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P20276

- RL2_HALMA

UniProt

P20276 - RL2_HALMA

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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: 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

  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. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 24023950S ribosomal protein L2PRO_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.By similarity2 Publications

Protein-protein interaction databases

STRINGi272569.rrnAC1608.

Structurei

Secondary structure

1
240
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 105Combined sources
Helixi15 – 173Combined sources
Helixi21 – 233Combined sources
Beta strandi35 – 373Combined sources
Beta strandi40 – 489Combined sources
Turni50 – 523Combined sources
Beta strandi53 – 619Combined sources
Turni62 – 643Combined sources
Beta strandi66 – 694Combined sources
Beta strandi72 – 743Combined sources
Beta strandi76 – 783Combined sources
Beta strandi80 – 845Combined sources
Beta strandi94 – 963Combined sources
Helixi97 – 993Combined sources
Beta strandi105 – 1095Combined sources
Beta strandi127 – 1315Combined sources
Beta strandi137 – 1404Combined sources
Turni142 – 1443Combined sources
Beta strandi146 – 1494Combined sources
Beta strandi154 – 1585Combined sources
Turni161 – 1677Combined sources
Helixi173 – 1808Combined sources
Turni181 – 1844Combined sources
Helixi192 – 1943Combined sources
Helixi197 – 1993Combined sources
Beta strandi205 – 2073Combined sources
Beta strandi214 – 2163Combined sources
Turni222 – 2243Combined sources
Beta strandi227 – 2293Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20276.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L2P family.Curated

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

        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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti86 – 861S → D in AAA86862. (PubMed:2406244)Curated
Sequence conflicti161 – 1611A → G in AAA86862. (PubMed:2406244)Curated

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.
RefSeqiYP_136231.1. 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 .
PIRi F35063. R5HS2L.
RefSeqi YP_136231.1. NC_006396.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

Chemistry

DrugBanki DB04865. Homoharringtonine.

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: November 26, 2014
This is version 118 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

External Data

Dasty 3