron microscopy11.50BU1-110[»]
4V6Selectron microscopy13.10AU1-110[»]
4V6Telectron microscopy8.30BS1-110[»]
4V6Velectron microscopy9.80BW1-110[»]
4V6Yelectron microscopy12.00BS1-110[»]
4V6Zelectron microscopy12.00BS1-110[»]
4V70electron microscopy17.00BS1-110[»]
4V71electron microscopy20.00BS1-110[»]
4V72electron microscopy13.00BS1-110[»]
4V73electron microscopy15.00BS1-110[»]
4V74electron microscopy17.00BS1-110[»]
4V75electron microscopy12.00BS1-110[»]
4V76electron microscopy17.00BS1-110[»]
4V77electron microscopy17.00BS1-110[»]
4V78electron microscopy20.00BS1-110[»]
4V79electron microscopy15.00BS1-110[»]
4V7Aelectron microscopy9.00BS1-110[»]
4V7Belectron microscopy6.80BS1-110[»]
4V7Celectron microscopy7.60BU1-110[»]
4V7Delectron microscopy7.60AV1-110[»]
4V7Ielectron microscopy9.60AS1-110[»]
4V7SX-ray3.25BS/DS1-110[»]
4V7TX-ray3.19BS/DS1-110[»]
4V7UX-ray3.10BS/DS1-110[»]
4V7VX-ray3.29BS/DS1-110[»]
4V85X-ray3.20W1-110[»]
4V89X-ray3.70BW1-110[»]
4V9CX-ray3.30BS/DS1-110[»]
4V9DX-ray3.00CS/DS1-110[»]
4V9OX-ray2.90AS/CS/ES/GS1-110[»]
4V9PX-ray2.90AS/CS/ES/GS1-110[»]
4WF1X-ray3.09BS/DS1-110[»]
4WOIX-ray3.00BS/CS1-110[»]
4WWWX-ray3.10RS/YS1-110[»]
4YBBX-ray2.10CT/DT1-110[»]
5ADYelectron microscopy4.50S1-110[»]
5AFIelectron microscopy2.90S1-110[»]
5AKAelectron microscopy5.70S1-110[»]
5GADelectron microscopy3.70T1-110[»]
5GAEelectron microscopy3.33T1-110[»]
5GAFelectron microscopy4.30T1-110[»]
5GAGelectron microscopy3.80T1-110[»]
5GAHelectron microscopy3.80T1-110[»]
5IQRelectron microscopy3.00S1-110[»]
5IT8X-ray3.12CT/DT1-110[»]
5J5BX-ray2.80CT/DT1-110[»]
5J7LX-ray3.00CT/DT1-110[»]
5J88X-ray3.32CT/DT1-110[»]
5J8AX-ray3.10CT/DT1-110[»]
5J91X-ray2.96CT/DT1-110[»]
5JC9X-ray3.03CT/DT1-110[»]
5JTEelectron microscopy3.60BS1-110[»]
5JU8electron microscopy3.60BS1-110[»]
5KCRelectron microscopy3.601W1-110[»]
5KCSelectron microscopy3.901W1-110[»]
5KPSelectron microscopy3.90S1-110[»]
5KPVelectron microscopy4.10R1-110[»]
5KPWelectron microscopy3.90R1-110[»]
5KPXelectron microscopy3.90R1-110[»]
5L3Pelectron microscopy3.70W1-110[»]
ProteinModelPortaliP61175.
SMRiP61175.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-35983N.
IntActiP61175. 128 interactors.
MINTiMINT-1253134.
STRINGi511145.b3315.

Proteomic databases

EPDiP61175.
PaxDbiP61175.
PRIDEiP61175.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76340; AAC76340; b3315.
BAE77976; BAE77976; BAE77976.
GeneIDi5548826.
947813.
KEGGiecj:JW3277.
eco:b3315.
PATRICi32122062. VBIEscCol129921_3408.

Organism-specific databases

EchoBASEiEB0875.
EcoGeneiEG10882. rplV.

Phylogenomic databases

eggNOGiCOG0091. LUCA.
HOGENOMiHOG000205046.
InParanoidiP61175.
KOiK02890.
OMAiVAILEHM.
PhylomeDBiP61175.

Enzyme and pathway databases

BioCyciEcoCyc:EG10882-MONOMER.
ECOL316407:JW3277-MONOMER.
MetaCyc:EG10882-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP61175.
PROiP61175.

Family and domain databases

CDDicd00336. Ribosomal_L22. 1 hit.
Gene3Di3.90.470.10. 1 hit.
HAMAPiMF_01331_B. Ribosomal_L22_B. 1 hit.
InterProiIPR001063. Ribosomal_L22.
IPR018260. Ribosomal_L22/L17_CS.
IPR005727. Ribosomal_L22_bac/chlpt-type.
[Graphical view]
PANTHERiPTHR13501. PTHR13501. 1 hit.
PfamiPF00237. Ribosomal_L22. 1 hit.
[Graphical view]
SUPFAMiSSF54843. SSF54843. 1 hit.
TIGRFAMsiTIGR01044. rplV_bact. 1 hit.
PROSITEiPS00464. RIBOSOMAL_L22. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRL22_ECOLI
AccessioniPrimary (citable) accession number: P61175
Secondary accession number(s): P02423, Q2M6Y0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 30, 2016
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The wild-type allele (erythromycin sensitive) is dominant over the resistant allele, and is also dominant over the temperature-sensitive allele at both low and high temperatures.

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.