P60405 (RL2_THET8) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
50S ribosomal protein L2

Gene names

Name:	rplB
Ordered Locus Names:	TTHA1689

Organism

Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Reference proteome] [HAMAP]

Taxonomic identifier

300852 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus › Thermus thermophilus

Protein attributes

Sequence length	276 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	One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial By similarity. Makes several contacts with the 16S rRNA (forming bridge B7b) in the 70S ribosome. HAMAP-Rule MF_01320_B
Subunit structure	Part of the 50S ribosomal subunit. Forms a bridge to the 30S subunit in the 70S ribosome, contacting the 16S rRNA. May also make transient contacts with protein S6 during translation in the 70S ribosome. Ref.5
Sequence similarities	Belongs to the ribosomal protein L2P family.
Mass spectrometry	Molecular mass is 30337 Da from positions 2 - 276. Determined by MALDI. Ref.3

Ontologies

Keywords
Ligand	RNA-binding rRNA-binding
Molecular function	Ribonucleoprotein Ribosomal protein
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	large ribosomal subunit Inferred from electronic annotation. Source: InterPro
Molecular_function	rRNA binding Inferred from electronic annotation. Source: HAMAP structural constituent of ribosome Inferred from electronic annotation. Source: InterPro transferase activity Inferred from electronic annotation. Source: InterPro
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 – 276

275

50S ribosomal protein L2 HAMAP-Rule MF_01320_B

PRO_0000129641

Secondary structure

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276

Helix Strand Turn

Details...

Beta strand

3 – 5

3

Beta strand

8 – 10

3

Turn

11 – 15

5

Beta strand

17 – 19

3

Turn

22 – 24

3

Helix

31 – 33

3

Beta strand

34 – 36

3

Beta strand

43 – 48

6

Beta strand

49 – 54

6

Beta strand

61 – 63

3

Helix

70 – 72

3

Beta strand

77 – 83

7

Beta strand

88 – 90

3

Beta strand

92 – 97

6

Beta strand

102 – 106

5

Beta strand

108 – 110

3

Beta strand

119 – 123

5

Beta strand

125 – 128

4

Beta strand

130 – 132

3

Helix

133 – 135

3

Beta strand

141 – 148

8

Turn

149 – 151

3

Beta strand

153 – 156

4

Beta strand

158 – 160

3

Beta strand

163 – 169

7

Beta strand

172 – 176

5

Beta strand

178 – 180

3

Beta strand

182 – 186

5

Beta strand

190 – 194

5

Helix

199 – 203

5

Helix

209 – 214

6

Helix

223 – 225

3

Turn

228 – 230

3

Beta strand

232 – 234

3

Beta strand

236 – 239

4

Beta strand

243 – 245

3

Beta strand

251 – 253

3

Helix

265 – 269

5

Beta strand

270 – 272

3

Sequences

	Sequence		Length	Mass (Da)
	P60405 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 7CF40C2BD586349B	FASTA	276	30,468
	10 20 30 40 50 60 MAVKKFKPYT PSRRFMTVAD FSEITKTEPE KSLVKPLKKT GGRNNQGRIT VRFRGGGHKR 70 80 90 100 110 120 LYRIIDFKRW DKVGIPAKVA AIEYDPNRSA RIALLHYVDG EKRYIIAPDG LQVGQQVVAG 130 140 150 160 170 180 PDAPIQVGNA LPLRFIPVGT VVHAVELEPK KGAKLARAAG TSAQIQGREG DYVILRLPSG 190 200 210 220 230 240 ELRKVHGECY ATVGAVGNAD HKNIVLGKAG RSRWLGRRPH VRGAAMNPVD HPHGGGEGRA 250 260 270 PRGRPPASPW GWQTKGLKTR KRRKPSSRFI IARRKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of Thermus thermophilus HB8." Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S. Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: HB8 / ATCC 27634 / DSM 579.
[2]	"Identification of the 50S ribosomal proteins from the eubacterium Thermus thermophilus." Katsani K.R., Tsiboli P., Anagnostopoulos K., Urlaub H., Choli-Papadopoulou T. Biol. Chem. 381:1079-1087(2000) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-22.
[3]	"Extending ribosomal protein identifications to unsequenced bacterial strains using matrix-assisted laser desorption/ionization mass spectrometry." Suh M.-J., Hamburg D.M., Gregory S.T., Dahlberg A.E., Limbach P.A. Proteomics 5:4818-4831(2005) [PubMed] [Europe PMC] [Abstract] Cited for: MASS SPECTROMETRY.
[4]	"The path of messenger RNA through the ribosome." Yusupova G.Z., Yusupov M.M., Cate J.H.D., Noller H.F. Cell 106:233-241(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (5.0 ANGSTROMS) OF THE RIBOSOME.
[5]	"Crystal structure of the ribosome at 5.5 A resolution." Yusupov M.M., Yusupova G.Z., Baucom A., Lieberman K., Earnest T.N., Cate J.H.D., Noller H.F. Science 292:883-896(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS) OF THE RIBOSOME, INTERSUBUNIT BRIDGE FORMATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AP008226 Genomic DNA. Translation: BAD71512.1.

