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P0A7M9

- RL31_ECOLI

UniProt

P0A7M9 - RL31_ECOLI

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Protein

50S ribosomal protein L31

Gene

rpmE

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Binds the 23S rRNA.By similarity

Cofactori

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 (PubMed:22196016).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi16 – 161ZincCurated

GO - Molecular functioni

  1. rRNA binding Source: UniProtKB-KW
  2. structural constituent of ribosome Source: InterPro
  3. zinc ion binding Source: EcoCyc

GO - Biological processi

  1. translation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

Metal-binding, RNA-binding, rRNA-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:EG10889-MONOMER.
ECOL316407:JW3907-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L31
Gene namesi
Name:rpmE
Ordered Locus Names:b3936, JW3907
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10889. rpmE.

Subcellular locationi

GO - Cellular componenti

  1. cytosolic large ribosomal subunit Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi16 – 161C → S: No Zn(2+) binding. 1 Publication
Mutagenesisi18 – 181C → S: Binds Zn(2+) normally. 1 Publication
Mutagenesisi37 – 404CSKC → SSKS: Binds Zn(2+) normally. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 707050S ribosomal protein L31PRO_0000173102Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei8 – 81N6-acetyllysine1 Publication

Post-translational modificationi

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 PubMed:339950 and PubMed:10556732. In strains B, D10, MRE-600 and Q13 the only protein seen in PubMed:10556732 was full length; the last 7 amino acids were sequenced only for strain MRE-600.

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP0A7M9.
PRIDEiP0A7M9.

Expressioni

Gene expression databases

GenevestigatoriP0A7M9.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit.

Protein-protein interaction databases

IntActiP0A7M9. 14 interactions.
STRINGi511145.b3936.

Structurei

Secondary structure

1
70
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 63
Beta strandi18 – 203
Beta strandi38 – 403
Turni49 – 535
Helixi54 – 574
Turni62 – 676

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP0A7M9.
SMRiP0A7M9. Positions 1-70.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7M9.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0254.
HOGENOMiHOG000284895.
InParanoidiP0A7M9.
KOiK02909.
OMAiTANCSCG.
OrthoDBiEOG6DVJZM.
PhylomeDBiP0A7M9.

Family and domain databases

HAMAPiMF_00501. Ribosomal_L31_1.
InterProiIPR002150. Ribosomal_L31.
IPR027491. Ribosomal_L31_A.
[Graphical view]
PfamiPF01197. Ribosomal_L31. 1 hit.
[Graphical view]
PRINTSiPR01249. RIBOSOMALL31.
TIGRFAMsiTIGR00105. L31. 1 hit.
PROSITEiPS01143. RIBOSOMAL_L31. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A7M9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKKDIHPKYE EITASCSCGN VMKIRSTVGH DLNLDVCSKC HPFFTGKQRD
60 70
VATGGRVDRF NKRFNIPGSK
Length:70
Mass (Da):7,871
Last modified:June 7, 2005 - v1
Checksum:iD657A681A0B858CF
GO

Mass spectrometryi

Molecular mass is 6971.1 Da from positions 1 - 62. Determined by MALDI. 1 Publication
Molecular mass is 7871.0 Da from positions 1 - 70. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X78541 Genomic DNA. Translation: CAA55286.1.
L19201 Genomic DNA. Translation: AAB03068.1.
U00096 Genomic DNA. Translation: AAC76918.1.
AP009048 Genomic DNA. Translation: BAE77374.1.
PIRiS40879. R5EC31.
RefSeqiNP_418371.1. NC_000913.3.
YP_491515.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76918; AAC76918; b3936.
BAE77374; BAE77374; BAE77374.
GeneIDi12932190.
948425.
KEGGiecj:Y75_p3251.
eco:b3936.
PATRICi32123389. VBIEscCol129921_4055.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X78541 Genomic DNA. Translation: CAA55286.1 .
L19201 Genomic DNA. Translation: AAB03068.1 .
U00096 Genomic DNA. Translation: AAC76918.1 .
AP009048 Genomic DNA. Translation: BAE77374.1 .
PIRi S40879. R5EC31.
RefSeqi NP_418371.1. NC_000913.3.
YP_491515.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1VS6 X-ray 3.46 Z 1-70 [» ]
1VS8 X-ray 3.46 Z 1-70 [» ]
2AW4 X-ray 3.46 Z 1-70 [» ]
2AWB X-ray 3.46 Z 1-70 [» ]
2J28 electron microscopy 8.00 Z 1-70 [» ]
2RDO electron microscopy 9.10 Z 1-70 [» ]
2VHM X-ray 3.74 Z 1-70 [» ]
2VHN X-ray 3.74 Z 1-70 [» ]
3BBX electron microscopy 10.00 Z 1-70 [» ]
3E1B electron microscopy - S 1-70 [» ]
3E1D electron microscopy - S 1-70 [» ]
3IZT electron microscopy - b 1-70 [» ]
3IZU electron microscopy - b 1-70 [» ]
3J0T electron microscopy 12.10 2 1-70 [» ]
3J0W electron microscopy 14.70 2 1-70 [» ]
3J0Y electron microscopy 13.50 2 1-70 [» ]
3J11 electron microscopy 13.10 2 1-70 [» ]
3J12 electron microscopy 11.50 2 1-70 [» ]
3J14 electron microscopy 11.50 2 1-70 [» ]
3J37 electron microscopy 9.80 4 1-70 [» ]
ProteinModelPortali P0A7M9.
SMRi P0A7M9. Positions 1-70.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P0A7M9. 14 interactions.
STRINGi 511145.b3936.

Chemistry

ChEMBLi CHEMBL2363135.

Proteomic databases

PaxDbi P0A7M9.
PRIDEi P0A7M9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76918 ; AAC76918 ; b3936 .
BAE77374 ; BAE77374 ; BAE77374 .
GeneIDi 12932190.
948425.
KEGGi ecj:Y75_p3251.
eco:b3936.
PATRICi 32123389. VBIEscCol129921_4055.

Organism-specific databases

EchoBASEi EB0882.
EcoGenei EG10889. rpmE.

Phylogenomic databases

eggNOGi COG0254.
HOGENOMi HOG000284895.
InParanoidi P0A7M9.
KOi K02909.
OMAi TANCSCG.
OrthoDBi EOG6DVJZM.
PhylomeDBi P0A7M9.

Enzyme and pathway databases

BioCyci EcoCyc:EG10889-MONOMER.
ECOL316407:JW3907-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A7M9.
PROi P0A7M9.

Gene expression databases

Genevestigatori P0A7M9.

Family and domain databases

HAMAPi MF_00501. Ribosomal_L31_1.
InterProi IPR002150. Ribosomal_L31.
IPR027491. Ribosomal_L31_A.
[Graphical view ]
Pfami PF01197. Ribosomal_L31. 1 hit.
[Graphical view ]
PRINTSi PR01249. RIBOSOMALL31.
TIGRFAMsi TIGR00105. L31. 1 hit.
PROSITEi PS01143. RIBOSOMAL_L31. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: ZINC-BINDING, COFACTOR, MUTAGENESIS OF CYS-16; CYS-18 AND 37-CYS--CYS-40.
    Strain: BW21135.
  10. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.

Entry informationi

Entry nameiRL31_ECOLI
AccessioniPrimary (citable) accession number: P0A7M9
Secondary accession number(s): P02432, Q2M8N2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 7, 2005
Last modified: October 29, 2014
This is version 89 of the entry and version 1 of the sequence. [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

External Data

Dasty 3