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Summary[edit | edit source]

  • pan ID?: SAUPAN003192000
  • symbol?:
  • synonym:
  • description?: RNA ligase, putative

      descriptions from strain specific annotations:

    • RNA ligase, putative
    • YjcG family protein
    • 2-5 RNA ligase
    • 2',5' RNA ligase
    • 2H phosphoesterase superfamily protein Bsu1186(yjcG)
    • conserved protein YjcG
  • strand?: +
  • coordinates?: 3584655..3585164
  • synteny block?: BlockID0022790
  • occurrence?: in 100% of 34 strains

yjcG : 2',3'-cyclic purine 2'-phosphodiesterase [1]

The physiological role of YjcG in firmicutes remains unclear and underexplored. It is established as a virulence factor in the silkworm model, required for virulence factor production, and biochemically characterized as a 2',3'-cyclic purine 2'-phosphodiesterase. However, although staphylococci do use 2',3'-cAMP signaling, the KD for free 2',3'-cGAMP is too high for free cyclic nucleotides to be the natural substrate. Furthermore, YjcG expression is regulated by binding of small RNA RsaE to the 5'-UTR of its mRNA suggesting tight regulatory control. Although to my knowledge this has not yet been proposed, the most likely role for YjcG is in modulation of mRNA stability. Many RNA endonucleases leave a terminal 2',3'-cyclic monophosphate after cleavage. Polynucleotide phosphorylase degrades RNAs with either a free 3'-OH or a 2',3'-cyclic monophosphate but is blocked by 3'-phosphates. Thus, YjcG may stabilize mRNA transcripts cleaved by ribonucleases to terminal 2,'3'-cyclic monophosphates by converting those ends to 3'-phosphates. Indeed, this is the exact mechanism of RNase Y (a.k.a. CvfA) and how it functions as a virulence factor to stabilize hemolysin transcripts.

Orthologs[edit | edit source]

    COL:
    N315:
    NCTC8325:
    Newman:
    USA300_FPR3757:
    04-02981:
    SA2981_0969
    08BA02176:
    C248_1039
    11819-97:
    MS7_0970
    6850:
    RSAU_000895
    71193:
    ST398NM01_1010
    ECT-R 2:
    ECTR2_869
    ED133:
    SAOV_0960
    ED98:
    SAAV_0977
    HO 5096 0412:
    SAEMRSA15_08450
    JH1:
    SaurJH1_1032
    JH9:
    SaurJH9_1013
    JKD6008:
    SAA6008_00969
    JKD6159:
    SAA6159_00871
    JSNZ:
    JSNZ_000974
    LGA251:
    SARLGA251_09300
    M013:
    M013TW_0939
    MRSA252:
    SAR0985
    MSHR1132:
    SAMSHR1132_08620
    MSSA476:
    SAS0884
    Mu3:
    SAHV_1009
    Mu50:
    SAV1015
    MW2:
    MW0896
    RF122:
    SAB0881
    ST398:
    SAPIG1010
    T0131:
    SAT0131_01049
    TCH60:
    HMPREF0772_12219
    TW20:
    SATW20_10120
    USA300_TCH1516:
    USA300HOU_0973
    VC40:
    SAVC_04240

Genome Viewer[edit | edit source]

COL
N315
NCTC8325
Newman
USA300_FPR3757

Alignments[edit | edit source]

  • alignment of orthologues:
    CLUSTAL format alignment by MAFFT L-INS-i (v7.307)


    COL             MILGLALIPSKSFQEAVDSYRKRYDKQYSRIKPHVTIKAPFEIKDGDLDSVIEQVRARIN
    N315            MILGLALIPSKSFQEAVDSYRKRYDKQYSRIKPHVTIKAPFEIEDGDLDSVIEQVRARIN
    NCTC8325        MILGLALIPSKSFQEAVDSYRKRYDKQYSRIKPHVTIKAPFEIKDGDLDSVIEQVRARIN
    Newman          MILGLALIPSKSFQEAVDSYRKRYDKQYSRIKPHVTIKAPFEIKDGDLDSVIEQVRARIN
    USA300_FPR3757  MILGLALIPSKSFQEAVDSYRKRYDKQYSRIKPHVTIKAPFEIKDGDLDSVIEQVRARIN
                    *******************************************:****************

