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P0A7M9 (RL31_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 77. 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.

Cofactor

Binds 1 zinc ion per subunit By similarity.

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 By similarity
Metal binding181Zinc By similarity
Metal binding371Zinc By similarity
Metal binding401Zinc By similarity

Amino acid modifications

Modified residue81N6-acetyllysine Ref.8

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 277:1453-1474(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, MASS SPECTROMETRY.
Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
[9]"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_000913.2.
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[»]
ProteinModelPortalP0A7M9.
SMRP0A7M9. Positions 1-70.
ModBaseSearch...

Protein-protein interaction databases

IntActP0A7M9. 7 interactions.
STRING511145.b3936.

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.
OMAEGIHPKY.
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.
[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.

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: May 1, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic 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