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P10970

- RL22_HALMA

UniProt

P10970 - RL22_HALMA

Protein

50S ribosomal protein L22

Gene

rpl22

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
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    This protein binds specifically to 23S rRNA. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.UniRule annotation
    Contacts all 6 domains of the 23S rRNA, helping stabilize their relative orientation. An extended beta-hairpin in the C-terminus forms part of the polypeptide exit tunnel, in which it helps forms a bend with protein L4, while most of the rest of the protein is located at the polypeptide exit tunnel on the outside of the subunit.

    GO - Molecular functioni

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

    GO - Biological processi

    1. translation Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Keywords - Ligandi

    RNA-binding, rRNA-binding

    Enzyme and pathway databases

    BioCyciHMAR272569:GJDH-1462-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    50S ribosomal protein L22UniRule annotation
    Alternative name(s):
    Hl23
    Hmal22
    Gene namesi
    Name:rpl22UniRule annotation
    Ordered Locus Names:rrnAC1606
    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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 15515450S ribosomal protein L22PRO_0000125272Add
    BLAST

    Interactioni

    Subunit structurei

    Part of the 50S ribosomal subunit. Contacts the macrolide antibiotic tylosin in the polypeptide exit tunnel.2 PublicationsUniRule annotation

    Protein-protein interaction databases

    STRINGi272569.rrnAC1606.

    Structurei

    Secondary structure

    1
    155
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi11 – 133
    Beta strandi14 – 229
    Helixi26 – 3611
    Helixi41 – 5212
    Beta strandi61 – 633
    Beta strandi74 – 807
    Helixi83 – 10220
    Helixi107 – 1093
    Beta strandi110 – 12314
    Beta strandi126 – 1283
    Helixi130 – 1323
    Beta strandi134 – 1363
    Beta strandi139 – 14911

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FFKX-ray2.40O2-155[»]
    1JJ2X-ray2.40Q2-155[»]
    1K73X-ray3.01S2-155[»]
    1K8AX-ray3.00S2-155[»]
    1K9MX-ray3.00S2-155[»]
    1KC8X-ray3.01S2-155[»]
    1KD1X-ray3.00S2-155[»]
    1KQSX-ray3.10Q2-155[»]
    1M1KX-ray3.20S2-155[»]
    1M90X-ray2.80S2-155[»]
    1N8RX-ray3.00S2-155[»]
    1NJIX-ray3.00S2-155[»]
    1Q7YX-ray3.20S2-155[»]
    1Q81X-ray2.95S2-155[»]
    1Q82X-ray2.98S2-155[»]
    1Q86X-ray3.00S2-155[»]
    1QVFX-ray3.10Q2-155[»]
    1QVGX-ray2.90Q2-155[»]
    1S72X-ray2.40R1-155[»]
    1VQ4X-ray2.70R1-155[»]
    1VQ5X-ray2.60R1-155[»]
    1VQ6X-ray2.70R1-155[»]
    1VQ7X-ray2.50R1-155[»]
    1VQ8X-ray2.20R1-155[»]
    1VQ9X-ray2.40R1-155[»]
    1VQKX-ray2.30R1-155[»]
    1VQLX-ray2.30R1-155[»]
    1VQMX-ray2.30R1-155[»]
    1VQNX-ray2.40R1-155[»]
    1VQOX-ray2.20R1-155[»]
    1VQPX-ray2.25R1-155[»]
    1W2BX-ray3.50Q2-155[»]
    1YHQX-ray2.40R1-155[»]
    1YI2X-ray2.65R1-155[»]
    1YIJX-ray2.60R1-155[»]
    1YITX-ray2.80R1-155[»]
    1YJ9X-ray2.80R1-152[»]
    1YJNX-ray3.00R1-155[»]
    1YJWX-ray2.90R1-155[»]
    2OTJX-ray2.90R1-155[»]
    2OTLX-ray2.70R1-155[»]
    2QA4X-ray3.00R1-155[»]
    2QEXX-ray2.90R1-155[»]
    3CC2X-ray2.40R1-155[»]
    3CC4X-ray2.70R1-155[»]
    3CC7X-ray2.70R1-155[»]
    3CCEX-ray2.75R1-155[»]
    3CCJX-ray2.70R1-155[»]
    3CCLX-ray2.90R1-155[»]
    3CCMX-ray2.55R1-155[»]
    3CCQX-ray2.90R1-155[»]
    3CCRX-ray3.00R1-155[»]
    3CCSX-ray2.95R1-155[»]
    3CCUX-ray2.80R1-155[»]
    3CCVX-ray2.90R1-155[»]
    3CD6X-ray2.75R1-155[»]
    3CMAX-ray2.80R1-155[»]
    3CMEX-ray2.95R1-155[»]
    3CPWX-ray2.70Q1-155[»]
    3CXCX-ray3.00Q2-155[»]
    3G4SX-ray3.20R2-151[»]
    3G6EX-ray2.70R2-151[»]
    3G71X-ray2.85R2-151[»]
    3I55X-ray3.11R1-155[»]
    3I56X-ray2.90R1-155[»]
    3OW2X-ray2.70Q2-151[»]
    4ADXelectron microscopy6.60R1-155[»]
    4HUBX-ray2.40R1-155[»]
    ProteinModelPortaliP10970.
    SMRiP10970. Positions 2-151.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10970.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L22P family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0091.
    HOGENOMiHOG000205045.
    KOiK02890.
    OMAiRFGYSFQ.