    COL             GIPAVEVHATKASSFKPTNNVIYFKVAKTDDLEELFNRFNGEDFYGEAEHVFVPHFTIAQ
    N315            GIPAVEVHATKASSFKPTNNVIYFKVAKTDDLEELFNRFNGEDFYGEAEHVFVPHFTIAQ
    NCTC8325        GIPAVEVHATKASSFKPTNNVIYFKVAKTDDLEELFNRFNGEDFYGEAEHVFVPHFTIAQ
    Newman          GIPAVEVHATKASSFKPTNNVIYFKVAKTDDLEELFNRFNGEDFYGEAEHVFVPHFTIAQ
    USA300_FPR3757  GIPAVEVHATKASSFKPTNNVIYFKVAKTDDLEELFNRFNGEDFYGEAEHVFVPHFTIAQ
                    ************************************************************

    COL             GLSSQEFEDIFGQVALAGVDHKEIIDELTLLRFDDDEDKWKVIETFKLA
    N315            GLSSQEFEDIFGQVALAGVDHKEIIDELTLLRFDDDEDKWKVIETFKLA
    NCTC8325        GLSSQEFEDIFGQVALAGVDHKEIIDELTLLRFDDDEDKWKVIETFKLA
    Newman          GLSSQEFEDIFGQVALAGVDHKEIIDELTLLRFDDDEDKWKVIETFKLA
    USA300_FPR3757  GLSSQEFEDIFGQVALAGVDHKEIIDELTLLRFDDDEDKWKVIETFKLA
                    *************************************************

  1. Thomas Geissmann, Clément Chevalier, Marie-Josée Cros, Sandrine Boisset, Pierre Fechter, Céline Noirot, Jacques Schrenzel, Patrice François, François Vandenesch, Christine Gaspin, Pascale Romby
    A search for small noncoding RNAs in Staphylococcus aureus reveals a conserved sequence motif for regulation.
    Nucleic Acids Res: 2009, 37(21);7239-57
    [PubMed:19786493] [WorldCat.org] [DOI] (I p)
    Shunsuke Numata, Makiko Nagata, Han Mao, Kazuhisa Sekimizu, Chikara Kaito
    CvfA protein and polynucleotide phosphorylase act in an opposing manner to regulate Staphylococcus aureus virulence.
    J Biol Chem: 2014, 289(12);8420-31
    [PubMed:24492613] [WorldCat.org] [DOI] (I p)
    Kenta Imae, Yuki Saito, Hayato Kizaki, Hiroki Ryuno, Han Mao, Atsushi Miyashita, Yutaka Suzuki, Kazuhisa Sekimizu, Chikara Kaito
    Novel Nucleoside Diphosphatase Contributes to Staphylococcus aureus Virulence.
    J Biol Chem: 2016, 291(36);18608-18619
    [PubMed:27422825] [WorldCat.org] [DOI] (I p)
    Yong Zhang, Rym Agrebi, Lauren E Bellows, Jean-François Collet, Volkhard Kaever, Angelika Gründling
    Evolutionary Adaptation of the Essential tRNA Methyltransferase TrmD to the Signaling Molecule 3',5'-cAMP in Bacteria.
    J Biol Chem: 2017, 292(1);313-327
    [PubMed:27881678] [WorldCat.org] [DOI] (I p)
    Shuhei Mitsutomi, Nobuyoshi Akimitsu, Kazuhisa Sekimizu, Chikara Kaito
    Identification of 2H phosphoesterase superfamily proteins with 2'-CPDase activity.
    Biochimie: 2019, 165;235-244
    [PubMed:31422053] [WorldCat.org] [DOI] (I p)