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P61175 (RL22_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
50S ribosomal protein L22
Gene names
Name:rplV
Synonyms:eryB
Ordered Locus Names:b3315, JW3277
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length110 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. HAMAP-Rule MF_01331_B

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. HAMAP-Rule MF_01331_B

Subunit structure

Part of the 50S ribosomal subunit.

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.

Sequence similarities

Belongs to the ribosomal protein L22P family.

Mass spectrometry

Molecular mass is 12225.3 Da from positions 1 - 110. Determined by MALDI. Ref.11

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ubiGP179932EBI-542255,EBI-559367

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11011050S ribosomal protein L22 HAMAP-Rule MF_01331_B
PRO_0000125153

Natural variations

Natural variant81R → 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.
Natural variant82 – 843Missing 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.

Experimental info

Mutagenesis82 – 9918Missing: Incorporated into ribosomes in vivo, but is easily removed by a salt wash.
Mutagenesis85 – 9511Missing: Incorporates into ribosomes in vivo.
Mutagenesis911G → A, D or S: Abolishes translation elongation arrest of SecM. Ref.9
Mutagenesis931A → S, T or V: Abolishes translation elongation arrest of SecM. Ref.9

Secondary structure

...................... 110
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P61175 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: F0E0C6982772277C

FASTA11012,226
        10         20         30         40         50         60 
METIAKHRHA RSSAQKVRLV ADLIRGKKVS QALDILTYTN KKAAVLVKKV LESAIANAEH 

