Q2G261 (SODM2_STAA8) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 53.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Superoxide dismutase [Mn/Fe] 2 EC=1.15.1.1 | ||||
| Gene names |
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| Organism | Staphylococcus aureus (strain NCTC 8325) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 93061 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus › ![]() |
Protein attributes
| Sequence length | 199 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | 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 |
| Catalytic activity | 2 superoxide + 2 H+ = O2 + H2O2. |
| Cofactor | Binds 1 manganese or iron ion per subunit By similarity. |
| Subunit structure | Homodimer. Can also form a heterodimer with SodA. Ref.4 |
| Induction | 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 |
| Miscellaneous | 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. |
| Sequence similarities | Belongs to the iron/manganese superoxide dismutase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Stress response |
| Ligand | Iron Manganese Metal-binding |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | response to stress Inferred from electronic annotation. Source: UniProtKB-KW superoxide metabolic processInferred from electronic annotation. Source: InterPro |
| Molecular_function | metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW superoxide dismutase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 199 | 199 | Superoxide dismutase [Mn/Fe] 2 | PRO_0000293965 | |||||
Sites | |||||||||
| 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 | ||||||
Experimental info | |||||||||
| Sequence conflict | 61 | 1 | D → G in AAG44813. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [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. |
| [2] | "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. |
| [3] | "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. |
| [4] | "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. |
| [5] | "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. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF273269 Genomic DNA. Translation: AAG44813.2. CP000253 Genomic DNA. Translation: ABD29276.1. Z49245 Genomic DNA. Translation: CAA89212.1. |
| PIR | S54793. |
| RefSeq | YP_498694.1. NC_007795.1. |
3D structure databases | |
| ProteinModelPortal | Q2G261. |
| SMR | Q2G261. Positions 3-198. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 93061.SAOUHSC_00093. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ABD29276; ABD29276; SAOUHSC_00093. |
| GeneID | 3919804. |
| KEGG | sao:SAOUHSC_00093. |
| PATRIC | 19577814. VBIStaAur99865_0083. |
Phylogenomic databases | |
| eggNOG | COG0605. |
| HOGENOM | HOG000013583. |
| KO | K04564. |
| OMA | KAWWNTV. |
| ProtClustDB | CLSK884424. |
Enzyme and pathway databases | |
| BioCyc | SAUR93061:GIWJ-88-MONOMER. |
Family and domain databases | |
| InterPro | IPR001189. Mn/Fe_SOD. IPR019833. Mn/Fe_SOD_BS. IPR019832. Mn/Fe_SOD_C. IPR019831. Mn/Fe_SOD_N. [Graphical view] |
| PANTHER | PTHR11404. PTHR11404. 1 hit. |
| Pfam | PF02777. Sod_Fe_C. 1 hit. PF00081. Sod_Fe_N. 1 hit. [Graphical view] |
| PIRSF | PIRSF000349. SODismutase. 1 hit. |
| PRINTS | PR01703. MNSODISMTASE. |
| SUPFAM | SSF46609. SODismutase. 1 hit. SSF54719. SODismutase. 1 hit. |
| PROSITE | PS00088. SOD_MN. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SODM2_STAA8 | ||||||||
| Accession | Primary (citable) accession number: Q2G261 Secondary accession number(s): Q59806, Q9EZZ2 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
