Q2G261 (SODM2_STAA8) Reviewed, UniProtKB/Swiss-Prot
Last modified July 9, 2014. Version 57. History...
Names and origin
|Protein names||Recommended name:|
Superoxide dismutase [Mn/Fe] 2
|Organism||Staphylococcus aureus (strain NCTC 8325) [Reference proteome] [HAMAP]|
|Taxonomic identifier||93061 [NCBI]|
|Taxonomic lineage||Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus ›|
|Sequence length||199 AA.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. May play a role in maintaining cell viability during the late-exponential and stationary phases of growth since it becomes a major source of activity under oxidative stress. Has a role in resisting external superoxide stress. Involved in acid tolerance and the acid-adaptive response. Mediates the derepression of perR regulon in the response to HOCl stress at low level of SOD activity By similarity. Ref.1 Ref.5
2 superoxide + 2 H+ = O2 + H2O2.
Binds 1 manganese or iron ion per subunit By similarity.
Homodimer. Can also form a heterodimer with SodA. Ref.4
Transcriptionally induced by externally generated superoxide stress in a manganese-dependent way. The presence of manganese increases SodA homodimer activity and simultaneously decreases SodM homodimer activity. This occurs primarily due to post-transcriptional effects, since the expression of the gene is independent of manganese availability in the absence of superoxide generating compounds. Ref.5
According to Ref.1 the levels of SodM activity and sodM expression are growth-phase dependent, occurring most during the late-exponential and stationary phases. This response is also dependent on the level of aeration with highest activity occurring under high aeration. SodM expression under low-aeration growth conditions is most abundant during the late-exponential phase while under high-aeration growth conditions is highest during the stationary phase.
Transcribed from a single sigmaA-type promoter (PM). Transcriptional data show an indirect repression of PM promoter by sigmaB which can also be involved in the post-transcriptional regulation of SodM homodimer activity.
Belongs to the iron/manganese superoxide dismutase family.
|Biological process||Stress response|
|Technical term||Complete proteome|
|Gene Ontology (GO)|
|Molecular_function||metal ion binding|
Inferred from electronic annotation. Source: UniProtKB-KWsuperoxide dismutase activity
Inferred from electronic annotation. Source: UniProtKB-EC
|Complete GO annotation...|
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Chain||1 – 199||199||Superoxide dismutase [Mn/Fe] 2||PRO_0000293965|
|Metal binding||27||1||Manganese or iron By similarity|
|Metal binding||81||1||Manganese or iron By similarity|
|Metal binding||161||1||Manganese or iron By similarity|
|Metal binding||165||1||Manganese or iron By similarity|
|Sequence conflict||61||1||D → G in AAG44813. Ref.1|
|||"Identification and characterization of a second superoxide dismutase gene (sodM) from Staphylococcus aureus."|
Wright Valderas M., Hart M.E.
J. Bacteriol. 183:3399-3407(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, EXPRESSION, SOD ACTIVITY.
|||"The Staphylococcus aureus NCTC 8325 genome."|
Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.
(In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.); Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington D.C. (2006)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 8325.
|||"Characterization of superoxide dismutase genes from Gram-positive bacteria by polymerase chain reaction using degenerate primers."|
Poyart C., Berche P., Trieu-Cuot P.
FEMS Microbiol. Lett. 131:41-45(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-160.
|||"The superoxide dismutase gene sodM is unique to Staphylococcus aureus: absence of sodM in coagulase-negative staphylococci."|
Wright Valderas M., Gatson J.W., Wreyford N., Hart M.E.
J. Bacteriol. 184:2465-2472(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SOD ACTIVITY, SUBUNIT.
|||"Role and regulation of the superoxide dismutases of Staphylococcus aureus."|
Karavolos M.H., Horsburgh M.J., Ingham E., Foster S.J.
Microbiology 149:2749-2758(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN OXIDATIVE STRESS RESISTANCE, EXPRESSION, REGULATION.
|AF273269 Genomic DNA. Translation: AAG44813.2.|
CP000253 Genomic DNA. Translation: ABD29276.1.
Z49245 Genomic DNA. Translation: CAA89212.1.
|RefSeq||YP_498694.1. NC_007795.1. |
3D structure databases
|SMR||Q2G261. Positions 3-198. |
Protein-protein interaction databases
Protocols and materials databases
Genome annotation databases
|EnsemblBacteria||ABD29276; ABD29276; SAOUHSC_00093. |
|PATRIC||19577814. VBIStaAur99865_0083. |
Enzyme and pathway databases
Family and domain databases
|InterPro||IPR001189. Mn/Fe_SOD. |
|PANTHER||PTHR11404. PTHR11404. 1 hit. |
|Pfam||PF02777. Sod_Fe_C. 1 hit. |
PF00081. Sod_Fe_N. 1 hit.
|PIRSF||PIRSF000349. SODismutase. 1 hit. |
|PRINTS||PR01703. MNSODISMTASE. |
|SUPFAM||SSF46609. SSF46609. 1 hit. |
SSF54719. SSF54719. 1 hit.
|PROSITE||PS00088. SOD_MN. 1 hit. |
|Accession||Primary (citable) accession number: Q2G261|
Secondary accession number(s): Q59806, Q9EZZ2
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Prokaryotic Protein Annotation Program|
Index of protein domains and families