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Protein

50S ribosomal protein L31

Gene

rpmE

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

Functioni

Binds the 23S rRNA.By similarity

Cofactori

Zn2+1 PublicationNote: 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)DescriptionActionsGraphical viewLength
Metal bindingi16ZincCurated1

GO - Molecular functioni

  • rRNA binding Source: UniProtKB-KW
  • structural constituent of ribosome Source: InterPro
  • zinc ion binding Source: EcoCyc

GO - Biological processi

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:EG10889-MONOMER.
MetaCyc:EG10889-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L31
Alternative name(s):
Large ribosomal subunit protein bL31-A1 Publication
Gene namesi
Name:rpmE
Ordered Locus Names:b3936, JW3907
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10889. rpmE.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • cytosolic large ribosomal subunit Source: EcoCyc

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi16C → S: No Zn(2+) binding. 1 Publication1
Mutagenesisi18C → S: Binds Zn(2+) normally. 1 Publication1
Mutagenesisi37 – 40CSKC → SSKS: Binds Zn(2+) normally. 1 Publication4

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001731021 – 7050S ribosomal protein L31Add BLAST70

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei8N6-acetyllysine1 Publication1

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-600.2 Publications

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP0A7M9.
PRIDEiP0A7M9.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit.6 Publications

Protein-protein interaction databases

BioGridi4261184. 44 interactors.
IntActiP0A7M9. 14 interactors.
STRINGi316385.ECDH10B_4125.

Structurei

Secondary structure

170
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 6Combined sources3
Beta strandi18 – 20Combined sources3
Beta strandi38 – 40Combined sources3
Turni49 – 53Combined sources5
Helixi54 – 57Combined sources4
Turni62 – 67Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2J28electron microscopy8.00Z1-70[»]
2RDOelectron microscopy9.10Z1-70[»]
3BBXelectron microscopy10.00Z1-70[»]
3J9Yelectron microscopy3.9061-70[»]
3J9Zelectron microscopy3.60LZ1-70[»]
3JA1electron microscopy3.60L21-70[»]
4V4HX-ray3.46BZ/DZ1-70[»]
4V4QX-ray3.46BZ/DZ1-70[»]
4V5BX-ray3.74AZ/CZ1-70[»]
4V65electron microscopy9.00BS1-70[»]
4V66electron microscopy9.00BS1-70[»]
4V6Kelectron microscopy8.25Ab1-70[»]
4V6Lelectron microscopy13.20Bb1-70[»]
4V6Nelectron microscopy12.10A21-70[»]
4V6Oelectron microscopy14.70B21-70[»]
4V6Pelectron microscopy13.50B21-70[»]
4V6Qelectron microscopy11.50B21-70[»]
4V6Relectron microscopy11.50B21-70[»]
4V6Selectron microscopy13.10A21-70[»]
4V6Velectron microscopy9.80B41-70[»]
5AFIelectron microscopy2.9061-70[»]
5AKAelectron microscopy5.70Z1-70[»]
5IQRelectron microscopy3.00a1-70[»]
5KCSelectron microscopy3.90141-70[»]
5KPSelectron microscopy3.9011-70[»]
5KPVelectron microscopy4.10Z1-70[»]
5KPWelectron microscopy3.90Z1-70[»]
5KPXelectron microscopy3.90Z1-70[»]
5L3Pelectron microscopy3.7041-70[»]
5LZAelectron microscopy3.6061-66[»]
5LZBelectron microscopy5.3061-66[»]
5LZCelectron microscopy4.8061-66[»]
5LZDelectron microscopy3.4061-66[»]
5LZEelectron microscopy3.5061-66[»]
5LZFelectron microscopy4.6061-66[»]
5MDVelectron microscopy2.97a1-70[»]
5MDWelectron microscopy3.06a1-70[»]
5MDYelectron microscopy3.35a1-70[»]
5MDZelectron microscopy3.10a1-70[»]
5MGPelectron microscopy3.1061-66[»]
5NP6electron microscopy3.6041-66[»]
5U9Felectron microscopy3.20291-70[»]
5U9Gelectron microscopy3.20291-70[»]
5UYKelectron microscopy3.90291-66[»]
5UYLelectron microscopy3.60291-66[»]
5UYMelectron microscopy3.20291-66[»]
5UYNelectron microscopy4.00291-66[»]
5UYPelectron microscopy3.90291-66[»]
5UYQelectron microscopy3.80291-66[»]
ProteinModelPortaliP0A7M9.
SMRiP0A7M9.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7M9.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105VFB. Bacteria.
COG0254. LUCA.
HOGENOMiHOG000284895.
InParanoidiP0A7M9.
KOiK02909.
PhylomeDBiP0A7M9.

Family and domain databases

HAMAPiMF_00501. Ribosomal_L31_1. 1 hit.
InterProiView protein in InterPro
IPR034704. L28p-like.
IPR002150. Ribosomal_L31.
IPR027491. Ribosomal_L31_A.
PANTHERiPTHR33280. PTHR33280. 1 hit.
PfamiView protein in Pfam
PF01197. Ribosomal_L31. 1 hit.
PRINTSiPR01249. RIBOSOMALL31.
SUPFAMiSSF143800. SSF143800. 1 hit.
TIGRFAMsiTIGR00105. L31. 1 hit.
PROSITEiView protein in PROSITE
PS01143. RIBOSOMAL_L31. 1 hit.

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:
EMBLi
GenBanki
DDBJi
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.
WP_000710769.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76918; AAC76918; b3936.
BAE77374; BAE77374; BAE77374.
GeneIDi948425.
KEGGiecj:JW3907.
eco:b3936.
PATRICifig|1411691.4.peg.2769.

Similar proteinsi

Entry informationi

Entry nameiRL31_ECOLI
AccessioniPrimary (citable) accession number: P0A7M9
Secondary accession number(s): P02432, Q2M8N2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 7, 2005
Last modified: September 27, 2017
This is version 116 of the entry and version 1 of the sequence. See 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