RefSeq

YP_144955.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GIY	X-ray	5.50	D	1-276	[»]
1YL3	X-ray	5.50	D	71-232	[»]
2HGJ	X-ray	5.00	D	1-276	[»]
2HGQ	X-ray	5.50	D	1-276	[»]
2HGU	X-ray	4.51	D	1-276	[»]
2J01	X-ray	2.80	D	2-275	[»]
2J03	X-ray	2.80	D	2-275	[»]
2V47	X-ray	3.80	D	2-275	[»]
2V49	X-ray	3.80	D	2-275	[»]
2WDI	X-ray	3.30	D	1-276	[»]
2WDJ	X-ray	3.30	D	1-276	[»]
2WDL	X-ray	3.50	D	1-276	[»]
2WDN	X-ray	3.50	D	1-276	[»]
2WH2	X-ray	3.45	D	1-276	[»]
2WH4	X-ray	3.45	D	1-276	[»]
2WRJ	X-ray	3.60	D	1-276	[»]
2WRL	X-ray	3.60	D	1-276	[»]
2WRO	X-ray	3.60	D	1-276	[»]
2WRR	X-ray	3.60	D	1-276	[»]
2X9S	X-ray	3.10	D	1-276	[»]
2X9U	X-ray	3.10	D	1-276	[»]
2XG0	X-ray	3.20	D	1-276	[»]
2XG2	X-ray	3.20	D	1-276	[»]
2XQE	X-ray	3.10	D	1-276	[»]
2XTG	electron microscopy	7.80	D	1-276	[»]
2XUX	electron microscopy	7.60	D	1-276	[»]
2Y0V	X-ray	3.10	D	1-276	[»]
2Y0X	X-ray	3.10	D	1-276	[»]
2Y0Z	X-ray	3.10	D	1-276	[»]
2Y11	X-ray	3.10	D	1-276	[»]
2Y13	X-ray	3.10	D	1-276	[»]
2Y15	X-ray	3.10	D	1-276	[»]
2Y17	X-ray	3.10	D	1-276	[»]
2Y19	X-ray	3.10	D	1-276	[»]
3FIN	electron microscopy	6.40	D	2-273	[»]
3HUX	X-ray	3.10	D	1-276	[»]
3HUZ	X-ray	3.10	D	1-276	[»]
3I8F	X-ray	3.10	D	1-276	[»]
3I8I	X-ray	3.10	D	1-276	[»]
3I9C	X-ray	3.50	D	1-276	[»]
3I9E	X-ray	3.50	D	1-276	[»]
3KIR	X-ray	3.30	D	1-276	[»]
3KIT	X-ray	3.30	D	1-276	[»]
3KIW	X-ray	3.60	D	1-276	[»]
3KIY	X-ray	3.60	D	1-276	[»]
3KNI	X-ray	3.00	D	1-276	[»]
3KNK	X-ray	3.00	D	1-276	[»]
3KNM	X-ray	3.45	D	1-276	[»]
3KNO	X-ray	3.45	D	1-276	[»]
3OH5	X-ray	3.00	D	1-276	[»]
3OH7	X-ray	3.00	D	1-276	[»]
3OHJ	X-ray	3.00	D	1-276	[»]
3OHK	X-ray	3.00	D	1-276	[»]
3OHZ	X-ray	3.00	D	1-276	[»]
3OI1	X-ray	3.00	D	1-276	[»]
3OI3	X-ray	3.10	D	1-276	[»]
3OI5	X-ray	3.10	D	1-276	[»]
3TVE	X-ray	3.10	D	2-273	[»]
3TVH	X-ray	3.10	D	2-273	[»]
3UXQ	X-ray	3.20	D	1-276	[»]
3UXR	X-ray	3.20	D	1-276	[»]
3UYE	X-ray	3.00	D	1-276	[»]
3UYG	X-ray	3.00	D	1-276	[»]
3UZ1	X-ray	3.30	D	1-276	[»]
3UZ2	X-ray	3.30	D	1-276	[»]
3UZ8	X-ray	3.00	D	1-276	[»]
3UZ9	X-ray	3.00	D	1-276	[»]
3UZF	X-ray	3.30	D	1-276	[»]
3UZH	X-ray	3.30	D	1-276	[»]
3UZK	X-ray	3.30	D	1-276	[»]
3UZN	X-ray	3.30	D	1-276	[»]
3V23	X-ray	3.00	D	1-276	[»]
3V25	X-ray	3.00	D	1-276	[»]
3V27	X-ray	3.10	D	1-276	[»]
3V29	X-ray	3.10	D	1-276	[»]
3V2D	X-ray	2.70	D	1-276	[»]
3V2F	X-ray	2.70	D	1-276	[»]
3ZVP	X-ray	3.80	D	1-276	[»]
4ABS	X-ray	3.10	D	1-276	[»]
4DHA	X-ray	3.20	D	1-276	[»]
4DHC	X-ray	3.20	D	1-276	[»]
4G5L	X-ray	3.30	D	1-276	[»]
4G5N	X-ray	3.30	D	1-276	[»]
4G5U	X-ray	3.10	D	1-276	[»]
4G5W	X-ray	3.10	D	1-276	[»]

