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P20276

- RL2_HALMA

UniProt

P20276 - RL2_HALMA

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Protein
50S ribosomal protein L2
Gene
rpl2, rrnAC1608
Organism
Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui)
Status
Reviewed - 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.UniRule annotation

GO - Molecular functioni

  1. rRNA binding Source: UniProtKB-HAMAP
  2. structural constituent of ribosome Source: InterPro

GO - Biological processi

  1. translation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciHMAR272569:GJDH-1464-MONOMER.

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
ProteomesiUP000001169: Chromosome I

Subcellular locationi

GO - Cellular componenti

  1. large ribosomal subunit Source: InterPro
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi200 – 2001H → A or G: No incorporation into translating E.coli polysomes; ribosomes assemble normally. Significantly reduced translational activity.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedUniRule annotation
Chaini2 – 24023950S ribosomal protein L2UniRule annotation
PRO_0000129712Add
BLAST

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.9 Publications

Protein-protein interaction databases

STRINGi272569.rrnAC1608.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 105
Helixi15 – 173
Helixi21 – 233
Beta strandi35 – 373
Beta strandi40 – 489
Turni50 – 523
Beta strandi53 – 619
Turni62 – 643
Beta strandi66 – 694
Beta strandi72 – 743
Beta strandi76 – 783
Beta strandi80 – 845
Beta strandi94 – 963
Helixi97 – 993
Beta strandi105 – 1095
Beta strandi127 – 1315
Beta strandi137 – 1404
Turni142 – 1443
Beta strandi146 – 1494
Beta strandi154 – 1585
Turni161 – 1677
Helixi173 – 1808
Turni181 – 1844
Helixi192 – 1943
Helixi197 – 1993
Beta strandi205 – 2073
Beta strandi214 – 2163
Turni222 – 2243
Beta strandi227 – 2293

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP20276.
SMRiP20276. Positions 14-238.

Miscellaneous databases

EvolutionaryTraceiP20276.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0090.
HOGENOMiHOG000232983.
KOiK02886.
OMAiNCTISPL.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
2.40.50.140. 1 hit.
4.10.950.10. 1 hit.
HAMAPiMF_01320_A. Ribosomal_L2_A.
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.
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

MGRRIQGQRR GRGTSTFRAP SHRYKADLEH RKVEDGDVIA GTVVDIEHDP    50
ARSAPVAAVE FEDGDRRLIL APEGVGVGDE LQVGVSAEIA PGNTLPLAEI 100
PEGVPVCNVE SSPGDGGKFA RASGVNAQLL THDRNVAVVK LPSGEMKRLD 150
PQCRATIGVV AGGGRTDKPF VKAGNKHHKM KARGTKWPNV RGVAMNAVDH 200
PFGGGGRQHP GKPKSISRNA PPGRKVGDIA SKRTGRGGNE 240
Length:240
Mass (Da):25,309
Last modified:January 23, 2007 - v4
Checksum:i986CA69D432C7F74
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti86 – 861S → D in AAA86862. 1 Publication
Sequence conflicti161 – 1611A → G in AAA86862. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05222 Genomic DNA. Translation: AAA86862.1.
AY596297 Genomic DNA. Translation: AAV46525.1.
PIRiF35063. R5HS2L.
RefSeqiYP_136231.1. NC_006396.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05222 Genomic DNA. Translation: AAA86862.1 .
AY596297 Genomic DNA. Translation: AAV46525.1 .
PIRi F35063. R5HS2L.
RefSeqi YP_136231.1. NC_006396.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 2-240 [» ]
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 2-240 [» ]
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 [» ]
4ADX electron microscopy 6.60 A 1-240 [» ]
4HUB X-ray 2.40 A 1-240 [» ]
ProteinModelPortali P20276.
SMRi P20276. Positions 14-238.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 272569.rrnAC1608.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAV46525 ; AAV46525 ; rrnAC1608 .
GeneIDi 3128427.
KEGGi hma:rrnAC1608.

Phylogenomic databases

eggNOGi COG0090.
HOGENOMi HOG000232983.
KOi K02886.
OMAi NCTISPL.

Enzyme and pathway databases

BioCyci HMAR272569:GJDH-1464-MONOMER.

Miscellaneous databases

EvolutionaryTracei P20276.

Family and domain databases

Gene3Di 2.30.30.30. 1 hit.
2.40.50.140. 1 hit.
4.10.950.10. 1 hit.
HAMAPi MF_01320_A. Ribosomal_L2_A.
InterProi 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 ]
PANTHERi PTHR13691. PTHR13691. 1 hit.
Pfami PF00181. Ribosomal_L2. 1 hit.
PF03947. Ribosomal_L2_C. 1 hit.
[Graphical view ]
PIRSFi PIRSF002158. Ribosomal_L2. 1 hit.
SUPFAMi SSF50104. SSF50104. 1 hit.
SSF50249. SSF50249. 1 hit.
PROSITEi PS00467. RIBOSOMAL_L2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

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: July 9, 2014
This is version 115 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

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

External Data

Dasty 3

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