50S ribosomal protein L22 - Escherichia coli (strain K12)

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P61175 (RL22_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 103. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
50S ribosomal protein L22

Gene names

Name:	rplV
Synonyms:	eryB
Ordered Locus Names:	b3315, JW3277

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	110 AA.
Sequence status	Complete.
Protein existence	Evidence 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. HAMAP-Rule MF_01331_B
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

Ontologies

Keywords
Biological process	Antibiotic resistance
Ligand	RNA-binding rRNA-binding
Molecular function	Ribonucleoprotein Ribosomal protein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	response to antibiotic Inferred from electronic annotation. Source: UniProtKB-KW translation Inferred from electronic annotation. Source: HAMAP
Cellular_component	large ribosomal subunit Inferred from electronic annotation. Source: InterPro
Molecular_function	rRNA binding Inferred from electronic annotation. Source: HAMAP structural constituent of ribosome Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
mobA	P07112	1	EBI-542255,EBI-554383	From a different organism.
ubiG	P17993	1	EBI-542255,EBI-559367

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 110

110

50S ribosomal protein L22 HAMAP-Rule MF_01331_B

PRO_0000125153

Natural variations

Natural variant

R → 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 variant

82 – 84

Missing 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

Mutagenesis

82 – 99

Missing: Incorporated into ribosomes in vivo, but is easily removed by a salt wash.

Mutagenesis

85 – 95

Missing: Incorporates into ribosomes in vivo.

Mutagenesis

G → A, D or S: Abolishes translation elongation arrest of SecM. Ref.9

Mutagenesis

A → S, T or V: Abolishes translation elongation arrest of SecM. Ref.9

Secondary structure

110

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P61175 [UniParc].

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

FASTA

110

12,226

        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' referencesShow '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 277:1453-1474(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.

PIR

R5EC22. G23129.

RefSeq

NP_417774.1. NC_000913.2.
YP_492117.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1P85	electron microscopy	12.30	Q	1-110	[»]
1P86	electron microscopy	11.50	Q	1-110	[»]
1VS6	X-ray	3.46	S	1-110	[»]
1VS8	X-ray	3.46	S	1-110	[»]
1VT2	X-ray	3.30	S	1-110	[»]
2AW4	X-ray	3.46	S	1-110	[»]
2AWB	X-ray	3.46	S	1-110	[»]
2GYA	electron microscopy	15.00	Q	5-110	[»]
2GYC	electron microscopy	15.00	Q	5-110	[»]
2I2T	X-ray	3.22	S	1-110	[»]
2I2V	X-ray	3.22	S	1-110	[»]
2J28	electron microscopy	8.00	S	1-110	[»]
2QAM	X-ray	3.21	S	1-110	[»]
2QAO	X-ray	3.21	S	1-110	[»]
2QBA	X-ray	3.54	S	1-110	[»]
2QBC	X-ray	3.54	S	1-110	[»]
2QBE	X-ray	3.30	S	1-110	[»]
2QBG	X-ray	3.30	S	1-110	[»]
2QBI	X-ray	4.00	S	1-110	[»]
2QBK	X-ray	4.00	S	1-110	[»]
2QOV	X-ray	3.93	S	1-110	[»]
2QOX	X-ray	3.93	S	1-110	[»]
2QOZ	X-ray	3.50	S	1-110	[»]
2QP1	X-ray	3.50	S	1-110	[»]
2RDO	electron microscopy	9.10	S	1-110	[»]
2VHM	X-ray	3.74	S	1-110	[»]
2VHN	X-ray	3.74	S	1-110	[»]
2WWQ	electron microscopy	5.80	S	1-110	[»]
2Z4L	X-ray	4.45	S	1-110	[»]
2Z4N	X-ray	4.45	S	1-110	[»]
3BBX	electron microscopy	10.00	S	1-110	[»]
3DF2	X-ray	3.50	S	1-110	[»]
3DF4	X-ray	3.50	S	1-110	[»]
3E1B	electron microscopy	-	L	1-110	[»]
3E1D	electron microscopy	-	L	1-110	[»]
3FIK	electron microscopy	6.70	S	1-110	[»]
3I1N	X-ray	3.19	S	1-110	[»]
3I1P	X-ray	3.19	S	1-110	[»]
3I1R	X-ray	3.81	S	1-110	[»]
3I1T	X-ray	3.81	S	1-110	[»]
3I20	X-ray	3.71	S	1-110	[»]
3I22	X-ray	3.71	S	1-110	[»]
3IZT	electron microscopy	-	T	1-110	[»]
3IZU	electron microscopy	-	T	1-110	[»]
3J01	electron microscopy	-	S	1-110	[»]
3J0T	electron microscopy	12.10	U	1-110	[»]
3J0W	electron microscopy	14.70	U	1-110	[»]
3J0Y	electron microscopy	13.50	U	1-110	[»]
3J11	electron microscopy	13.10	U	1-110	[»]
3J12	electron microscopy	11.50	U	1-110	[»]
3J14	electron microscopy	11.50	U	1-110	[»]
3J19	electron microscopy	8.30	S	1-110	[»]
3KCR	electron microscopy	-	S	1-110	[»]
3OAS	X-ray	3.25	S	1-110	[»]
3OAT	X-ray	3.25	S	1-110	[»]
3OFC	X-ray	3.19	S	1-110	[»]
3OFD	X-ray	3.19	S	1-110	[»]
3OFQ	X-ray	3.10	S	1-110	[»]
3OFR	X-ray	3.10	S	1-110	[»]
3OFZ	X-ray	3.29	S	1-110	[»]
3OG0	X-ray	3.29	S	1-110	[»]
3ORB	X-ray	3.30	S	1-110	[»]
3R8S	X-ray	3.00	S	1-110	[»]
3R8T	X-ray	3.00	S	1-110	[»]
3SGF	X-ray	3.20	W	1-110	[»]
3UOS	X-ray	3.70	W	1-110	[»]
4GAR	X-ray	3.30	S	1-110	[»]
4GAU	X-ray	3.30	S	1-110	[»]

