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Protein

Superoxide dismutase [Mn] 1

Gene

sodA

Organism
Staphylococcus aureus (strain NCTC 8325)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

2 superoxide + 2 H+ = O2 + H2O2.3 Publications

Cofactori

Mn2+By similarityNote: Binds 1 Mn2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi27 – 271ManganeseBy similarity
Metal bindingi81 – 811ManganeseBy similarity
Metal bindingi161 – 1611ManganeseBy similarity
Metal bindingi165 – 1651ManganeseBy similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. superoxide dismutase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Stress response

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciSAUR93061:GIWJ-1579-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Mn] 1 (EC:1.15.1.1)
Gene namesi
Name:sodA
Ordered Locus Names:SAOUHSC_01653
OrganismiStaphylococcus aureus (strain NCTC 8325)
Taxonomic identifieri93061 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000008816: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 199199Superoxide dismutase [Mn] 1PRO_0000160075Add
BLAST

Expressioni

Inductioni

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.

Interactioni

Subunit structurei

Homodimer. Can also form a heterodimer with SodM.1 Publication

Protein-protein interaction databases

STRINGi93061.SAOUHSC_01653.

Structurei

3D structure databases

ProteinModelPortaliP0A0J3.
SMRiP0A0J3. Positions 2-196.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0605.
HOGENOMiHOG000013583.
KOiK04564.
OMAiFWEVIAP.
OrthoDBiEOG63NMNT.

Family and domain databases

InterProiIPR001189. Mn/Fe_SOD.
IPR019833. Mn/Fe_SOD_BS.
IPR019832. Mn/Fe_SOD_C.
IPR019831. Mn/Fe_SOD_N.
[Graphical view]
PANTHERiPTHR11404. PTHR11404. 1 hit.
PfamiPF02777. Sod_Fe_C. 1 hit.
PF00081. Sod_Fe_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000349. SODismutase. 1 hit.
PRINTSiPR01703. MNSODISMTASE.
SUPFAMiSSF46609. SSF46609. 1 hit.
SSF54719. SSF54719. 1 hit.
PROSITEiPS00088. SOD_MN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A0J3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAFELPKLPY AFDALEPHFD KETMEIHHDR HHNTYVTKLN AAVEGTDLES
60 70 80 90 100
KSIEEIVANL DSVPANIQTA VRNNGGGHLN HSLFWELLSP NSEEKGTVVE
110 120 130 140 150
KIKEQWGSLE EFKKEFADKA AARFGSGWAW LVVNNGQLEI VTTPNQDNPL
160 170 180 190
TEGKTPILGL DVWEHAYYLK YQNKRPDYIG AFWNVVNWEK VDELYNATK
Length:199
Mass (Da):22,711
Last modified:March 1, 2005 - v1
Checksum:iF2CEC7B4701AC559
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF121672 Genomic DNA. Translation: AAD17309.1.
CP000253 Genomic DNA. Translation: ABD30729.1.
RefSeqiWP_000863556.1. NC_007795.1.
YP_500165.1. NC_007795.1.

Genome annotation databases

EnsemblBacteriaiABD30729; ABD30729; SAOUHSC_01653.
GeneIDi3920105.
KEGGisao:SAOUHSC_01653.
PATRICi19580689. VBIStaAur99865_1504.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF121672 Genomic DNA. Translation: AAD17309.1.
CP000253 Genomic DNA. Translation: ABD30729.1.
RefSeqiWP_000863556.1. NC_007795.1.
YP_500165.1. NC_007795.1.

3D structure databases

ProteinModelPortaliP0A0J3.
SMRiP0A0J3. Positions 2-196.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi93061.SAOUHSC_01653.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABD30729; ABD30729; SAOUHSC_01653.
GeneIDi3920105.
KEGGisao:SAOUHSC_01653.
PATRICi19580689. VBIStaAur99865_1504.

Phylogenomic databases

eggNOGiCOG0605.
HOGENOMiHOG000013583.
KOiK04564.
OMAiFWEVIAP.
OrthoDBiEOG63NMNT.

Enzyme and pathway databases

BioCyciSAUR93061:GIWJ-1579-MONOMER.

Family and domain databases

InterProiIPR001189. Mn/Fe_SOD.
IPR019833. Mn/Fe_SOD_BS.
IPR019832. Mn/Fe_SOD_C.
IPR019831. Mn/Fe_SOD_N.
[Graphical view]
PANTHERiPTHR11404. PTHR11404. 1 hit.
PfamiPF02777. Sod_Fe_C. 1 hit.
PF00081. Sod_Fe_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000349. SODismutase. 1 hit.
PRINTSiPR01703. MNSODISMTASE.
SUPFAMiSSF46609. SSF46609. 1 hit.
SSF54719. SSF54719. 1 hit.
PROSITEiPS00088. SOD_MN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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 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. "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.

Entry informationi

Entry nameiSODM1_STAA8
AccessioniPrimary (citable) accession number: P0A0J3
Secondary accession number(s): Q2FY20, Q9Z5W5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2005
Last modified: January 7, 2015
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

According to PubMed:10383955 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.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.