P20276 (RL2_HALMA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
50S ribosomal protein L2

Alternative name(s):
Hl4
Hmal2

Gene names

Name:	rpl2
Ordered Locus Names:	rrnAC1608

Organism

Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui) [Complete proteome] [HAMAP]

Taxonomic identifier

272569 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Euryarchaeota › Halobacteria › Halobacteriales › Halobacteriaceae › Haloarcula › Haloarcula marismortui

Protein attributes

Sequence length	240 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. HAMAP-Rule MF_01320_A
Subunit structure	Part of the 50S ribosomal subunit. Forms a bridge to the 30S subunit in the 70S ribosome By similarity. Interacts weakly with protein L37Ae. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12
Miscellaneous	This protein can be partially incorporated into E.coli polysomes in vivo, indicating it can replace the endogenous protein. HAMAP-Rule MF_01320_A
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 Complete proteome 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
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed HAMAP-Rule MF_01320_A

Chain

2 – 240

239

50S ribosomal protein L2 HAMAP-Rule MF_01320_A

PRO_0000129712

Experimental info

Mutagenesis

200

1

H → A or G: No incorporation into translating E.coli polysomes; ribosomes assemble normally. Significantly reduced translational activity.

Sequence conflict

86

1

S → D in AAA86862. Ref.1

Sequence conflict

161

1

A → G in AAA86862. Ref.1

Secondary structure

1

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240

Helix Strand Turn

Details...

