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P0A7M9 (RL31_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 85. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
50S ribosomal protein L31
Gene names
Name:rpmE
Ordered Locus Names:b3936, JW3907
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length70 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds the 23S rRNA By similarity. HAMAP-Rule MF_00501

Cofactor

Binds 1 zinc ion per subunit. Only 1 ligand appears to be Cys, the other are thought to be His and either backbone amides or solvent (Ref.9). Ref.9

Subunit structure

Part of the 50S ribosomal subunit.

Post-translational modification

Proteolytically cleaved by protease VII to yield a peptide lacking residues 63-70. It is not clear if this is due to protein degradation or is a bona fide processing event in the strain used in Ref.4 and Ref.6. In strains B, D10, MRE-600 and Q13 the only protein seen in Ref.6 was full length; the last 7 amino acids were sequenced only for strain MRE-600. HAMAP-Rule MF_00501

Sequence similarities

Belongs to the ribosomal protein L31P family. Type A subfamily.

Mass spectrometry

Molecular mass is 6971.1 Da from positions 1 - 62. Determined by MALDI. Ref.7

Molecular mass is 7871.0 Da from positions 1 - 70. Determined by MALDI. Ref.7

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 707050S ribosomal protein L31 HAMAP-Rule MF_00501
PRO_0000173102

Sites

Metal binding161Zinc Probable

Amino acid modifications

Modified residue81N6-acetyllysine Ref.8

Experimental info

Mutagenesis161C → S: No Zn(2+) binding. Ref.9
Mutagenesis181C → S: Binds Zn(2+) normally. Ref.9
Mutagenesis37 – 404CSKC → SSKS: Binds Zn(2+) normally. Ref.9

Secondary structure

............ 70
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A7M9 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: D657A681A0B858CF

FASTA707,871
        10         20         30         40         50         60 
MKKDIHPKYE EITASCSCGN VMKIRSTVGH DLNLDVCSKC HPFFTGKQRD VATGGRVDRF 

        70 
NKRFNIPGSK 

« Hide

References

« Hide 'large scale' references
[1]"Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes."
Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.
Nucleic Acids Res. 21:3391-3398(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[2]"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.
[3]"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.
[4]"Primary structure of Escherichia coli ribosomal protein L31."
Brosius J.
Biochemistry 17:501-508(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-62.
Strain: B.
[5]"Small genes/gene-products in Escherichia coli K-12."
Wasinger V.C., Humphery-Smith I.
FEMS Microbiol. Lett. 169:375-382(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-10.
Strain: K12.
[6]"Characterization of Escherichia coli 50S ribosomal protein L31."
Eistetter A.J., Butler P.D., Traut R.R., Fanning T.G.
FEMS Microbiol. Lett. 180:345-349(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 64-70 (STRAIN MRE-600), EXAMINATION OF MOLECULAR WEIGHT IN SEVERAL STRAINS.
Strain: B, K12 / D10, K12 / Q13 and MRE-600.
[7]"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.
[8]"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-8, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
[9]"Characterization of Zn(II)-responsive ribosomal proteins YkgM and L31 in E. coli."
Hensley M.P., Gunasekera T.S., Easton J.A., Sigdel T.K., Sugarbaker S.A., Klingbeil L., Breece R.M., Tierney D.L., Crowder M.W.
J. Inorg. Biochem. 111:164-172(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ZINC-BINDING, COFACTOR, MUTAGENESIS OF CYS-16; CYS-18 AND 37-CYS--CYS-40.
Strain: BW21135.
[10]"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
X78541 Genomic DNA. Translation: CAA55286.1.
L19201 Genomic DNA. Translation: AAB03068.1.
U00096 Genomic DNA. Translation: AAC76918.1.
AP009048 Genomic DNA. Translation: BAE77374.1.
PIRR5EC31. S40879.
RefSeqNP_418371.1. NC_000913.3.
YP_491515.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1VS6X-ray3.46Z1-70[»]
1VS8X-ray3.46Z1-70[»]
2AW4X-ray3.46Z1-70[»]
2AWBX-ray3.46Z1-70[»]
2J28electron microscopy8.00Z1-70[»]
2RDOelectron microscopy9.10Z1-70[»]
2VHMX-ray3.74Z1-70[»]
2VHNX-ray3.74Z1-70[»]
3BBXelectron microscopy10.00Z1-70[»]
3E1Belectron microscopy-S1-70[»]
3E1Delectron microscopy-S1-70[»]
3IZTelectron microscopy-b1-70[»]
3IZUelectron microscopy-b1-70[»]
3J0Telectron microscopy12.1021-70[»]
3J0Welectron microscopy14.7021-70[»]
3J0Yelectron microscopy13.5021-70[»]
3J11electron microscopy13.1021-70[»]
3J12electron microscopy11.5021-70[»]
3J14electron microscopy11.5021-70[»]
3J37electron microscopy9.8041-70[»]
ProteinModelPortalP0A7M9.
SMRP0A7M9. Positions 1-70.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP0A7M9. 14 interactions.
STRING511145.b3936.

Chemistry

ChEMBLCHEMBL2363135.

Proteomic databases

PaxDbP0A7M9.
PRIDEP0A7M9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76918; AAC76918; b3936.
BAE77374; BAE77374; BAE77374.
GeneID12932190.
948425.
KEGGecj:Y75_p3251.
eco:b3936.
PATRIC32123389. VBIEscCol129921_4055.

Organism-specific databases

EchoBASEEB0882.
EcoGeneEG10889. rpmE.

Phylogenomic databases

eggNOGCOG0254.
HOGENOMHOG000284895.
KOK02909.
OMACACGETF.
OrthoDBEOG6DVJZM.
PhylomeDBP0A7M9.
ProtClustDBPRK00019.

Enzyme and pathway databases

BioCycEcoCyc:EG10889-MONOMER.
ECOL316407:JW3907-MONOMER.

Gene expression databases

GenevestigatorP0A7M9.

Family and domain databases

HAMAPMF_00501. Ribosomal_L31_1.
InterProIPR002150. Ribosomal_L31.
IPR027491. Ribosomal_L31_A.
[Graphical view]
PfamPF01197. Ribosomal_L31. 1 hit.
[Graphical view]
PRINTSPR01249. RIBOSOMALL31.
TIGRFAMsTIGR00105. L31. 1 hit.
PROSITEPS01143. RIBOSOMAL_L31. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A7M9.
PROP0A7M9.

Entry information

Entry nameRL31_ECOLI
AccessionPrimary (citable) accession number: P0A7M9
Secondary accession number(s): P02432, Q2M8N2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 7, 2005
Last modified: April 16, 2014
This is version 85 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