ProteinModelPortal

P61175.

SMR

P61175. Positions 1-110.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35983N.

IntAct

P61175. 128 interactions.

MINT

MINT-1253134.

STRING

511145.b3315.

Proteomic databases

PaxDb

P61175.

PRIDE

P61175.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76340; AAC76340; b3315.
BAE77976; BAE77976; BAE77976.

GeneID

12932293.
947813.

KEGG

ecj:Y75_p3861.
eco:b3315.

PATRIC

32122062. VBIEscCol129921_3408.

Organism-specific databases

EchoBASE

EB0875.

EcoGene

EG10882. rplV.

Phylogenomic databases

eggNOG

COG0091.

HOGENOM

HOG000205046.

K02890.

OMA

ASRINKR.

ProtClustDB

PRK00565.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10882-MONOMER.
ECOL316407:JW3277-MONOMER.

Gene expression databases

Genevestigator

P61175.

Family and domain databases

Gene3D

3.90.470.10. 1 hit.

HAMAP

MF_01331_B. Ribosomal_L22_B.

InterPro

IPR001063. Ribosomal_L22.
IPR018260. Ribosomal_L22/L17_CS.
IPR005727. Ribosomal_L22_bac/chlpt-type.
[Graphical view]

PANTHER

PTHR13501. PTHR13501. 1 hit.

Pfam

PF00237. Ribosomal_L22. 1 hit.
[Graphical view]

SUPFAM

SSF54843. Ribosomal_L22. 1 hit.

TIGRFAMs

TIGR01044. rplV_bact. 1 hit.

PROSITE

PS00464. RIBOSOMAL_L22. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P61175.

Entry information

Entry name

RL22_ECOLI

Accession

Primary (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:	May 1, 2013
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Ribosomal proteins

Ribosomal proteins families and list of entries

Escherichia coli

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Natural variations

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents