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Protein

Proline--tRNA ligase

Gene

proS

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 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). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). Misacylated Cys-tRNA(Pro) is not edited by ProRS, but instead may be edited in trans by YbaK.

Catalytic activityi

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

Kineticsi

  1. KM=0.25 mM for proline3 Publications
  2. KM=140 mM for alanine3 Publications
  3. KM=0.17 mM for cysteine3 Publications

    GO - Molecular functioni

    • Ala-tRNA(Pro) hydrolase activity Source: UniProtKB
    • ATP binding Source: UniProtKB-KW
    • proline-tRNA ligase activity Source: EcoCyc

    GO - Biological processi

    • prolyl-tRNA aminoacylation Source: EcoCyc

    Keywordsi

    Molecular functionAminoacyl-tRNA synthetase, Ligase
    Biological processProtein biosynthesis
    LigandATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:PROS-MONOMER.
    MetaCyc:PROS-MONOMER.
    BRENDAi6.1.1.15. 2026.
    SABIO-RKiP16659.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proline--tRNA ligase (EC:6.1.1.15)
    Alternative name(s):
    Global RNA synthesis factor
    Prolyl-tRNA synthetase
    Short name:
    ProRS
    Gene namesi
    Name:proS
    Synonyms:drpA
    Ordered Locus Names:b0194, JW0190
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10770. proS.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi257T → A: Reduces the posttransfer editing activity 5-fold, with little change in both the aminoacylation and the pretransfer editing activities. 1 Publication1
    Mutagenesisi279K → A: Severely affects the posttransfer editing activity, with little change in both the aminoacylation and the pretransfer editing activities. 1 Publication1
    Mutagenesisi350D → A: Abolishes the pretransfer editing activity and reduces the aminoacylation activity 20-fold and the posttransfer editing activity 5-fold. 1 Publication1
    Mutagenesisi369H → A: Reduces both the aminoacylation and the pretransfer editing activities 2.5-fold, and the posttransfer editing activity 5-fold. Loss of specificity in deacylation. 1 Publication1
    Mutagenesisi378D → A: Little change in both the aminoacylation and the editing activities. 1 Publication1
    Mutagenesisi386D → A: Reduces the posttransfer editing activity approximately 2-fold, with little change in both the aminoacylation and the pretransfer editing activities. 1 Publication1
    Mutagenesisi394D → A: Reduces the posttransfer editing activity approximately 2-fold, with little change in both the aminoacylation and the pretransfer editing activities. 1 Publication1
    Mutagenesisi443C → G: 150-fold decrease in posttransfer editing activity against alanine, without change neither in pretransfer editing nor in aminoacylation. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001393291 – 572Proline--tRNA ligaseAdd BLAST572

    Proteomic databases

    EPDiP16659.
    PaxDbiP16659.
    PRIDEiP16659.

    2D gel databases

    SWISS-2DPAGEiP16659.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    BioGridi4261629. 6 interactors.
    DIPiDIP-10573N.
    IntActiP16659. 20 interactors.
    MINTiMINT-1261583.
    STRINGi316385.ECDH10B_0175.

    Structurei

    3D structure databases

    ProteinModelPortaliP16659.
    SMRiP16659.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domaini

    Consists of three domains: the N-terminal catalytic domain, the editing domain and the C-terminal anticodon-binding domain.

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105C90. Bacteria.
    COG0442. LUCA.
    HOGENOMiHOG000076893.
    InParanoidiP16659.
    KOiK01881.
    PhylomeDBiP16659.

