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Summary[edit | edit source]

  • pan ID?: SAUPAN005782000
  • symbol?:
  • synonym:
  • description?: N-acetylmuramoyl-L-alanine amidase

      descriptions from strain specific annotations:

    • N-acetylmuramoyl-L-alanine amidase
    • autolysin E, putative
    • N-acetylglucosaminidase
    • putative N-acetylmuramoyl-L-alanine amidase
    • autolysin E
    • bifunctional autolysin
    • mannosyl-glycoendo-beta-N-acetylglucosaminidase family protein
    • mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase
    • mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase family protein
    • peptidoglycan endo-beta-N-acetylglucosaminidase
  • strand?: -
  • coordinates?: 5869017..5869655
  • synteny block?: BlockID0045270
  • occurrence?: in 100% of 34 strains

sagA (atlE, lytD) : peptidoglycan N-acetylglucosaminidase SagA [1]

• A crystal structure is available: 4PIA

  • Staphylocci produce multiple cell wall remodeling enzymes that differ in where they digest peptidoglycan, their localization on the membrane and regulation of their activity
    • Staphylococci produce one bifunctional N-acetylglucosaminidase/amidase: Atl (AtlA)
    • Staphylococci produce three N-acetylglucosaminidases: SagA (LytD, AtlE), SagB and ScaH (Aly)
    • Staphylococci produce two bifunctional amidase/endopeptidases: LytN and EssH
    • Staphylococci produce two lytic transglycosylases: SceD and IsaA
    • Staphylococci produce two monofunctional amidases: SsaA and Sle1
    • Staphylococci produce three monofunctional endopeptidases: LytH, LytM and LytU
    • Staphylococci produce five uncharacterized probable monofunctional amidases: (SsaA2), (SsaA3), (SsaA4), (SsaA5) and (SsaA6)

Orthologs[edit | edit source]

    COL:
    N315:
    NCTC8325:
    Newman:
    USA300_FPR3757:
    04-02981:
    SA2981_2245
    08BA02176:
    C248_2348
    11819-97:
    MS7_2324
    6850:
    RSAU_002144
    71193:
    ST398NM01_2357
    ECT-R 2:
    ECTR2_2166
    ED133:
    SAOV_2346c
    ED98:
    SAAV_2368
    HO 5096 0412:
    SAEMRSA15_22040
    JH1:
    SaurJH1_2373
    JH9:
    SaurJH9_2330
    JKD6008:
    SAA6008_02342 (lytA)
    JKD6159:
    SAA6159_02210 (lytA)
    JSNZ:
    JSNZ_002273
    LGA251:
    SARLGA251_20890
    M013:
    M013TW_2263
    MRSA252:
    SAR2391
    MSHR1132:
    SAMSHR1132_21310
    MSSA476:
    SAS2198
    Mu3:
    SAHV_2291
    Mu50:
    SAV2307
    MW2:
    MW2226
    RF122:
    SAB2183c
    ST398:
    SAPIG2357
    T0131:
    SAT0131_02485 (mutS2)
    TCH60:
    HMPREF0772_10889 (amiD3)
    TW20:
    SATW20_24370
    USA300_TCH1516:
    USA300HOU_2288 (lytA)
    VC40:
    SAVC_10390

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             MKKNFKLRISTLLLIVILVVFAVLLIVNETKLFKNDVNYSFDEAVSMQQGKGIVQTKEED
    N315            MKKNFKLRISTLLLIVILVVFAVLLIVNETKLFKNDVNYSFDEAVSMQQGKGIVQTKEED
    NCTC8325        ----------------------------------------------MQQGKGIVQTKEED
    Newman          MKKNFKLRISTLLLIVILVVFAVLLIVNETKLFKNDVNYSFDEAVSMQQGKGIVQTKEED
    USA300_FPR3757  MKKNFKLRISTLLLIVILVVFAVLLIVNETKLFKNDVNYSFDEAVSMQQGKGIVQTKEED
                                                                  **************

