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Protein

50S ribosomal protein L2

Gene

rpl2

Organism
Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L2
Alternative name(s):
Hl4
Hmal2
Gene namesi
Name:rpl2
Ordered Locus Names:rrnAC1608
OrganismiHaloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui)
Taxonomic identifieri272569 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloarcula
Proteomesi
  • UP000001169 Componenti: Chromosome I

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi200H → A or G: No incorporation into translating E.coli polysomes; ribosomes assemble normally. Significantly reduced translational activity. 1 Publication1

Chemistry databases

DrugBankiDB04865. Homoharringtonine.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00001297122 – 24050S ribosomal protein L2Add BLAST239

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Forms a bridge to the 30S subunit in the 70S ribosome (By similarity). Interacts weakly with protein L37Ae.By similarity2 Publications

Protein-protein interaction databases

STRINGi272569.rrnAC1608.

Structurei

Secondary structure

1240
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 10Combined sources5
Helixi15 – 17Combined sources3
Helixi21 – 23Combined sources3
Beta strandi35 – 37Combined sources3
Beta strandi40 – 48Combined sources9
Turni50 – 52Combined sources3
Beta strandi53 – 61Combined sources9
Turni62 – 64Combined sources3
Beta strandi66 – 69Combined sources4
Beta strandi72 – 74Combined sources3
Beta strandi76 – 78Combined sources3
Beta strandi80 – 84Combined sources5
Beta strandi94 – 96Combined sources3
Helixi97 – 99Combined sources3
Beta strandi105 – 109Combined sources5
Beta strandi127 – 131Combined sources5
Beta strandi137 – 140Combined sources4
Turni142 – 144Combined sources3
Beta strandi146 – 149Combined sources4
Beta strandi154 – 158Combined sources5
Turni161 – 167Combined sources7
Helixi173 – 180Combined sources8
Turni181 – 184Combined sources4
Helixi192 – 194Combined sources3
Helixi197 – 199Combined sources3
Beta strandi205 – 207Combined sources3
Beta strandi214 – 216Combined sources3
Turni222 – 224Combined sources3
Beta strandi227 – 229Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4V9FX-ray2.40A1-240[»]
ProteinModelPortaliP20276.
SMRiP20276.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20276.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L2P family.Curated

Phylogenomic databases

eggNOGiarCOG04067. Archaea.
COG0090. LUCA.
HOGENOMiHOG000232983.
KOiK02886.
OMAiCMNVIDH.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
4.10.950.10. 1 hit.
HAMAPiMF_01320_A. Ribosomal_L2_A. 1 hit.
InterProiIPR012340. 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]
PANTHERiPTHR13691. PTHR13691. 1 hit.
PfamiPF00181. Ribosomal_L2. 1 hit.
PF03947. Ribosomal_L2_C. 1 hit.
[Graphical view]
PIRSFiPIRSF002158. Ribosomal_L2. 1 hit.
SMARTiSM01383. Ribosomal_L2. 1 hit.
SM01382. Ribosomal_L2_C. 1 hit.
[Graphical view]
SUPFAMiSSF50104. SSF50104. 1 hit.
SSF50249. SSF50249. 1 hit.
PROSITEiPS00467. RIBOSOMAL_L2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P20276-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRRIQGQRR GRGTSTFRAP SHRYKADLEH RKVEDGDVIA GTVVDIEHDP
60 70 80 90 100
ARSAPVAAVE FEDGDRRLIL APEGVGVGDE LQVGVSAEIA PGNTLPLAEI
110 120 130 140 150
PEGVPVCNVE SSPGDGGKFA RASGVNAQLL THDRNVAVVK LPSGEMKRLD
160 170 180 190 200
PQCRATIGVV AGGGRTDKPF VKAGNKHHKM KARGTKWPNV RGVAMNAVDH
210 220 230 240
PFGGGGRQHP GKPKSISRNA PPGRKVGDIA SKRTGRGGNE
Length:240
Mass (Da):25,309
Last modified:January 23, 2007 - v4
Checksum:i986CA69D432C7F74
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti86S → D in AAA86862 (PubMed:2406244).Curated1
Sequence conflicti161A → G in AAA86862 (PubMed:2406244).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05222 Genomic DNA. Translation: AAA86862.1.
AY596297 Genomic DNA. Translation: AAV46525.1.
PIRiF35063. R5HS2L.
RefSeqiWP_004957415.1. NC_006396.1.

Genome annotation databases

EnsemblBacteriaiAAV46525; AAV46525; rrnAC1608.
GeneIDi3128427.
KEGGihma:rrnAC1608.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05222 Genomic DNA. Translation: AAA86862.1.
AY596297 Genomic DNA. Translation: AAV46525.1.
PIRiF35063. R5HS2L.
RefSeqiWP_004957415.1. NC_006396.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4V9FX-ray2.40A1-240[»]
ProteinModelPortaliP20276.
SMRiP20276.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272569.rrnAC1608.

Chemistry databases

DrugBankiDB04865. Homoharringtonine.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAV46525; AAV46525; rrnAC1608.
GeneIDi3128427.
KEGGihma:rrnAC1608.

Phylogenomic databases

eggNOGiarCOG04067. Archaea.
COG0090. LUCA.
HOGENOMiHOG000232983.
KOiK02886.
OMAiCMNVIDH.

Miscellaneous databases

EvolutionaryTraceiP20276.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
4.10.950.10. 1 hit.
HAMAPiMF_01320_A. Ribosomal_L2_A. 1 hit.
InterProiIPR012340. 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]
PANTHERiPTHR13691. PTHR13691. 1 hit.
PfamiPF00181. Ribosomal_L2. 1 hit.
PF03947. Ribosomal_L2_C. 1 hit.
[Graphical view]
PIRSFiPIRSF002158. Ribosomal_L2. 1 hit.
SMARTiSM01383. Ribosomal_L2. 1 hit.
SM01382. Ribosomal_L2_C. 1 hit.
[Graphical view]
SUPFAMiSSF50104. SSF50104. 1 hit.
SSF50249. SSF50249. 1 hit.
PROSITEiPS00467. RIBOSOMAL_L2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRL2_HALMA
AccessioniPrimary (citable) accession number: P20276
Secondary accession number(s): Q5V1S7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 132 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Ribosomal proteins
    Ribosomal proteins families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.