Reviewed, UniProtKB/Swiss-Prot P0A7M9 (RL31_ECOLI)

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) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	70 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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. HAMAP MF_00501
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 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
Gene Ontology (GO)
Biological process	translation Inferred from electronic annotation. Source: HAMAP
Cellular component	ribosome Inferred from electronic annotation. Source: UniProtKB-KW
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 electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 70

70

50S ribosomal protein L31 HAMAP MF_00501

PRO_0000173102

Sites

Metal binding

16

1

Zinc By similarity

Metal binding

18

1

Zinc By similarity

Metal binding

37

1

Zinc By similarity

Metal binding

40

1

Zinc By similarity

Amino acid modifications

Modified residue

8

1

N6-acetyllysine Ref.8

Secondary structure

1

.

.

.

.

.

.

.

.

70

Helix Strand Turn

Details...

Beta strand

38 – 40

3

Turn

49 – 53

5

Helix

54 – 57

4

Turn

62 – 67

6

Sequences

	Sequence		Length	Mass (Da)
	P0A7M9-1 [UniParc]. Last modified June 7, 2005. Version 1. Checksum: D657A681A0B858CF	FASTA	70	7,871
	10 20 30 40 50 60 MKKDIHPKYE EITASCSCGN VMKIRSTVGH DLNLDVCSKC HPFFTGKQRD VATGGRVDRF 70 NKRFNIPGSK

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: 8346018] [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: 9278503] [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: 16738553] [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: 339950] [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: 9868784] [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: 10556732] [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: 10094780] [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: 18723842] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-8, MASS SPECTROMETRY.
[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: 16272117] [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

EMBLGenBankDDBJ

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

AP_003873.1.
NP_418371.1.

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Genome annotation databases

GeneID

948425.

GenomeReviews

Gene locus JW3907 in contig AP009048_GR.
Gene locus b3936 in contig U00096_GR.

KEGG

ecj:JW3907.
eco:b3936.

Organism-specific databases

EchoBASE

EB0882.

EcoGene

EG10889. rpmE.

CMR

Search...

Phylogenomic databases

HOGENOM

P0A7M9.

OMA

P0A7M9. GRVERFK.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10889-MON.

Family and domain databases

HAMAP

MF_00501.
[Tree]

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...

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:	June 16, 2009
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)