    Family and domain databases

    Gene3Di3.90.470.10. 1 hit.
    HAMAPiMF_01331_A. Ribosomal_L22_A.
    InterProiIPR001063. Ribosomal_L22.
    IPR018260. Ribosomal_L22/L17_CS.
    IPR005721. Ribosomal_L22/L17_euk/arc.
    [Graphical view]
    PANTHERiPTHR11593. PTHR11593. 1 hit.
    PfamiPF00237. Ribosomal_L22. 1 hit.
    [Graphical view]
    SUPFAMiSSF54843. SSF54843. 1 hit.
    TIGRFAMsiTIGR01038. L22_arch. 1 hit.
    PROSITEiPS00464. RIBOSOMAL_L22. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P10970-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGISYSVEAD PDTTAKAMLR ERQMSFKHSK AIAREIKGKT AGEAVDYLEA    50
    VIEGDQPVPF KQHNSGVGHK SKVDGWDAGR YPEKASKAFL DLLENAVGNA 100
    DHQGFDGEAM TIKHVAAHKV GEQQGRKPRA MGRASAWNSP QVDVELILEE 150
    PEVED 155
    Length:155
    Mass (Da):16,941
    Last modified:January 23, 2007 - v2
    Checksum:iE6730272296C0D7C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05222 Genomic DNA. Translation: AAA86864.1.
    AY596297 Genomic DNA. Translation: AAV46523.1.
    PIRiH35063. R5HS22.
    RefSeqiWP_011223742.1. NC_006396.1.
    YP_136229.1. NC_006396.1.

