P41201 (RL5_THETH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
50S ribosomal protein L5

Alternative name(s):
TL4
TthL5

Gene names

Name:	rplE
Synonyms:	rpl5

Organism

Thermus thermophilus

Taxonomic identifier

274 [NCBI]

Taxonomic lineage

Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus

Protein attributes

Sequence length	182 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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 (forming bridge B1b) connecting the head of the 30S subunit to the top of the 50S subunit. The bridge itself contacts the P site tRNA and is implicated in movement during ribosome translocation. Also contacts the P site tRNA independently of the intersubunit bridge; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs By similarity. HAMAP MF_01333_B
Subunit structure	Forms a bridge to the 30S subunit in the 70S ribosome, contacting protein S13; this bridge is straddled by the 5S rRNA. Contacts the P site tRNA By similarity. Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18/L25 (TL5) subcomplex.
Sequence similarities	Belongs to the ribosomal protein L5P family.

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: InterPro
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 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

Initiator methionine

1

1

Removed Ref.2

Chain

2 – 182

181

50S ribosomal protein L5 HAMAP MF_01333_B

PRO_0000125015

Experimental info

Sequence conflict

5

1

V → L AA sequence Ref.2

Sequence conflict

33

1

R → RE AA sequence Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

182

Helix Strand Turn

Details...

Helix

6 – 13

8

Helix

15 – 22

8

Helix

28 – 30

3

Beta strand

34 – 42

9

Turn

44 – 46

3

Helix

50 – 64

15

Beta strand

69 – 72

4

Beta strand

80 – 83

4

Beta strand

86 – 94

9

Helix

96 – 108

13

Turn

109 – 113

5

Beta strand

127 – 135

9

Turn

149 – 151

3

Beta strand

155 – 162

8

Helix

166 – 176

11

Sequences

	Sequence		Length	Mass (Da)
	P41201 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 69A3361F6825929B	FASTA	182	21,030
	10 20 30 40 50 60 MPLDVALKRK YYEEVRPELI RRFGYQNVWE VPRLEKVVIN QGLGEAKEDA RILEKAAQEL 70 80 90 100 110 120 ALITGQKPAV TRAKKSISNF KLRKGMPIGL RVTLRRDRMW IFLEKLLNVA LPRIRDFRGL 130 140 150 160 170 180 NPNSFDGRGN YNLGLREQLI FPEITYDMVD ALRGMDIAVV TTAETDEEAR ALLELLGFPF RK

References

[1]	"Comparative analysis of ribosomal protein L5 sequences from bacteria of the genus Thermus." Jahn O., Hartmann R.K., Boeckh T., Erdmann V.A. Biochimie 73:669-678(1991) [PubMed: 1764514] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 33923 / DSM 674 / AT-62.
[2]	"5S rRNA binding ribosomal proteins from Thermus thermophilus: identification and some structural properties." Gongadze G.M., Kashparov I., Lorenz S., Schroeder W., Erdmann V.A., Liljas A., Garber M.B. FEBS Lett. 386:260-262(1996) [PubMed: 8647295] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-40. Strain: VK1.
[3]	"The Thermus thermophilus 5S rRNA-protein complex: identification of specific binding sites for proteins L5 and L18 in 5S rRNA." Gongadze G.M., Perederina A.A., Meshcheriakov V.A., Fedorov R.V., Moskalenko S.E., Rak A.V., Serganov A.A., Shcherbakov D.V., Nikonov S.V., Garber M.B. Mol. Biol. (Mosk.) 35:610-616(2001) [PubMed: 11524947] [Abstract] Cited for: BINDING TO 5S RRNA. Strain: VK1.
[4]	"Detailed analysis of RNA-protein interactions within the bacterial ribosomal protein L5/5S rRNA complex." Perederina A., Nevskaya N., Nikonov O., Nikulin A., Dumas P., Yao M., Tanaka I., Garber M.B., Gongadze G., Nikonov S. RNA 8:1548-1557(2002) [PubMed: 12515387] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF THE PROTEIN IN COMPLEX WITH A 5S RRNA FRAGMENT. Strain: VK1.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

S77826 Genomic DNA. Translation: AAB21093.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MJI	X-ray	2.50	A/B	1-182	[»]

ProteinModelPortal

P41201.

SMR

P41201. Positions 1-182.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

HAMAP

MF_01333_B. Ribosomal_L5_B.
[Tree]

InterPro

IPR002132. Ribosomal_L5.
IPR020930. Ribosomal_L5_bac-type.
IPR020929. Ribosomal_L5_CS.
IPR022803. Ribosomal_L5_domain.
[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.

SUPFAM

SSF55282. Ribosomal_L5. 1 hit.

PROSITE

PS00358. RIBOSOMAL_L5. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

RL5_THETH

Accession

Primary (citable) accession number: P41201

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	January 23, 2007
Last modified:	November 30, 2010
This is version 73 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program