P0A0J3 (SODM1_STAA8) Reviewed, UniProtKB/Swiss-Prot
Last modified May 1, 2013. Version 53. History...
Names and origin
|Protein names||Recommended name:|
Superoxide dismutase [Mn] 1
|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 throughout all stages of growth, but may be the major SOD activity in the exponential growth-phase. 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 when the level of SOD activity is low. Ref.1 Ref.5 Ref.6
Binds 1 manganese ion per subunit By similarity. Ref.1
Homodimer. Can also form a heterodimer with SodM. Ref.4
Transcriptionally induced by internally 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 SodA activity and sodA expression are growth-phase dependent, occurring most during post-exponential phase. This response was also dependent on the level of aeration, with highest activity and expression occurring under high aeration.
Transcribed from two sigma-A-type promoters (PA1 and PA2). Transcriptional data show an indirect repression of PA1 promoter by sigma-B.
Belongs to the iron/manganese superoxide dismutase family.
|Biological process||Stress response|
|Technical term||Complete proteome|
|Gene Ontology (GO)|
|Biological_process||response to stress|
Inferred from electronic annotation. Source: UniProtKB-KWsuperoxide metabolic process
Inferred from electronic annotation. Source: InterPro
|Molecular_function||metal ion binding|
Inferred from electronic annotation. Source: UniProtKB-KWsuperoxide dismutase activity
Inferred from electronic annotation. Source: EC
|Complete GO annotation...|
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Chain||1 – 199||199||Superoxide dismutase [Mn] 1||PRO_0000160075|
|Metal binding||27||1||Manganese By similarity|
|Metal binding||81||1||Manganese By similarity|
|Metal binding||161||1||Manganese By similarity|
|Metal binding||165||1||Manganese By similarity|
|||"Characterization of the major superoxide dismutase of Staphylococcus aureus and its role in starvation survival, stress resistance, and pathogenicity."|
Clements M.O., Watson S.P., Foster S.J.
J. Bacteriol. 181:3898-3903(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], EXPRESSION, ENZYMATIC ACTIVITY, COFACTOR, FUNCTION.
|||"The Staphylococcus aureus NCTC8325 genome."|
Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 8325.
|||"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: ENZYMATIC ACTIVITY.
|||"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: ENZYMATIC 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.
|||"The impairment of superoxide dismutase coordinates the derepression of the perR regulon in the response of Staphylococcus aureus to HOCl stress."|
Maalej S., Dammak I., Dukan S.
Microbiology 152:855-861(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN REGULATION OF PERR REGULON.
|AF121672 Genomic DNA. Translation: AAD17309.1.|
CP000253 Genomic DNA. Translation: ABD30729.1.
|RefSeq||YP_500165.1. NC_007795.1. |
3D structure databases
|SMR||P0A0J3. Positions 2-196. |
Protein-protein interaction databases
Protocols and materials databases
Genome annotation databases
|EnsemblBacteria||ABD30729; ABD30729; SAOUHSC_01653. |
|PATRIC||19580689. VBIStaAur99865_1504. |
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. SODismutase. 1 hit. |
SSF54719. SODismutase. 1 hit.
|PROSITE||PS00088. SOD_MN. 1 hit. |
|Accession||Primary (citable) accession number: P0A0J3|
Secondary accession number(s): Q2FY20, Q9Z5W5
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Prokaryotic Protein Annotation Program|
Index of protein domains and families