⊟Summary[edit | edit source]
- pan ID?: SAUPAN006405000
- symbol?: msrA3
- synonym:
- description?: methionine sulfoxide reductase A
- methionine sulfoxide reductase A
- peptide-methionine (S)-S-oxide reductase
- Peptide methionine sulfoxide reductase MsrA
- methionine sulfoxide reductase A, MsrA
- peptide methionine sulfoxide reductase family protein
- peptide methionine sulfoxide reductase MsrA/msrB
- peptide methionine sulfoxide reductase msrA/msrB domain protein
descriptions from strain specific annotations:
- strand?: -
- coordinates?: 6456096..6456572
- synteny block?: BlockID0051120
- occurrence?: in 100% of 34 strains
msrA3 : peptide-methionine-(S)-sulfoxide reductase A3 [1]
Under conditions of oxidative stress, free sulfides (thioethers) in proteins containing methionine can be oxidized resulting in protein dysfunction. Peptide-methionine-sulfoxide reductases (MSRs) restore methionine to its reduced (functional) form. Staphylococci produce at least four MSRs. Since the sulfide group is prochiral, distinct enzymes are required to reduce the (S) [MsrA] and (R) [MsrB] enantiomers. MsrA1 and MsrB are induced under oxidative stresses and play a role in pathogenesis, virulence and response to host defenses. The roles of the other MSRs are less certain. MsrA2 may respond to sunlight-induced oxidative damage whereas MsrA3 may respond to stationary phase-associated oxidative damage.
⊟Orthologs[edit | edit source]
⊟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 MAVVYVAGGCLWGVEAFFATIPGIIHTEAGRANGRSSKLDGPYDGYAECVKLHFDDRMLT
N315 MVVVYVAGGCLWGVEAFFATIPGIIHTEAGRANGRSSKLDGPYDGYAECVKLHFDDRMLT
NCTC8325 MAVVYVAGGCLWGVEAFFATIPGIIHTEAGRANGRSSKLDGPYDGYAECVKLHFDDRMLT
Newman MAVVYVAGGCLWGVEAFFATIPGIIHTEAGRANGRSSKLDGPYDGYAECVKLHFDDRMLT
USA300_FPR3757 MAVVYVAGGCLWGVEAFFATIPGIIHTEAGRANGRSSKLDGPYDGYAECVKLHFDDRMLT
*.**********************************************************
COL ITDIMNYLFEIIDPYSVNQQGNDIGQKYRTGLYSCVDDHLIEARQFIERRKDRDQIAVEV
N315 ITDIMNYLFEIIDPYSVNQQGNDIGEKYRTGLYSCVDDHLIEARQFIERRKDRDQIAVEV
NCTC8325 ITDIMNYLFEIIDPYSVNQQGNDIGQKYRTGLYSCVDDHLIEARQFIERRKDRDQIAVEV
Newman ITDIMNYLFEIIDPYSVNQQGNDIGQKYRTGLYSCVDDHLIEARQFIERRKDRDQIAVEV
USA300_FPR3757 ITDIMNYLFEIIDPYSVNQQGNDIGQKYRTGLYSCVDDHLIEARQFIERRKDRDQIAVEV
*************************:**********************************
COL LPLSNYIKSAEEHQQHLEKYPEDMHMCHISKDLLNKYK
N315 LPLSNYIKSAEEHQQHLEKYPEDMHMCHISKDLLNKYK
NCTC8325 LPLSNYIKSAEEHQQHLEKYPEDMHMCHISKDLLNKYK
Newman LPLSNYIKSAEEHQQHLEKYPEDMHMCHISKDLLNKYK
USA300_FPR3757 LPLSNYIKSAEEHQQHLEKYPEDMHMCHISKDLLNKYK
**************************************
- ↑ Kuldeep Singh, Vineet K Singh
Expression of Four Methionine Sulfoxide Reductases in Staphylococcus aureus.
Int J Microbiol: 2012, 2012;719594
[PubMed:22272204] [WorldCat.org] [DOI] (I p)Vineet K Singh, Manisha Vaish, Trintje R Johansson, Kyle R Baum, Robert P Ring, Saumya Singh, Sanjay K Shukla, Jackob Moskovitz
Significance of four methionine sulfoxide reductases in Staphylococcus aureus.
PLoS One: 2015, 10(2);e0117594
[PubMed:25680075] [WorldCat.org] [DOI] (I e)Vineet K Singh, Kuldeep Singh, Kyle Baum
The Role of Methionine Sulfoxide Reductases in Oxidative Stress Tolerance and Virulence of Staphylococcus aureus and Other Bacteria.
Antioxidants (Basel): 2018, 7(10);
[PubMed:30274148] [WorldCat.org] [DOI] (P e)