    Family and domain databases

    CDDicd00779. ProRS_core_prok. 1 hit.
    Gene3Di3.40.50.800. 1 hit.
    HAMAPiMF_01569. Pro_tRNA_synth_type1. 1 hit.
    InterProiView protein in InterPro
    IPR002314. aa-tRNA-synt_IIb.
    IPR006195. aa-tRNA-synth_II.
    IPR004154. Anticodon-bd.
    IPR002316. Pro-tRNA-ligase_IIa.
    IPR004500. Pro-tRNA-synth_IIa_bac-type.
    IPR023717. Pro-tRNA-Synthase_IIa_type1.
    IPR033730. ProRS_core_prok.
    IPR007214. YbaK/aa-tRNA-synth-assoc-dom.
    PfamiView protein in Pfam
    PF03129. HGTP_anticodon. 1 hit.
    PF00587. tRNA-synt_2b. 1 hit.
    PF04073. tRNA_edit. 1 hit.
    PIRSFiPIRSF001535. ProRS_1. 1 hit.
    PRINTSiPR01046. TRNASYNTHPRO.
    SUPFAMiSSF52954. SSF52954. 1 hit.
    SSF55826. SSF55826. 1 hit.
    TIGRFAMsiTIGR00409. proS_fam_II. 1 hit.
    PROSITEiView protein in PROSITE
    PS50862. AA_TRNA_LIGASE_II. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P16659-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRTSQYLLST LKETPADAEV ISHQLMLRAG MIRKLASGLY TWLPTGVRVL
    60 70 80 90 100
    KKVENIVREE MNNAGAIEVS MPVVQPADLW QESGRWEQYG PELLRFVDRG
    110 120 130 140 150
    ERPFVLGPTH EEVITDLIRN ELSSYKQLPL NFYQIQTKFR DEVRPRFGVM
    160 170 180 190 200
    RSREFLMKDA YSFHTSQESL QETYDAMYAA YSKIFSRMGL DFRAVQADTG
    210 220 230 240 250
    SIGGSASHEF QVLAQSGEDD VVFSDTSDYA ANIELAEAIA PKEPRAAATQ
    260 270 280 290 300
    EMTLVDTPNA KTIAELVEQF NLPIEKTVKT LLVKAVEGSS FPQVALLVRG
    310 320 330 340 350
    DHELNEVKAE KLPQVASPLT FATEEEIRAV VKAGPGSLGP VNMPIPVVID
    360 370 380 390 400
    RTVAAMSDFA AGANIDGKHY FGINWDRDVA TPEVADIRNV VAGDPSPDGQ
    410 420 430 440 450
    GRLLIKRGIE VGHIFQLGTK YSEALKASVQ GEDGRNQILT MGCYGIGVTR
    460 470 480 490 500
    VVAAAIEQNY DERGIVWPDA IAPFQVAILP MNMHKSFRVQ ELAEKLYSEL
    510 520 530 540 550
    RAQGIEVLLD DRKERPGVMF ADMELIGIPH TIVLGDRNLD NDDIEYKYRR
    560 570
    NGEKQLIKTG DIVEYLVKQI KG
    Length:572
    Mass (Da):63,693
    Last modified:August 29, 2003 - v4
    Checksum:i312D29390E91C486
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti26 – 27ML → IV (PubMed:2203971).Curated2
    Sequence conflicti127 – 128QL → HV in AAA23710 (PubMed:1688424).Curated2
    Sequence conflicti205 – 216SASHE…VLAQS → RPLTNSRCWRR in AAA23710 (PubMed:1688424).CuratedAdd BLAST12
    Sequence conflicti205S → Q (PubMed:2203971).Curated1
    Sequence conflicti516 – 517PG → RA (PubMed:1688424).Curated2
    Sequence conflicti518 – 572Missing (PubMed:1688424).CuratedAdd BLAST55

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X55518 Genomic DNA. Translation: CAA39134.1.
    M97858 Genomic DNA. Translation: AAA24420.1.
    M32357 Genomic DNA. Translation: AAA23710.1.
    U70214 Genomic DNA. Translation: AAB08622.1.
    U00096 Genomic DNA. Translation: AAC73305.1.
    AP009048 Genomic DNA. Translation: BAA77870.2.
    D15061 Genomic DNA. Translation: BAA03654.1.
    PIRiB64744. YPEC.
    RefSeqiNP_414736.1. NC_000913.3.
    WP_001260717.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73305; AAC73305; b0194.
    BAA77870; BAA77870; BAA77870.
    GeneIDi949116.
    KEGGiecj:JW0190.
    eco:b0194.
    PATRICifig|1411691.4.peg.2084.

    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.

    Entry informationi

    Entry nameiSYP_ECOLI
    AccessioniPrimary (citable) accession number: P16659
    Secondary accession number(s): P78272, Q59430
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: August 29, 2003
    Last modified: July 5, 2017
    This is version 166 of the entry and version 4 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    3. SIMILARITY comments
      Index of protein domains and families