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Protein

Proline--tRNA ligase

Gene

proS

Organism
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). Can inadvertently accommodate and process cysteine. The misacylated Cys-tRNA(Pro) is not edited by ProRS.

Catalytic activityi

ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro).

Kineticsi

  1. KM=0.28 mM for proline1 Publication
  2. KM=0.17 mM for cysteine1 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi6.1.1.15. 5412.
    SABIO-RKQ6N5P6.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proline--tRNA ligase (EC:6.1.1.15)
    Alternative name(s):
    Prolyl-tRNA synthetase
    Short name:
    ProRS
    Gene namesi
    Name:proS
    Ordered Locus Names:RPA2928
    OrganismiRhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
    Taxonomic identifieri258594 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas
    Proteomesi
    • UP000001426 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 438438Proline--tRNA ligasePRO_0000248227Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    DIPiDIP-29058N.
    STRINGi258594.RPA2928.

    Structurei

    Secondary structure

    1
    438
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 53Combined sources
    Helixi21 – 288Combined sources
    Beta strandi32 – 365Combined sources
    Beta strandi39 – 424Combined sources
    Helixi44 – 6320Combined sources
    Beta strandi73 – 764Combined sources
    Helixi77 – 826Combined sources
    Helixi85 – 884Combined sources
    Helixi90 – 923Combined sources
    Beta strandi93 – 975Combined sources
    Beta strandi103 – 1064Combined sources
    Helixi111 – 12111Combined sources
    Helixi125 – 1273Combined sources
    Beta strandi129 – 13911Combined sources
    Helixi148 – 1503Combined sources
    Beta strandi153 – 16614Combined sources
    Helixi167 – 18620Combined sources
    Turni187 – 1893Combined sources
    Beta strandi192 – 1965Combined sources
    Helixi200 – 2023Combined sources
    Beta strandi207 – 2137Combined sources
    Beta strandi218 – 2247Combined sources
    Helixi225 – 2295Combined sources
    Beta strandi239 – 2413Combined sources
    Helixi244 – 2529Combined sources
    Beta strandi255 – 2573Combined sources
    Turni258 – 2603Combined sources
    Helixi265 – 2695Combined sources
    Turni272 – 2743Combined sources
    Beta strandi275 – 29016Combined sources
    Helixi292 – 2965Combined sources
    Beta strandi300 – 3023Combined sources
    Beta strandi308 – 3103Combined sources
    Beta strandi312 – 3198Combined sources
    Helixi320 – 33011Combined sources
    Beta strandi331 – 3333Combined sources
    Turni341 – 3433Combined sources
    Beta strandi347 – 3548Combined sources
    Helixi358 – 37316Combined sources
    Beta strandi378 – 3814Combined sources
    Helixi387 – 39711Combined sources
    Beta strandi400 – 4056Combined sources
    Helixi407 – 4104Combined sources
    Turni411 – 4133Combined sources
    Beta strandi414 – 4196Combined sources
    Turni420 – 4223Combined sources
    Beta strandi425 – 4295Combined sources
    Turni430 – 4345Combined sources
    Turni435 – 4373Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2I4LX-ray2.00A/B/C1-438[»]
    2I4MX-ray2.80A/B/C1-438[»]
    2I4NX-ray2.85A/B/C1-438[»]
    2I4OX-ray2.40A/B/C1-438[»]
    ProteinModelPortaliQ6N5P6.
    SMRiQ6N5P6. Positions 1-438.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ6N5P6.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105C90. Bacteria.
    COG0442. LUCA.
    HOGENOMiHOG000076894.
    KOiK01881.
    OMAiIQPAELW.
    OrthoDBiEOG6TTVMR.
    PhylomeDBiQ6N5P6.