    Genome annotation databases

    EnsemblBacteriaiAAV46523; AAV46523; rrnAC1606.
    GeneIDi3128443.
    KEGGihma:rrnAC1606.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05222 Genomic DNA. Translation: AAA86864.1 .
    AY596297 Genomic DNA. Translation: AAV46523.1 .
    PIRi H35063. R5HS22.
    RefSeqi WP_011223742.1. NC_006396.1.
    YP_136229.1. NC_006396.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FFK X-ray 2.40 O 2-155 [» ]
    1JJ2 X-ray 2.40 Q 2-155 [» ]
    1K73 X-ray 3.01 S 2-155 [» ]
    1K8A X-ray 3.00 S 2-155 [» ]
    1K9M X-ray 3.00 S 2-155 [» ]
    1KC8 X-ray 3.01 S 2-155 [» ]
    1KD1 X-ray 3.00 S 2-155 [» ]
    1KQS X-ray 3.10 Q 2-155 [» ]
    1M1K X-ray 3.20 S 2-155 [» ]
    1M90 X-ray 2.80 S 2-155 [» ]
    1N8R X-ray 3.00 S 2-155 [» ]
    1NJI X-ray 3.00 S 2-155 [» ]
    1Q7Y X-ray 3.20 S 2-155 [» ]
    1Q81 X-ray 2.95 S 2-155 [» ]
    1Q82 X-ray 2.98 S 2-155 [» ]
    1Q86 X-ray 3.00 S 2-155 [» ]
    1QVF X-ray 3.10 Q 2-155 [» ]
    1QVG X-ray 2.90 Q 2-155 [» ]
    1S72 X-ray 2.40 R 1-155 [» ]
    1VQ4 X-ray 2.70 R 1-155 [» ]
    1VQ5 X-ray 2.60 R 1-155 [» ]
    1VQ6 X-ray 2.70 R 1-155 [» ]
    1VQ7 X-ray 2.50 R 1-155 [» ]
    1VQ8 X-ray 2.20 R 1-155 [» ]
    1VQ9 X-ray 2.40 R 1-155 [» ]
    1VQK X-ray 2.30 R 1-155 [» ]
    1VQL X-ray 2.30 R 1-155 [» ]
    1VQM X-ray 2.30 R 1-155 [» ]
    1VQN X-ray 2.40 R 1-155 [» ]
    1VQO X-ray 2.20 R 1-155 [» ]
    1VQP X-ray 2.25 R 1-155 [» ]
    1W2B X-ray 3.50 Q 2-155 [» ]
    1YHQ X-ray 2.40 R 1-155 [» ]
    1YI2 X-ray 2.65 R 1-155 [» ]
    1YIJ X-ray 2.60 R 1-155 [» ]
    1YIT X-ray 2.80 R 1-155 [» ]
    1YJ9 X-ray 2.80 R 1-152 [» ]
    1YJN X-ray 3.00 R 1-155 [» ]
    1YJW X-ray 2.90 R 1-155 [» ]
    2OTJ X-ray 2.90 R 1-155 [» ]
    2OTL X-ray 2.70 R 1-155 [» ]
    2QA4 X-ray 3.00 R 1-155 [» ]
    2QEX X-ray 2.90 R 1-155 [» ]
    3CC2 X-ray 2.40 R 1-155 [» ]
    3CC4 X-ray 2.70 R 1-155 [» ]
    3CC7 X-ray 2.70 R 1-155 [» ]
    3CCE X-ray 2.75 R 1-155 [» ]
    3CCJ X-ray 2.70 R 1-155 [» ]
    3CCL X-ray 2.90 R 1-155 [» ]
    3CCM X-ray 2.55 R 1-155 [» ]
    3CCQ X-ray 2.90 R 1-155 [» ]
    3CCR X-ray 3.00 R 1-155 [» ]
    3CCS X-ray 2.95 R 1-155 [» ]
    3CCU X-ray 2.80 R 1-155 [» ]
    3CCV X-ray 2.90 R 1-155 [» ]
    3CD6 X-ray 2.75 R 1-155 [» ]
    3CMA X-ray 2.80 R 1-155 [» ]
    3CME X-ray 2.95 R 1-155 [» ]
    3CPW X-ray 2.70 Q 1-155 [» ]
    3CXC X-ray 3.00 Q 2-155 [» ]
    3G4S X-ray 3.20 R 2-151 [» ]
    3G6E X-ray 2.70 R 2-151 [» ]
    3G71 X-ray 2.85 R 2-151 [» ]
    3I55 X-ray 3.11 R 1-155 [» ]
    3I56 X-ray 2.90 R 1-155 [» ]
    3OW2 X-ray 2.70 Q 2-151 [» ]
    4ADX electron microscopy 6.60 R 1-155 [» ]
    4HUB X-ray 2.40 R 1-155 [» ]
    ProteinModelPortali P10970.
    SMRi P10970. Positions 2-151.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272569.rrnAC1606.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAV46523 ; AAV46523 ; rrnAC1606 .
    GeneIDi 3128443.
    KEGGi hma:rrnAC1606.

    Phylogenomic databases

    eggNOGi COG0091.
    HOGENOMi HOG000205045.
    KOi K02890.
    OMAi RFGYSFQ.

    Enzyme and pathway databases

    BioCyci HMAR272569:GJDH-1462-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P10970.

    Family and domain databases

    Gene3Di 3.90.470.10. 1 hit.
    HAMAPi MF_01331_A. Ribosomal_L22_A.
    InterProi IPR001063. Ribosomal_L22.
    IPR018260. Ribosomal_L22/L17_CS.
    IPR005721. Ribosomal_L22/L17_euk/arc.
    [Graphical view ]
    PANTHERi PTHR11593. PTHR11593. 1 hit.
    Pfami PF00237. Ribosomal_L22. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54843. SSF54843. 1 hit.
    TIGRFAMsi TIGR01038. L22_arch. 1 hit.
    PROSITEi PS00464. RIBOSOMAL_L22. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
    3. "The primary structures of ribosomal proteins L16, L23 and L33 from the archaebacterium Halobacterium marismortui."
      Hatakeyama T., Hatakeyama T., Kimura M.
      FEBS Lett. 240:21-28(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-155.
    4. "Extended N-terminal sequencing of proteins of archaebacterial ribosomes blotted from two-dimensional gels onto glass fiber and poly(vinylidene difluoride) membrane."
      Walsh M.J., McDougall J., Wittmann-Liebold B.
      Biochemistry 27:6867-6876(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-27.
    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 nameiRL22_HALMA
    AccessioniPrimary (citable) accession number: P10970
    Secondary accession number(s): Q5V1S9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 113 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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