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P20276 (RL2_HALMA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
50S ribosomal protein L2
Alternative name(s):
Hl4
Hmal2
Gene names
Name:rpl2
Ordered Locus Names:rrnAC1608
OrganismHaloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui) [Complete proteome] [HAMAP]
Taxonomic identifier272569 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloarcula

Protein attributes

Sequence length240 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 Ref.13

Miscellaneous

This protein can be partially incorporated into E.coli polysomes in vivo, indicating it can replace the endogenous protein.

Sequence similarities

Belongs to the ribosomal protein L2P family.

Ontologies

Keywords
   LigandRNA-binding
rRNA-binding
   Molecular functionRibonucleoprotein
Ribosomal protein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological_processtranslation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentlarge ribosomal subunit

Inferred from electronic annotation. Source: InterPro

   Molecular_functionrRNA binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

structural constituent of ribosome

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed HAMAP-Rule MF_01320_A
Chain2 – 24023950S ribosomal protein L2 HAMAP-Rule MF_01320_A
PRO_0000129712

Experimental info

Mutagenesis2001H → A or G: No incorporation into translating E.coli polysomes; ribosomes assemble normally. Significantly reduced translational activity.
Sequence conflict861S → D in AAA86862. Ref.1
Sequence conflict1611A → G in AAA86862. Ref.1

Secondary structure

....................................................... 240
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P20276 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 986CA69D432C7F74

FASTA24025,309
        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 

« Hide

References

« Hide '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.
[13]"Revisiting the Haloarcula marismortui 50S ribosomal subunit model."
Gabdulkhakov A., Nikonov S., Garber M.
Acta Crystallogr. D 69:997-1004(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J05222 Genomic DNA. Translation: AAA86862.1.
AY596297 Genomic DNA. Translation: AAV46525.1.
PIRR5HS2L. F35063.
RefSeqYP_136231.1. NC_006396.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1C04X-ray5.00A46-145[»]
1FFKX-ray2.40A2-240[»]
1JJ2X-ray2.40A2-240[»]
1K73X-ray3.01C2-240[»]
1K8AX-ray3.00C2-240[»]
1K9MX-ray3.00C2-240[»]
1KC8X-ray3.01C2-240[»]
1KD1X-ray3.00C2-240[»]
1KQSX-ray3.10A2-240[»]
1M1KX-ray3.20C2-240[»]
1M90X-ray2.80C2-240[»]
1N8RX-ray3.00C2-240[»]
1NJIX-ray3.00C2-240[»]
1Q7YX-ray3.20C2-240[»]
1Q81X-ray2.95C2-240[»]
1Q82X-ray2.98C2-240[»]
1Q86X-ray3.00C2-240[»]
1QVFX-ray3.10A2-240[»]
1QVGX-ray2.90A2-240[»]
1S72X-ray2.40A1-240[»]
1VQ4X-ray2.70A1-240[»]
1VQ5X-ray2.60A1-240[»]
1VQ6X-ray2.70A1-240[»]
1VQ7X-ray2.50A1-240[»]
1VQ8X-ray2.20A1-240[»]
1VQ9X-ray2.40A1-240[»]
1VQKX-ray2.30A1-240[»]
1VQLX-ray2.30A1-240[»]
1VQMX-ray2.30A1-240[»]
1VQNX-ray2.40A1-240[»]
1VQOX-ray2.20A1-240[»]
1VQPX-ray2.25A1-240[»]
1W2BX-ray3.50A2-240[»]
1YHQX-ray2.40A1-240[»]
1YI2X-ray2.65A1-240[»]
1YIJX-ray2.60A1-240[»]
1YITX-ray2.80A1-240[»]
1YJ9X-ray2.90A1-240[»]
1YJNX-ray3.00A1-240[»]
1YJWX-ray2.90A1-240[»]
2OTJX-ray2.90A1-240[»]
2OTLX-ray2.70A2-240[»]
2QA4X-ray3.00A1-240[»]
2QEXX-ray2.90A1-240[»]
3CC2X-ray2.40A1-240[»]
3CC4X-ray2.70A1-240[»]
3CC7X-ray2.70A1-240[»]
3CCEX-ray2.75A1-240[»]
3CCJX-ray2.70A1-240[»]
3CCLX-ray2.90A1-240[»]
3CCMX-ray2.55A1-240[»]
3CCQX-ray2.90A1-240[»]
3CCRX-ray3.00A1-240[»]
3CCSX-ray2.95A1-240[»]
3CCUX-ray2.80A1-240[»]
3CCVX-ray2.90A1-240[»]
3CD6X-ray2.75A1-240[»]
3CMAX-ray2.80A1-240[»]
3CMEX-ray2.95A1-240[»]
3CPWX-ray2.70A1-240[»]
3CXCX-ray3.00A2-240[»]
3G4SX-ray3.20A2-238[»]
3G6EX-ray2.70A2-238[»]
3G71X-ray2.85A2-238[»]
3I55X-ray3.11A1-240[»]
3I56X-ray2.90A1-240[»]
3OW2X-ray2.70A2-238[»]
4ADXelectron microscopy6.60A1-240[»]
4HUBX-ray2.40A1-240[»]
ProteinModelPortalP20276.
SMRP20276. Positions 14-238.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272569.rrnAC1608.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV46525; AAV46525; rrnAC1608.
GeneID3128427.
KEGGhma:rrnAC1608.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0090.
HOGENOMHOG000232983.
KOK02886.
OMANCTISPL.

Enzyme and pathway databases

BioCycHMAR272569:GJDH-1464-MONOMER.

Family and domain databases

Gene3D2.30.30.30. 1 hit.
2.40.50.140. 1 hit.
4.10.950.10. 1 hit.
HAMAPMF_01320_A. Ribosomal_L2_A.
InterProIPR012340. 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]
PANTHERPTHR13691. PTHR13691. 1 hit.
PfamPF00181. Ribosomal_L2. 1 hit.
PF03947. Ribosomal_L2_C. 1 hit.
[Graphical view]
PIRSFPIRSF002158. Ribosomal_L2. 1 hit.
SUPFAMSSF50104. SSF50104. 1 hit.
SSF50249. SSF50249. 1 hit.
PROSITEPS00467. RIBOSOMAL_L2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP20276.

Entry information

Entry nameRL2_HALMA
AccessionPrimary (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: July 9, 2014
This is version 115 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references