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⊟Summary[edit | edit source]
- pan ID?: SAUPAN004467000
- symbol?: —
- synonym:
- description?: autolysin
- 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
descriptions from strain specific annotations:
- 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]
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
********************************************
- ↑ 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)