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P0A0J3 (SODM1_STAA8) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 55. 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] 1

EC=1.15.1.1
Gene names
Name:sodA
Ordered Locus Names:SAOUHSC_01653
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 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

Catalytic activity

2 superoxide + 2 H+ = O2 + H2O2. Ref.1 Ref.3 Ref.4

Cofactor

Binds 1 manganese ion per subunit By similarity. Ref.1

Subunit structure

Homodimer. Can also form a heterodimer with SodM. Ref.4

Induction

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

Miscellaneous

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.

Sequence similarities

Belongs to the iron/manganese superoxide dismutase family.

Ontologies

Keywords
   Biological processStress response
   LigandManganese
Metal-binding
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processresponse to stress

Inferred from electronic annotation. Source: UniProtKB-KW

superoxide metabolic process

Inferred from electronic annotation. Source: InterPro

   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] 1
PRO_0000160075

Sites

Metal binding271Manganese By similarity
Metal binding811Manganese By similarity
Metal binding1611Manganese By similarity
Metal binding1651Manganese By similarity

Sequences

Sequence LengthMass (Da)Tools
P0A0J3 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: F2CEC7B4701AC559

FASTA19922,711
        10         20         30         40         50         60 
MAFELPKLPY AFDALEPHFD KETMEIHHDR HHNTYVTKLN AAVEGTDLES KSIEEIVANL 

        70         80         90        100        110        120 
DSVPANIQTA VRNNGGGHLN HSLFWELLSP NSEEKGTVVE KIKEQWGSLE EFKKEFADKA 

       130        140        150        160        170        180 
AARFGSGWAW LVVNNGQLEI VTTPNQDNPL TEGKTPILGL DVWEHAYYLK YQNKRPDYIG 

       190 
AFWNVVNWEK VDELYNATK 

« Hide

References

« Hide 'large scale' references
[1]"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.
[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]"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.
[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: ENZYMATIC 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.
[6]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF121672 Genomic DNA. Translation: AAD17309.1.
CP000253 Genomic DNA. Translation: ABD30729.1.
RefSeqYP_500165.1. NC_007795.1.

3D structure databases

ProteinModelPortalP0A0J3.
SMRP0A0J3. Positions 2-196.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING93061.SAOUHSC_01653.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD30729; ABD30729; SAOUHSC_01653.
GeneID3920105.
KEGGsao:SAOUHSC_01653.
PATRIC19580689. VBIStaAur99865_1504.

Phylogenomic databases

eggNOGCOG0605.
HOGENOMHOG000013583.
KOK04564.
OMADYISAFW.
OrthoDBEOG63NMNT.
ProtClustDBCLSK884424.

Enzyme and pathway databases

BioCycSAUR93061:GIWJ-1579-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 nameSODM1_STAA8
AccessionPrimary (citable) accession number: P0A0J3
Secondary accession number(s): Q2FY20, Q9Z5W5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2005
Last modified: November 13, 2013
This is version 55 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