50S ribosomal protein L31 - Escherichia coli (strain K12)

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P0A7M9 (RL31_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 77. History...

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

Documents (4) |

Third-party data

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

Names and origin

Protein names

Recommended name:
50S ribosomal protein L31

Gene names

Name:	rpmE
Ordered Locus Names:	b3936, JW3907

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	70 AA.
Sequence status	Complete.
Protein existence	Evidence 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

Ontologies

Keywords
Ligand	Metal-binding RNA-binding Zinc rRNA-binding
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	translation Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytosolic large ribosomal subunit Inferred from direct assay Ref.6. Source: EcoCyc
Molecular_function	rRNA binding Inferred from electronic annotation. Source: UniProtKB-KW structural constituent of ribosome Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from direct assay PubMed 22196016. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 70

50S ribosomal protein L31 HAMAP-Rule MF_00501

PRO_0000173102

Sites

Metal binding

Zinc By similarity

Metal binding

Zinc By similarity

Metal binding

Zinc By similarity

Metal binding

Zinc By similarity

Amino acid modifications

Modified residue

N6-acetyllysine Ref.8

Secondary structure

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A7M9 [UniParc].

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

7,871

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

        70 
NKRFNIPGSK

« Hide

References

	« Hide 'large scale' referencesShow '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.

PIR

R5EC31. S40879.

RefSeq

NP_418371.1. NC_000913.2.
YP_491515.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P0A7M9.

SMR

P0A7M9. Positions 1-70.

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A7M9. 7 interactions.

STRING

511145.b3936.

Proteomic databases

PaxDb

P0A7M9.

PRIDE

P0A7M9.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76918; AAC76918; b3936.
BAE77374; BAE77374; BAE77374.

GeneID

12932190.
948425.

KEGG

ecj:Y75_p3251.
eco:b3936.

PATRIC

32123389. VBIEscCol129921_4055.

Organism-specific databases

EchoBASE

EB0882.

EcoGene

EG10889. rpmE.

Phylogenomic databases

eggNOG

COG0254.

HOGENOM

HOG000284895.

K02909.

OMA

EGIHPKY.

ProtClustDB

PRK00019.

Enzyme and pathway databases

BioCyc

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

Gene expression databases

Genevestigator

P0A7M9.

Family and domain databases

HAMAP

MF_00501. Ribosomal_L31_1.

InterPro

IPR002150. Ribosomal_L31.
[Graphical view]

Pfam

PF01197. Ribosomal_L31. 1 hit.
[Graphical view]

PRINTS

PR01249. RIBOSOMALL31.

TIGRFAMs

TIGR00105. L31. 1 hit.

PROSITE

PS01143. RIBOSOMAL_L31. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0A7M9.

Entry information

Entry name

RL31_ECOLI

Accession

Primary (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 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

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