Helix

6 – 10

5

Helix

15 – 17

3

Helix

21 – 23

3

Beta strand

35 – 37

3

Beta strand

40 – 48

9

Turn

50 – 52

3

Beta strand

53 – 61

9

Turn

62 – 64

3

Beta strand

66 – 69

4

Beta strand

72 – 74

3

Beta strand

76 – 78

3

Beta strand

80 – 84

5

Beta strand

94 – 96

3

Helix

97 – 99

3

Beta strand

105 – 109

5

Beta strand

127 – 131

5

Beta strand

137 – 140

4

Turn

142 – 144

3

Beta strand

146 – 149

4

Beta strand

154 – 158

5

Turn

161 – 167

7

Helix

173 – 180

8

Turn

181 – 184

4

Helix

192 – 194

3

Helix

197 – 199

3

Beta strand

205 – 207

3

Beta strand

214 – 216

3

Turn

222 – 224

3

Beta strand

227 – 229

3

Sequences

	Sequence		Length	Mass (Da)
	P20276 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 986CA69D432C7F74	FASTA	240	25,309
	10 20 30 40 50 60 MGRRIQGQRR GRGTSTFRAP SHRYKADLEH RKVEDGDVIA GTVVDIEHDP ARSAPVAAVE 70 80 90 100 110 120 FEDGDRRLIL APEGVGVGDE LQVGVSAEIA PGNTLPLAEI PEGVPVCNVE SSPGDGGKFA 130 140 150 160 170 180 RASGVNAQLL THDRNVAVVK LPSGEMKRLD PQCRATIGVV AGGGRTDKPF VKAGNKHHKM 190 200 210 220 230 240 KARGTKWPNV RGVAMNAVDH PFGGGGRQHP GKPKSISRNA PPGRKVGDIA SKRTGRGGNE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Organization and nucleotide sequence of a gene cluster coding for eight ribosomal proteins in the archaebacterium Halobacterium marismortui." Arndt E., Kroemer W., Hatakeyama T. J. Biol. Chem. 265:3034-3039(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[2]	"Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea." Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W., Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E., Hood L., Ng W.V. Genome Res. 14:2221-2234(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[3]	"Functional implications of ribosomal protein L2 in protein biosynthesis as shown by in vivo replacement studies." Uehlein M., Wegloehner W., Urlaub H., Wittmann-Liebold B. Biochem. J. 331:423-430(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN REPLACEMENT STUDIES IN E.COLI, MUTAGENESIS.
[4]	"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] [Europe PMC] [Abstract] Cited for: 3D-STRUCTURE MODELING.
[5]	"The complete atomic structure of the large ribosomal subunit at 2.4 A resolution." Ban N., Nissen P., Hansen J., Moore P.B., Steitz T.A. Science 289:905-920(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT. Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[6]	"The structural basis of ribosome activity in peptide bond synthesis." Nissen P., Hansen J., Ban N., Moore P.B., Steitz T.A. Science 289:920-930(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT. Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[7]	"A pre-translocational intermediate in protein synthesis observed in crystals of enzymatically active 50S subunits." Schmeing T.M., Seila A.C., Hansen J.L., Freeborn B., Soukup J.K., Scaringe S.A., Strobel S.A., Moore P.B., Steitz T.A. Nat. Struct. Biol. 9:225-230(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF THE 50S SUBUNIT. Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[8]	"The kink-turn: a new RNA secondary structure motif." Klein D.J., Schmeing T.M., Moore P.B., Steitz T.A. EMBO J. 20:4214-4221(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT. Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[9]	"The structures of four macrolide antibiotics bound to the large ribosomal subunit." Hansen J.L., Ippolito J.A., Ban N., Nissen P., Moore P.B., Steitz T.A. Mol. Cell 10:117-128(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH FOUR MACROLIDE ANTIBIOTICS. Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[10]	"Structural insights into peptide bond formation." Hansen J.L., Schmeing T.M., Moore P.B., Steitz T.A. Proc. Natl. Acad. Sci. U.S.A. 99:11670-11675(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE 50S SUBUNIT. Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[11]	"Structures of five antibiotics bound at the peptidyl transferase center of the large ribosomal subunit." Hansen J.L., Moore P.B., Steitz T.A. J. Mol. Biol. 330:1061-1075(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH FIVE ANTIBIOTICS AT THE PEPTIDYL TRANSFERASE CENTER. Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[12]	"Structures of deacylated tRNA mimics bound to the E site of the large ribosomal subunit." Schmeing T.M., Moore P.B., Steitz T.A. RNA 9:1345-1352(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF THE 50S SUBUNIT WITH TWO DIFFERENT E SITE SUBSTRATES.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J05222 Genomic DNA. Translation: AAA86862.1.
AY596297 Genomic DNA. Translation: AAV46525.1.

PIR

R5HS2L. F35063.

