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Summary[edit | edit source]

  • pan ID?: SAUPAN004467000
  • symbol?:
  • synonym:
  • description?: autolysin

      descriptions from strain specific annotations:

    • autolysin
    • beta-N-acetylglucosaminidase, putative
    • mannosyl-glycoprotein endo-beta-N-acetylglucosamidase
    • N-acetylglucosaminidase
    • N-acetylmuramoyl-L-alanine amidase
    • exported protein
    • family 4 N-acetylmuramoyl-L-alanine amidase
    • mannosyl-glycoendo-beta-N-acetylglucosaminidase family protein
    • mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase
    • mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase family protein
    • mannosyl-glycoprotein endo-beta-N-glucosaminidase
    • peptidoglycan endo-beta-N-acetylglucosaminidase
  • strand?: -
  • coordinates?: 4713518..4714376
  • synteny block?: BlockID0034630
  • occurrence?: in 97% of 34 strains

sagB : membrane-associated peptidoglycan N-acetylglucosaminidase SagB [1]

• A crystal structure is available: 6FXP

  • 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_1730
    08BA02176:
    C248_1820
    11819-97:
    MS7_1777
    6850:
    RSAU_001630
    71193:
    ST398NM01_1825
    ECT-R 2:
    ECTR2_1611
    ED133:
    SAOV_1759
    ED98:
    SAAV_1785
    HO 5096 0412:
    SAEMRSA15_16840
    JH1:
    SaurJH1_1862
    JH9:
    SaurJH9_1827
    JKD6008:
    SAA6008_01747
    JKD6159:
    SAA6159_01696
    JSNZ:
    JSNZ_001764
    LGA251:
    SARLGA251_16620
    M013:
    M013TW_1788
    MRSA252:
    SAR1857
    MSHR1132:
    SAMSHR1132_16220
    MSSA476:
    SAS1698
    Mu3:
    SAHV_1760
    Mu50:
    SAV1775
    MW2:
    MW1715
    RF122:
    SAB1633c
    ST398:
    SAPIG1825
    T0131:
    SAT0131_01890
    TCH60:
    HMPREF0772_11380
    TW20:
    SATW20_17650
    USA300_TCH1516:
    USA300HOU_1765
    VC40:

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             MNKHKKGSIFGIIGLVVIFAVVSFLFFSMISDQIFFKHVKSDIKIEKLNVTLNDAAKKQI
    N315            MNKHKKGSIFGIIGLVVIFAVVSFLFFSMISDQIFFKHVKSDIKIEKLNVTLNDAAKKQI
    NCTC8325        MNKHKKGSIFGIIGLVVIFAVVSFLFFSMISDQIFFKHVKSDIKIEKLNVTLNDAAKKQI
    Newman          MNKHKKGSIFGIIGLVVIFAVVSFLFFSMISDQIFFKHVKSDIKIEKLNVTLNDAAKKQI
    USA300_FPR3757  MNKHKKGSIFGIIGLVVIFAVVSFLFFSMISDQIFFKHVKSDIKIEKLNVTLNDAAKKQI
                    ************************************************************

    COL             NNYTSQQVSNKKNDAWRDASATEIKSAMDSGTFIDNEKQKYQFLDLSKYQGIDKNRIKRM
    N315            NNYTSQQVSNKKNDAWRDASATEIKSAMDSGTFIDNEKQKYQFLDLSKYQGIDKNRIKRM
    NCTC8325        NNYTSQQVSNKKNDAWRDASATEIKSAMDSGTFIDNEKQKYQFLDLSKYQGIDKNRIKRM
    Newman          NNYTSQQVSNKKNDAWRDASATEIKSAMDSGTFIDNEKQKYQFLDLSKYQGIDKNRIKRM
    USA300_FPR3757  NNYTSQQVSNKKNDAWRDASATEIKSAMDSGTFIDNEKQKYQFLDLSKYQGIDKNRIKRM
                    ************************************************************

    COL             LVDRPTLLKHTDDFLKAAKDKHVNEVYLISHALLETGAVKSELANGVEIDGKKYYNFYGV
    N315            LVDRPTLLKHTDDFLKAAKDKHVNEVYLISHALLETGAVKSELANGVEIDGKKYYNFYGV
    NCTC8325        LVDRPTLLKHTDDFLKAAKDKHVNEVYLISHALLETGAVKSELANGVEIDGKKYYNFYGV
    Newman          LVDRPTLLKHTDDFLKAAKDKHVNEVYLISHALLETGAVKSELANGVEIDGKKYYNFYGV
    USA300_FPR3757  LVDRPTLLKHTDDFLKAAKDKHVNEVYLISHALLETGAVKSELANGVEIDGKKYYNFYGV
                    ************************************************************

    COL             GALDKDPIKTGAEYAKKHGWDTPEKAISGGADFIHKHFLSSTDQNTLYSMRWNPKNPGEH
    N315            GALDKDPIKTGAEYAKKHGWDTPEKAISGGADFIHKHFLSSTDQNTLYSMRWNPKNPGEH
    NCTC8325        GALDKDPIKTGAEYAKKHGWDTPEKAISGGADFIHKHFLSSTDQNTLYSMRWNPKNPGEH
    Newman          GALDKDPIKTGAEYAKKHGWDTPEKAISGGADFIHKHFLSSTDQNTLYSMRWNPKNPGEH
    USA300_FPR3757  GALDKDPIKTGAEYAKKHGWDTPEKAISGGADFIHKHFLSSTDQNTLYSMRWNPKNPGEH
                    ************************************************************

    COL             QYATDIKWAESNATIIADFYKNMKTEGKYFKYFVYKDDSKHLNK
    N315            QYATDIKWAESNATIIADFYKNMKTEGKYFKYFVYKDDSKHLNK
    NCTC8325        QYATDIKWAESNATIIADFYKNMKTEGKYFKYFVYKDDSKHLNK
    Newman          QYATDIKWAESNATIIADFYKNMKTEGKYFKYFVYKDDSKHLNK
    USA300_FPR3757  QYATDIKWAESNATIIADFYKNMKTEGKYFKYFVYKDDSKHLNK
                    ********************************************

  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)
    Sara Pintar, Jure Borišek, Aleksandra Usenik, Andrej Perdih, Dušan Turk
    Domain sliding of two Staphylococcus aureus N-acetylglucosaminidases enables their substrate-binding prior to its catalysis.
    Commun Biol: 2020, 3(1);178
    [PubMed:32313083] [WorldCat.org] [DOI] (I e)
    Yvonne G Y Chan, Matthew B Frankel, Dominique Missiakas, Olaf Schneewind
    SagB Glucosaminidase Is a Determinant of Staphylococcus aureus Glycan Chain Length, Antibiotic Susceptibility, and Protein Secretion.
    J Bacteriol: 2016, 198(7);1123-36
    [PubMed:26811319] [WorldCat.org] [DOI] (I e)