    Family and domain databases

    Gene3Di3.40.50.800. 1 hit.
    HAMAPiMF_01570. Pro_tRNA_synth_type2.
    InterProiIPR002314. aa-tRNA-synt_IIb.
    IPR006195. aa-tRNA-synth_II.
    IPR004154. Anticodon-bd.
    IPR002316. Pro-tRNA-ligase_IIa.
    IPR004500. Pro-tRNA-synth_IIa_bac-type.
    IPR023716. Prolyl-tRNA_ligase_IIa_type2.
    [Graphical view]
    PANTHERiPTHR11451:SF3. PTHR11451:SF3. 2 hits.
    PfamiPF03129. HGTP_anticodon. 1 hit.
    PF00587. tRNA-synt_2b. 1 hit.
    [Graphical view]
    PRINTSiPR01046. TRNASYNTHPRO.
    SUPFAMiSSF52954. SSF52954. 1 hit.
    TIGRFAMsiTIGR00409. proS_fam_II. 1 hit.
    PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q6N5P6-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRLSRFFLPI LKENPKEAEI VSHRLMLRAG MLRQEAAGIY AWLPLGHRVL
    60 70 80 90 100
    KKIEQIVREE QNRAGAIELL MPTLQLADLW RESGRYDAYG PEMLRIADRH
    110 120 130 140 150
    KRELLYGPTN EEMITEIFRA YIKSYKSLPL NLYHIQWKFR DEQRPRFGVM
    160 170 180 190 200
    RGREFLMKDA YSFDVDEAGA RKSYNKMFVA YLRTFARMGL KAIPMRAETG
    210 220 230 240 250
    PIGGDLSHEF IVLAETGESG VYIDRDVLNL PVPDENVDYD GDLTPIIKQW
    260 270 280 290 300
    TSVYAATEDV HEPARYESEV PEANRLNTRG IEVGQIFYFG TKYSDSMKAN
    310 320 330 340 350
    VTGPDGTDAP IHGGSYGVGV SRLLGAIIEA CHDDNGIIWP EAVAPFRVTI
    360 370 380 390 400
    LNLKQGDAAT DAACDQLYRE LSAKGVDVLY DDTDQRAGAK FATADLIGIP
    410 420 430
    WQIHVGPRGL AEGKVELKRR SDGARENLAL ADVVARLT
    Length:438
    Mass (Da):49,309
    Last modified:July 5, 2004 - v1
    Checksum:i36D07FB76904F42A
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    BX572602 Genomic DNA. Translation: CAE28369.1.
    RefSeqiWP_011158477.1. NC_005296.1.

    Genome annotation databases

    EnsemblBacteriaiCAE28369; CAE28369; RPA2928.
    KEGGirpa:RPA2928.
    PATRICi23290299. VBIRhoPal84835_3076.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    BX572602 Genomic DNA. Translation: CAE28369.1.
    RefSeqiWP_011158477.1. NC_005296.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2I4LX-ray2.00A/B/C1-438[»]
    2I4MX-ray2.80A/B/C1-438[»]
    2I4NX-ray2.85A/B/C1-438[»]
    2I4OX-ray2.40A/B/C1-438[»]
    ProteinModelPortaliQ6N5P6.
    SMRiQ6N5P6. Positions 1-438.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-29058N.
    STRINGi258594.RPA2928.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCAE28369; CAE28369; RPA2928.
    KEGGirpa:RPA2928.
    PATRICi23290299. VBIRhoPal84835_3076.

    Phylogenomic databases

    eggNOGiENOG4105C90. Bacteria.
    COG0442. LUCA.
    HOGENOMiHOG000076894.
    KOiK01881.
    OMAiIQPAELW.
    OrthoDBiEOG6TTVMR.
    PhylomeDBiQ6N5P6.

    Enzyme and pathway databases

    BRENDAi6.1.1.15. 5412.
    SABIO-RKQ6N5P6.

    Miscellaneous databases

    EvolutionaryTraceiQ6N5P6.

    Family and domain databases

    Gene3Di3.40.50.800. 1 hit.
    HAMAPiMF_01570. Pro_tRNA_synth_type2.
    InterProiIPR002314. aa-tRNA-synt_IIb.
    IPR006195. aa-tRNA-synth_II.
    IPR004154. Anticodon-bd.
    IPR002316. Pro-tRNA-ligase_IIa.
    IPR004500. Pro-tRNA-synth_IIa_bac-type.
    IPR023716. Prolyl-tRNA_ligase_IIa_type2.
    [Graphical view]
    PANTHERiPTHR11451:SF3. PTHR11451:SF3. 2 hits.
    PfamiPF03129. HGTP_anticodon. 1 hit.
    PF00587. tRNA-synt_2b. 1 hit.
    [Graphical view]
    PRINTSiPR01046. TRNASYNTHPRO.
    SUPFAMiSSF52954. SSF52954. 1 hit.
    TIGRFAMsiTIGR00409. proS_fam_II. 1 hit.
    PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-98 / CGA009.
    2. "Cysteine activation is an inherent in vitro property of prolyl-tRNA synthetases."
      Ahel I., Stathopoulos C., Ambrogelly A., Sauerwald A., Toogood H., Hartsch T., Soell D.
      J. Biol. Chem. 277:34743-34748(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROLINE AND CYSTEINE ACTIVATION, LACK OF EDITING ACTIVITY, KINETIC PARAMETERS.

    Entry informationi

    Entry nameiSYP_RHOPA
    AccessioniPrimary (citable) accession number: Q6N5P6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 5, 2006
    Last sequence update: July 5, 2004
    Last modified: November 11, 2015
    This is version 89 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    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.