RefSeq

YP_136231.1. NC_006396.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1C04	X-ray	5.00	A	46-145	[»]
1FFK	X-ray	2.40	A	2-240	[»]
1JJ2	X-ray	2.40	A	2-240	[»]
1K73	X-ray	3.01	C	2-240	[»]
1K8A	X-ray	3.00	C	2-240	[»]
1K9M	X-ray	3.00	C	2-240	[»]
1KC8	X-ray	3.01	C	2-240	[»]
1KD1	X-ray	3.00	C	2-240	[»]
1KQS	X-ray	3.10	A	2-240	[»]
1M1K	X-ray	3.20	C	2-240	[»]
1M90	X-ray	2.80	C	2-240	[»]
1N8R	X-ray	3.00	C	2-240	[»]
1NJI	X-ray	3.00	C	2-240	[»]
1Q7Y	X-ray	3.20	C	2-240	[»]
1Q81	X-ray	2.95	C	2-240	[»]
1Q82	X-ray	2.98	C	2-240	[»]
1Q86	X-ray	3.00	C	2-240	[»]
1QVF	X-ray	3.10	A	2-240	[»]
1QVG	X-ray	2.90	A	2-240	[»]
1S72	X-ray	2.40	A	1-240	[»]
1VQ4	X-ray	2.70	A	1-240	[»]
1VQ5	X-ray	2.60	A	1-240	[»]
1VQ6	X-ray	2.70	A	1-240	[»]
1VQ7	X-ray	2.50	A	1-240	[»]
1VQ8	X-ray	2.20	A	1-240	[»]
1VQ9	X-ray	2.40	A	1-240	[»]
1VQK	X-ray	2.30	A	1-240	[»]
1VQL	X-ray	2.30	A	1-240	[»]
1VQM	X-ray	2.30	A	1-240	[»]
1VQN	X-ray	2.40	A	1-240	[»]
1VQO	X-ray	2.20	A	1-240	[»]
1VQP	X-ray	2.25	A	1-240	[»]
1W2B	X-ray	3.50	A	2-239	[»]
1YHQ	X-ray	2.40	A	1-240	[»]
1YI2	X-ray	2.65	A	1-240	[»]
1YIJ	X-ray	2.60	A	1-240	[»]
1YIT	X-ray	2.80	A	1-240	[»]
1YJ9	X-ray	2.90	A	1-240	[»]
1YJN	X-ray	3.00	A	1-240	[»]
1YJW	X-ray	2.90	A	1-240	[»]
2OTJ	X-ray	2.90	A	1-240	[»]
2OTL	X-ray	2.70	A	2-240	[»]
2QA4	X-ray	3.00	A	1-240	[»]
2QEX	X-ray	2.90	A	1-240	[»]
3CC2	X-ray	2.40	A	1-240	[»]
3CC4	X-ray	2.70	A	1-240	[»]
3CC7	X-ray	2.70	A	1-240	[»]
3CCE	X-ray	2.75	A	1-240	[»]
3CCJ	X-ray	2.70	A	1-240	[»]
3CCL	X-ray	2.90	A	1-240	[»]
3CCM	X-ray	2.55	A	1-240	[»]
3CCQ	X-ray	2.90	A	1-240	[»]
3CCR	X-ray	3.00	A	1-240	[»]
3CCS	X-ray	2.95	A	1-240	[»]
3CCU	X-ray	2.80	A	1-240	[»]
3CCV	X-ray	2.90	A	1-240	[»]
3CD6	X-ray	2.75	A	1-240	[»]
3CMA	X-ray	2.80	A	1-240	[»]
3CME	X-ray	2.95	A	1-240	[»]
3CPW	X-ray	2.70	A	1-240	[»]
3CXC	X-ray	3.00	A	2-239	[»]
3G4S	X-ray	3.20	A	2-238	[»]
3G6E	X-ray	2.70	A	2-238	[»]
3G71	X-ray	2.85	A	2-238	[»]
3I55	X-ray	3.11	A	1-240	[»]
3I56	X-ray	2.90	A	1-240	[»]
3OW2	X-ray	2.70	A	2-238	[»]

ProteinModelPortal

P20276.

SMR

P20276. Positions 14-238.

ModBase

Search...

Protein-protein interaction databases

STRING

272569.rrnAC1608.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAV46525; AAV46525; rrnAC1608.

GeneID

3128427.

KEGG

hma:rrnAC1608.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

COG0090.

HOGENOM

HOG000232983.

KO

K02886.

OMA

GRVIRNQ.

ProtClustDB

PRK09612.

Enzyme and pathway databases

BioCyc

HMAR272569:GJDH-1464-MONOMER.

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_A. Ribosomal_L2_A.

InterPro

IPR012340. NA-bd_OB-fold.
IPR022666. Rbsml_prot_L2_RNA-bd_dom.
IPR014722. Rib_L2_dom2.
IPR002171. Ribosomal_L2.
IPR023672. Ribosomal_L2_arc.
IPR022669. Ribosomal_L2_C.
IPR022671. Ribosomal_L2_CS.
IPR014726. Ribosomal_L2_dom3.
IPR008991. Translation_prot_SH3-like.
[Graphical view]

PANTHER

PTHR13691. PTHR13691. 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.

PROSITE

PS00467. RIBOSOMAL_L2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P20276.

Entry information

Entry name

RL2_HALMA

Accession

Primary (citable) accession number: P20276
Secondary accession number(s): Q5V1S7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 110 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program