Reviewed, UniProtKB/Swiss-Prot P04257 (RL2_BACST)

Names and origin

Protein names

Recommended name:
    50S ribosomal protein L2
      Short name=BstL2
Alternative name(s):
    L3

Gene names

Name:

rplB

Organism

Bacillus stearothermophilus (Geobacillus stearothermophilus)

Taxonomic identifier

1422 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

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. Makes several contacts with the 16S rRNA in the 70S ribosome By similarity.
Subunit structure	Part of the 50S ribosomal subunit. Forms a bridge to the 30S subunit in the 70S ribosome By similarity.
Sequence similarities	Belongs to the ribosomal protein L2P family.

Ontologies

Keywords
Ligand	RNA-binding rRNA-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	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.3

Chain

2 – 276

275

50S ribosomal protein L2 HAMAP MF_01320

PRO_0000129528

Experimental info

Sequence conflict

40

1

R → K in BAA31210. Ref.1

Sequence conflict

106

1

A → R in BAA31210. Ref.1

Sequence conflict

163

1

Q → L in BAA31210. Ref.1

Secondary structure

1

.

.

.

.

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.

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.

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276

Helix Strand Turn

Details...

Beta strand

76 – 84

9

Helix

85 – 87

3

Beta strand

89 – 96

8

Beta strand

101 – 105

5

Beta strand

129 – 131

3

Helix

132 – 134

3

Beta strand

140 – 147

8

Beta strand

152 – 159

8

Beta strand

162 – 168

7

Beta strand

171 – 175

5

Beta strand

181 – 185

5

Beta strand

188 – 193

6

Sequences

	Sequence		Length	Mass (Da)
	P04257-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 871DBC74317C3AAD	FASTA	276	30,331
	10 20 30 40 50 60 MAIKKYKPTS NGRRGMTVLD FSEITTDQPE KSLLAPLKKR AGRNNQGKIT VRHQGGGHKR 70 80 90 100 110 120 QYRIIDFKRD KDGIPGRVAT IEYDPNRSAN IALINYADGE KRYIIAPKNL KVGMEIMSGP 130 140 150 160 170 180 DADIKIGNAL PLENIPVGTL VHNIELKPGR GGQLVRAAGT SAQVLGKEGK YVIVRLASGE 190 200 210 220 230 240 VRMILGKCRA TVGEVGNEQH ELVNIGKAGR ARWLGIRPTV RGSVMNPVDH PHGGGEGKAP 250 260 270 IGRKSPMTPW GKPTLGYKTR KKKNKSDKFI IRRRKK

References

[1]	"Nucleotide sequence of the genes encoding the ribosomal proteins L23 and L2 from the Bacillus stearothermophilus ribosome." Kimura M. Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Nucleotide sequences of Bacillus stearothermophilus ribosomal protein genes: part of the ribosomal S10 operon." Kroemer W.J., Hatakeyama T., Kimura M. Biol. Chem. Hoppe-Seyler 371:631-636(1990) [PubMed: 2222862] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 81-276. Strain: ATCC 29609 / DSM 2027 / NCA 1503 / NCIB 8924.
[3]	"The primary structure of ribosomal protein L2 from Bacillus stearothermophilus." Kimura M., Kimura J., Watanabe K. Eur. J. Biochem. 153:289-297(1985) [PubMed: 3908098] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-276.
[4]	"Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by cross-linking studies." Urlaub H., Kruft V., Bischof O., Mueller E.-C., Wittmann-Liebold B. EMBO J. 14:4578-4588(1995) [PubMed: 7556101] [Abstract] Cited for: PROTEIN SEQUENCE OF 239-247, CROSS-LINKING TO RRNA. Strain: 799.
[5]	"The three-dimensional structure of the RNA-binding domain of ribosomal protein L2; a protein at the peptidyl transferase center of the ribosome." Nakagawa A., Nakashima T., Taniguchi M., Hosaka H., Kimura M., Tanaka I. EMBO J. 18:1459-1467(1999) [PubMed: 10075918] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 61-202.
[6]	"Placement of protein and RNA structures into a 5 A-resolution map of the 50S ribosomal subunit." Ban N., Nissen P., Hansen J., Capel M., Moore P.B., Steitz T.A. Nature 400:841-847(1999) [PubMed: 10476961] [Abstract] Cited for: 3D-STRUCTURE MODELING OF 62-197 ONTO THE H.MARISMORTUI 50S RIBOSOME.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AB015722 Genomic DNA. Translation: BAA31210.1.
X54994 Genomic DNA. Translation: CAA38737.1.

PIR

R5BS2F. A02759.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1RL2	X-ray	2.30	A/B	61-197	[»]

ModBase

Search...

Family and domain databases

HAMAP

MF_01320.
[Tree]

InterPro

IPR012340. NA-bd_OB-fold.
IPR002171. Ribosomal_L2.
IPR005880. Ribosomal_L2_bac-type.
IPR014722. Transl_SH3-like_sub.
[Graphical view]

Gene3D

G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
G3DSA:2.30.30.30. Ribosomal_L2. 1 hit.

PANTHER

PTHR13691:SF5. Ribosom_L2_bac. 1 hit.
PTHR13691. Ribosomal_L2. 1 hit.

Pfam

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

PIRSF

PIRSF002158. Ribosomal_L2. 1 hit.

TIGRFAMs

TIGR01171. rplB_bact. 1 hit.

PROSITE

PS00467. RIBOSOMAL_L2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

RL2_BACST

Accession

Primary (citable) accession number: P04257
Secondary accession number(s): O82995

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 1987
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 81 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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