    COL             GKFVEANNNEIAKAMTISHKDNDMKYMDITEKVPMSESEVNQLLKGKGILENRGKVFLEA
    N315            GKFVEANNNEIAKAMTISHKDNDMKYMDITEKVPMSESEVNQLLKGKGILENRGKVFLEA
    NCTC8325        GKFVEANNNEIAKAMTISHKDNDMKYMDITEKVPMSESEVNQLLKGKGILENRGKVFLEA
    Newman          GKFVEANNNEIAKAMTISHKDNDMKYMDITEKVPMSESEVNQLLKGKGILENRGKVFLEA
    USA300_FPR3757  GKFVEANNNEIAKAMTISHKDNDMKYMDITEKVPMSESEVNQLLKGKGILENRGKVFLEA
                    ************************************************************

    COL             QEKYEVNVIYLVSHALVETGNGKSELAKGIKDGKKRYYNFFGIGAFDSSAVRSGKSYAEK
    N315            QEKYEVNVIYLVSHALVETGNGKSELAKGIKDGKKRYYNFFGIGAFDSSAVRSGKSYAEK
    NCTC8325        QEKYEVNVIYLVSHALVETGNGKSELAKGIKDGKKRYYNFFGIGAFDSSAVRSGKSYAEK
    Newman          QEKYEVNVIYLVSHALVETGNGKSELAKGIKDGKKRYYNFFGIGAFDSSAVRSGKSYAEK
    USA300_FPR3757  QEKYEVNVIYLVSHALVETGNGKSELAKGIKDGKKRYYNFFGIGAFDSSAVRSGKSYAEK
                    ************************************************************

    COL             EQWTSPDKAIIGGAKFIRNEYFENNQLNLYQMRWNPENPAQHQYASDIRWADKIAKLMDK
    N315            EQWTSPDKAIIGGAKFIRNEYFENNQLNLYQMRWNPENPAQHQYASDIRWADKIAKLMDK
    NCTC8325        EQWTSPDKAIIGGAKFIRNEYFENNQLNLYQMRWNPENPAQHQYASDIRWADKIAKLMDK
    Newman          EQWTSPDKAIIGGAKFIRNEYFENNQLNLYQMRWNPENPAQHQYASDIRWADKIAKLMDK
    USA300_FPR3757  EQWTSPDKAIIGGAKFIRNEYFENNQLNLYQMRWNPENPAQHQYASDIRWADKIAKLMDK
                    ************************************************************

    COL             SYKQFGIKKDDIRQTYYK
    N315            SYKQFGIKKDDIRQTYYK
    NCTC8325        SYKQFGIKKDDIRQTYYK
    Newman          SYKQFGIKKDDIRQTYYK
    USA300_FPR3757  SYKQFGIKKDDIRQTYYK
                    ******************

  1. Min Wang, Girbe Buist, Jan Maarten van Dijl
    Staphylococcus aureus cell wall maintenance - the multifaceted roles of peptidoglycan hydrolases in bacterial growth, fitness, and virulence.
    FEMS Microbiol Rev: 2022, 46(5);
    [PubMed:35675307] [WorldCat.org] [DOI] (I p)
    Marko Mihelič, Kristina Vlahoviček-Kahlina, Miha Renko, Stephane Mesnage, Andreja Doberšek, Ajda Taler-Verčič, Andreja Jakas, Dušan Turk
    The mechanism behind the selection of two different cleavage sites in NAG-NAM polymers.
    IUCrJ: 2017, 4(Pt 2);185-198
    [PubMed:28250957] [WorldCat.org] [DOI] (P e)
    Min Wang, Xiaofang Li, Francis M Cavallo, Harita Yedavally, Sjouke Piersma, Elisa J M Raineri, Elias Vera Murguia, Jeroen Kuipers, Zhenhua Zhang, Jan Maarten van Dijl, Girbe Buist
    Functional profiling of CHAP domain-containing peptidoglycan hydrolases of Staphylococcus aureus USA300 uncovers potential targets for anti-staphylococcal therapies.
    Int J Med Microbiol: 2024, 316;151632
    [PubMed:39142057] [WorldCat.org] [DOI] (I p)