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UniProtKB - P61175 (RL22_ECOLI)

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Protein

50S ribosomal protein L22

Gene

rplV

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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

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.

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

  • response to antibiotic Source: UniProtKB-KW
  • ribosome assembly Source: CAFA
  • translation Source: InterPro
View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding
Biological processAntibiotic resistance

Enzyme and pathway databases

BioCyciEcoCyc:EG10882-MONOMER
MetaCyc:EG10882-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L22
Alternative name(s):
Large ribosomal subunit protein uL221 Publication
Gene namesi
Name:rplV
Synonyms:eryB
Ordered Locus Names:b3315, JW3277
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
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
  • large ribosomal subunit Source: CAFA
  • polysomal ribosome Source: CAFA
View the complete GO annotation on QuickGO ...

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.10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ubiGP179933EBI-542255,EBI-559367

Protein-protein interaction databases

DIPiDIP-35983N
IntActiP61175, 132 interactors
STRINGi316385.ECDH10B_3490

Structurei

Secondary structure

1110
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 12Combined sources11
Helixi14 – 21Combined sources8
Helixi29 – 38Combined sources10
Helixi42 – 61Combined sources20
Helixi66 – 68Combined sources3
Beta strandi70 – 78Combined sources9
Beta strandi82 – 87Combined sources6
Helixi89 – 91Combined sources3
Beta strandi93 – 98Combined sources6
Beta strandi100 – 108Combined sources9

3D structure databases

ProteinModelPortaliP61175
SMRiP61175
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61175

Family & Domainsi

Sequence similaritiesi

Belongs to the universal ribosomal protein uL22 family.Curated

Phylogenomic databases

eggNOGiCOG0091 LUCA
HOGENOMiHOG000205046
InParanoidiP61175
KOiK02890
OMAiPQGRAHR
PhylomeDBiP61175

Family and domain databases

CDDicd00336 Ribosomal_L22, 1 hit
Gene3Di3.90.470.10, 1 hit
HAMAPiMF_01331_B Ribosomal_L22_B, 1 hit
InterProiView protein in InterPro
IPR001063 Ribosomal_L22
IPR018260 Ribosomal_L22/L17_CS
IPR036394 Ribosomal_L22/L17_sf
IPR005727 Ribosomal_L22_bac/chlpt-type
PANTHERiPTHR13501 PTHR13501, 1 hit
PfamiView protein in Pfam
PF00237 Ribosomal_L22, 1 hit
SUPFAMiSSF54843 SSF54843, 1 hit
TIGRFAMsiTIGR01044 rplV_bact, 1 hit
PROSITEiView protein in PROSITE
PS00464 RIBOSOMAL_L22, 1 hit

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
GeneIDi29456686
947813
KEGGiecj:JW3277
eco:b3315
PATRICifig|1411691.4.peg.3416

Similar proteinsi

Entry informationi

Entry nameiRL22_ECOLI
AccessioniPrimary (citable) accession number: P61175
Secondary accession number(s): P02423, Q2M6Y0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 20, 2018
This is version 150 of the entry and version 1 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

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