Reviewed, UniProtKB/Swiss-Prot P08895 (RL5_BACST)

Names and origin

Protein names

Recommended name:
    50S ribosomal protein L5
      Short name=BstL5
      Short name=BL5

Gene names

Name:

rplE

Organism

Bacillus stearothermophilus (Geobacillus stearothermophilus)

Taxonomic identifier

1422 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length	179 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs By similarity.
Subunit structure	Contacts the P site tRNA. Forms a bridge to the 30S subunit in the 70S ribosome By similarity. Part of the 50S ribosomal subunit. Part of the 5S rRNA/L5/L18 subcomplex; in this organism only 2 proteins, L5 and L18 have been shown to be part of the 5S rRNA subcomplex, unlike E.coli and T.thermophilus where L25 (TL5) is also found. Has been shown to bind 5S rRNA.
Sequence similarities	Belongs to the ribosomal protein L5P family.
Mass spectrometry	Molecular mass is 20090 Da from positions 1 - 179. Determined by MALDI. Ref.3

Ontologies

Keywords
Ligand	RNA-binding rRNA-binding tRNA-binding
Molecular function	Ribonucleoprotein Ribosomal protein
Technical term	3D-structure 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: HAMAP structural constituent of ribosome Inferred from electronic annotation. Source: InterPro tRNA 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 – 179

179

50S ribosomal protein L5 HAMAP MF_01333

PRO_0000124891

Experimental info

Mutagenesis

33

1

K → A: A 3-fold decrease in binding of the 5S rRNA. Ref.3

Mutagenesis

37

1

N → A: A 25-fold decrease in binding of the 5S rRNA. Ref.3

Mutagenesis

63

1

Q → A: A 12.5-fold decrease in binding of the 5S rRNA. Ref.3

Mutagenesis

77

1

F → A: An 8-fold decrease in binding of the 5S rRNA. Ref.3

Mutagenesis

90

1

T → A: A 4-fold decrease in binding of the 5S rRNA. Ref.3

Secondary structure

1

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179

Helix Strand Turn

Details...

Helix

3 – 10

8

Helix

12 – 20

9

Helix

25 – 27

3

Beta strand

31 – 39

9

Beta strand

43 – 45

3

Helix

47 – 61

15

Beta strand

66 – 69

4

Beta strand

76 – 78

3

Beta strand

84 – 91

8

Helix

93 – 105

13

Helix

108 – 110

3

Beta strand

124 – 133

10

Helix

135 – 137

3

Helix

143 – 145

3

Beta strand

152 – 159

8

Helix

163 – 173

11

Sequences

	Sequence		Length	Mass (Da)
	P08895-1 [UniParc]. Last modified November 1, 1988. Version 1. Checksum: 84E1D7BA91C84E8A	FASTA	179	20,159
	10 20 30 40 50 60 MNRLKEKYVK EVVPALMSKF NYKSIMQVPK IEKIVINMGV GDAVQNPKAL DSAVEELTLI 70 80 90 100 110 120 AGQRPVVTRA KKSIAGFRLR QGMPIGAKVT LRGERMYEFL DKLISVSLPR VRDFRGVSKK 130 140 150 160 170 AFDGRGNYTL GIKEQLIFPE IDYDKVNKVR GMDIVIVTTA NTDEEARELL ALLGMPFQK

References

[1]	"The complete amino acid sequences of the 5 S rRNA binding proteins L5 and L18 from the moderate thermophile Bacillus stearothermophilus ribosome." Kimura J., Kimura M. FEBS Lett. 210:85-90(1987) [PubMed: 3542562] [Abstract] Cited for: PROTEIN SEQUENCE. Strain: ATCC 29609 / DSM 2027 / NCA 1503 / NCIB 8924.
[2]	"Isolation and characterization of 5S RNA-protein complexes from Bacillus stearothermophilus and Escherichia coli ribosomes." Horne J.R., Erdmann V.A. Mol. Gen. Genet. 119:337-344(1972) [PubMed: 4567807] [Abstract] Cited for: ISOLATION OF 5S RNA-PROTEIN COMPLEXES.
[3]	"On the interaction of ribosomal protein L5 with 5S rRNA." Iwasaki K., Kikukawa S., Kawamura S., Kouzuma Y., Tanaka I., Kimura M. Biosci. Biotechnol. Biochem. 66:103-109(2002) [PubMed: 11866091] [Abstract] Cited for: MUTAGENESIS OF CONSERVED RESIDUES, MASS SPECTROMETRY.
[4]	"Ribosomal protein L5 has a highly twisted concave surface and flexible arms responsible for rRNA binding." Nakashima T., Yao M., Kawamura S., Iwasaki K., Kimura M., Tanaka I. RNA 7:692-701(2001) [PubMed: 11350033] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), MUTAGENESIS.

Cross-references

Sequence databases

PIR

R5BS5F. A29102.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IQ4	X-ray	1.80	A/B	1-179	[»]

ModBase

Search...

Family and domain databases

HAMAP

MF_01333.
[Tree]

InterPro

IPR002132. Ribosomal_L5.
[Graphical view]

Gene3D

G3DSA:3.30.1440.10. Ribosomal_L5. 1 hit.

PANTHER

PTHR11994. Ribosomal_L5. 1 hit.

Pfam

PF00281. Ribosomal_L5. 1 hit.
PF00673. Ribosomal_L5_C. 1 hit.
[Graphical view]

PIRSF

PIRSF002161. Ribosomal_L5. 1 hit.

ProDom

PD013434. Ribosomal_L5_mit. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

PS00358. RIBOSOMAL_L5. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

RL5_BACST

Accession

Primary (citable) accession number: P08895

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	November 1, 1988
Last modified:	June 16, 2009
This is version 67 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)