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Q2G261 (SODM2_STAA8) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Superoxide dismutase [Mn/Fe] 2

EC=1.15.1.1
Gene names
Name:sodM
Ordered Locus Names:SAOUHSC_00093
OrganismStaphylococcus aureus (strain NCTC 8325) [Reference proteome] [HAMAP]
Taxonomic identifier93061 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length199 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processStress response
   LigandIron
Manganese
Metal-binding
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

superoxide dismutase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 199199Superoxide dismutase [Mn/Fe] 2
PRO_0000293965

Sites

Metal binding271Manganese or iron By similarity
Metal binding811Manganese or iron By similarity
Metal binding1611Manganese or iron By similarity
Metal binding1651Manganese or iron By similarity

Experimental info

Sequence conflict611D → G in AAG44813. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q2G261 [UniParc].

Last modified March 21, 2006. Version 1.
Checksum: 388566FB9943C635

FASTA19923,041
        10         20         30         40         50         60 
MAFKLPNLPY AYDALEPYID QRTMEFHHDK HHNTYVTKLN ATVEGTELEH QSLADMIANL 

        70         80         90        100        110        120 
DKVPEAMRMS VRNNGGGHFN HSLFWEILSP NSEEKGGVID DIKAQWGTLD EFKNEFANKA 

       130        140        150        160        170        180 
TTLFGSGWTW LVVNDGKLEI VTTPNQDNPL TEGKTPILLF DVWEHAYYLK YQNKRPDYMT 

       190 
AFWNIVNWKK VDELYQAAK 

« Hide

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 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.
[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.
PIRS54793.
RefSeqYP_498694.1. NC_007795.1.

3D structure databases

ProteinModelPortalQ2G261.
SMRQ2G261. Positions 3-198.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING93061.SAOUHSC_00093.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD29276; ABD29276; SAOUHSC_00093.
GeneID3919804.
KEGGsao:SAOUHSC_00093.
PATRIC19577814. VBIStaAur99865_0083.

Phylogenomic databases

eggNOGCOG0605.
HOGENOMHOG000013583.
KOK04564.
OMADSLINWD.
OrthoDBEOG63NMNT.

Enzyme and pathway databases

BioCycSAUR93061:GIWJ-88-MONOMER.

Family and domain databases

InterProIPR001189. Mn/Fe_SOD.
IPR019833. Mn/Fe_SOD_BS.
IPR019832. Mn/Fe_SOD_C.
IPR019831. Mn/Fe_SOD_N.
[Graphical view]
PANTHERPTHR11404. PTHR11404. 1 hit.
PfamPF02777. Sod_Fe_C. 1 hit.
PF00081. Sod_Fe_N. 1 hit.
[Graphical view]
PIRSFPIRSF000349. SODismutase. 1 hit.
PRINTSPR01703. MNSODISMTASE.
SUPFAMSSF46609. SSF46609. 1 hit.
SSF54719. SSF54719. 1 hit.
PROSITEPS00088. SOD_MN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSODM2_STAA8
AccessionPrimary (citable) accession number: Q2G261
Secondary accession number(s): Q59806, Q9EZZ2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: March 21, 2006
Last modified: July 9, 2014
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families