ProteinModelPortal

P60405.

SMR

P60405. Positions 2-273.

ModBase

Search...

Protein-protein interaction databases

STRING

300852.TTHA1689.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

BAD71512; BAD71512; BAD71512.

GeneID

3168720.

KEGG

ttj:TTHA1689.

PATRIC

23958333. VBITheThe93045_1659.

Phylogenomic databases

eggNOG

COG0090.

HOGENOM

HOG000232982.

KO

K02886.

OMA

STIHCIE.

ProtClustDB

PRK09374.

Family and domain databases

Gene3D

2.30.30.30. 1 hit.
2.40.50.140. 1 hit.
4.10.950.10. 1 hit.

HAMAP

MF_01320_B. Ribosomal_L2_B.

InterPro

IPR012340. NA-bd_OB-fold.
IPR022666. Rbsml_prot_L2_RNA-bd_dom.
IPR014722. Rib_L2_dom2.
IPR002171. Ribosomal_L2.
IPR005880. Ribosomal_L2_bac/org-type.
IPR022669. Ribosomal_L2_C.
IPR022671. Ribosomal_L2_CS.
IPR014726. Ribosomal_L2_dom3.
IPR008991. Translation_prot_SH3-like.
[Graphical view]

PANTHER

PTHR13691. PTHR13691. 1 hit.
PTHR13691:SF5. PTHR13691:SF5. 1 hit.

Pfam

PF00181. Ribosomal_L2. 1 hit.
PF03947. Ribosomal_L2_C. 1 hit.
[Graphical view]

PIRSF

PIRSF002158. Ribosomal_L2. 1 hit.

SUPFAM

SSF50249. Nucleic_acid_OB. 1 hit.
SSF50104. Transl_SH3_like. 1 hit.

TIGRFAMs

TIGR01171. rplB_bact. 1 hit.

PROSITE

PS00467. RIBOSOMAL_L2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P60405.

Entry information

Entry name

RL2_THET8

Accession

Primary (citable) accession number: P60405
Secondary accession number(s): Q5SHP1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 16, 2004
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 87 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program