        70         80         90        100        110 
NDGADIDDLK VTKIFVDEGP SMKRIMPRAK GRADRILKRT SHITVVVSDR 

« Hide

References

« Hide 'large scale' references
[1]"Amino acid sequence of protein L22 from the large subunit of the Escherichia coli ribosome."
Wittmann-Liebold B., Greuer B.
FEBS Lett. 121:105-112(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
[2]"Structure of the Escherichia coli S10 ribosomal protein operon."
Zurawski G., Zurawski S.M.
Nucleic Acids Res. 13:4521-4526(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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]"Biochemical and genetic studies on two different types of erythromycin resistant mutants of Escherichia coli with altered ribosomal proteins."
Wittmann H.G., Stoffler G., Apirion D., Rosen L., Tanaka K., Tamaki M., Takata R., Dekio S., Otaka E.
Mol. Gen. Genet. 127:175-189(1973) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOCHEMICAL CHARACTERIZATION OF ERYTHROMYCIN-RESISTANT VARIANT N281.
Strain: N281.
[6]"A temperature-sensitive mutant of Escherichia coli with an alteration in ribosomal protein L22."
Burnette-Vick B., Champney W.S., Musich P.R.
Genetica 94:17-25(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: TEMPERATURE-SENSITIVE VARIANT.
Strain: SK1048.
[7]"Ribosomal protein gene sequence changes in erythromycin-resistant mutants of Escherichia coli."
Chittum H.S., Champney W.S.
J. Bacteriol. 176:6192-6198(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF CHANGES IN ERYTHROMYCIN-RESISTANT VARIANT N281.
Strain: N281.
[8]"Erythromycin inhibits the assembly of the large ribosomal subunit in growing Escherichia coli cells."
Chittum H.S., Champney W.S.
Curr. Microbiol. 30:273-279(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: ERYTHROMYCIN AND RIBOSOME ASSEMBLY.
Strain: N281 and SK901.
[9]"The ribosomal exit tunnel functions as a discriminating gate."
Nakatogawa H., Ito K.
Cell 108:629-636(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLY-91 AND ALA-93.
[10]"The extended loops of ribosomal proteins L4 and L22 are not required for ribosome assembly or L4-mediated autogenous control."
Zengel J.M., Jerauld A., Walker A., Wahl M.C., Lindahl L.
RNA 9:1188-1197(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS TO EXAMINE REQUIREMENTS FOR RIBOSOME ASSEMBLY.
Strain: K12 / LL308.
[11]"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.
[12]"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.
[13]"The polypeptide tunnel system in the ribosome and its gating in erythromycin resistance mutants of L4 and L22."
Gabashvili I.S., Gregory S.T., Valle M., Grassucci R., Worbs M., Wahl M.C., Dahlberg A.E., Frank J.
Mol. Cell 8:181-188(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (17.1 ANGSTROMS), EFFECT OF THE ERYTHROMYCIN-RESISTANT VARIANT ON THE POLYPEPTIDE EXIT TUNNEL.
Strain: N281.
[14]"Structures of the bacterial ribosome at 3.5 A resolution."
Schuwirth B.S., Borovinskaya M.A., Hau C.W., Zhang W., Vila-Sanjurjo A., Holton J.M., Cate J.H.D.
Science 310:827-834(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
Strain: MRE-600.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X02613 Genomic DNA. Translation: CAA26465.1.
U18997 Genomic DNA. Translation: AAA58112.1.
U00096 Genomic DNA. Translation: AAC76340.1.
AP009048 Genomic DNA. Translation: BAE77976.1.
PIRR5EC22. G23129.
RefSeqNP_417774.1. NC_000913.3.
YP_492117.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1P85electron microscopy12.30Q1-110[»]
1P86electron microscopy11.50Q1-110[»]
1VS6X-ray3.46S1-110[»]
1VS8X-ray3.46S1-110[»]
1VT2X-ray3.30S1-110[»]
2AW4X-ray3.46S1-110[»]
2AWBX-ray3.46S1-110[»]
2GYAelectron microscopy15.00Q5-110[»]
2GYCelectron microscopy15.00Q5-110[»]
2I2TX-ray3.22S1-110[»]
2I2VX-ray3.22S1-110[»]
2J28electron microscopy8.00S1-110[»]
2QAMX-ray3.21S1-110[»]
2QAOX-ray3.21S1-110[»]
2QBAX-ray3.54S1-110[»]
2QBCX-ray3.54S1-110[»]
2QBEX-ray3.30S1-110[»]
2QBGX-ray3.30S1-110[»]
2QBIX-ray4.00S1-110[»]
2QBKX-ray4.00S1-110[»]
2QOVX-ray3.93S1-110[»]
2QOXX-ray3.93S1-110[»]
2QOZX-ray3.50S1-110[»]
2QP1X-ray3.50S1-110[»]
2RDOelectron microscopy9.10S1-110[»]
2VHMX-ray3.74S1-110[»]
2VHNX-ray3.74S1-110[»]
2WWQelectron microscopy5.80S1-110[»]
2Z4LX-ray4.45S1-110[»]
2Z4NX-ray4.45S1-110[»]
3BBXelectron microscopy10.00S1-110[»]
3DF2X-ray3.50S1-110[»]
3DF4X-ray3.50S1-110[»]
3E1Belectron microscopy-L1-110[»]
3E1Delectron microscopy-L1-110[»]
3FIKelectron microscopy6.70S1-110[»]
3I1NX-ray3.19S1-110[»]
3I1PX-ray3.19S1-110[»]
3I1RX-ray3.81S1-110[»]
3I1TX-ray3.81S1-110[»]
3I20X-ray3.71S1-110[»]
3I22X-ray3.71S1-110[»]
3IZTelectron microscopy-T1-110[»]
3IZUelectron microscopy-T1-110[»]
3J01electron microscopy-S1-110[»]
3J0Telectron microscopy12.10U1-110[»]
3J0Welectron microscopy14.70U1-110[»]
3J0Yelectron microscopy13.50U1-110[»]
3J11electron microscopy13.10U1-110[»]
3J12electron microscopy11.50U1-110[»]
3J14electron microscopy11.50U1-110[»]
3J19electron microscopy8.30S1-110[»]
3J37electron microscopy9.80W1-110[»]
3J4Xelectron microscopy12.00S1-110[»]
3J50electron microscopy20.00S1-110[»]
3J51electron microscopy17.00S1-110[»]
3J52electron microscopy12.00S1-110[»]
3J54electron microscopy13.00S1-110[»]
3J56electron microscopy15.00S1-110[»]
3J58electron microscopy17.00S1-110[»]
3J5Aelectron microscopy12.00S1-110[»]
3J5Celectron microscopy17.00S1-110[»]
3J5Eelectron microscopy17.00S1-110[»]
3J5Gelectron microscopy20.00S1-110[»]
3J5Ielectron microscopy15.00S1-110[»]
3J5Kelectron microscopy9.00S1-110[»]
3J5Lelectron microscopy6.60S1-110[»]
3J5Oelectron microscopy6.80S1-110[»]
3J5Uelectron microscopy7.60U1-110[»]
3J5Welectron microscopy7.60V1-110[»]
3KCRelectron microscopy-S1-110[»]
3OASX-ray3.25S1-110[»]
3OATX-ray3.25S1-110[»]
3OFCX-ray3.19S1-110[»]
3OFDX-ray3.19S1-110[»]
3OFQX-ray3.10S1-110[»]
3OFRX-ray3.10S1-110[»]
3OFZX-ray3.29S1-110[»]
3OG0X-ray3.29S1-110[»]
3ORBX-ray3.30S1-110[»]
3R8SX-ray3.00S1-110[»]
3R8TX-ray3.00S1-110[»]
3SGFX-ray3.20W1-110[»]
3UOSX-ray3.70W1-110[»]
4GARX-ray3.30S1-110[»]
4GAUX-ray3.30S1-110[»]
4KIXX-ray2.90S1-110[»]
4KIZX-ray2.90S1-110[»]
4KJ1X-ray2.90S1-110[»]
4KJ3X-ray2.90S1-110[»]
4KJ5X-ray2.90S1-110[»]
4KJ7X-ray2.90S1-110[»]
4KJ9X-ray2.90S1-110[»]
4KJBX-ray2.90S1-110[»]
ProteinModelPortalP61175.
SMRP61175. Positions 1-110.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-35983N.
IntActP61175. 128 interactions.
MINTMINT-1253134.
STRING511145.b3315.

Chemistry

ChEMBLCHEMBL2363135.

Proteomic databases

PaxDbP61175.
PRIDEP61175.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76340; AAC76340; b3315.
BAE77976; BAE77976; BAE77976.
GeneID12932293.
947813.
KEGGecj:Y75_p3861.
eco:b3315.
PATRIC32122062. VBIEscCol129921_3408.

Organism-specific databases

EchoBASEEB0875.
EcoGeneEG10882. rplV.

Phylogenomic databases

eggNOGCOG0091.
HOGENOMHOG000205046.
KOK02890.
OMAMKRIRPR.
OrthoDBEOG6V4GKB.
PhylomeDBP61175.

Enzyme and pathway databases

BioCycEcoCyc:EG10882-MONOMER.
ECOL316407:JW3277-MONOMER.

Gene expression databases

GenevestigatorP61175.

Family and domain databases

Gene3D3.90.470.10. 1 hit.
HAMAPMF_01331_B. Ribosomal_L22_B.
InterProIPR001063. Ribosomal_L22.
IPR018260. Ribosomal_L22/L17_CS.
IPR005727. Ribosomal_L22_bac/chlpt-type.
[Graphical view]
PANTHERPTHR13501. PTHR13501. 1 hit.
PfamPF00237. Ribosomal_L22. 1 hit.
[Graphical view]
SUPFAMSSF54843. SSF54843. 1 hit.
TIGRFAMsTIGR01044. rplV_bact. 1 hit.
PROSITEPS00464. RIBOSOMAL_L22. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP61175.
PROP61175.

Entry information

Entry nameRL22_ECOLI
AccessionPrimary (citable) accession number: P61175
Secondary accession number(s): P02423, Q2M6Y0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 11, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene