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Protein

Superoxide dismutase [Mn/Fe] 2

Gene

sodM

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 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).By similarity2 Publications

Catalytic activityi

2 superoxide + 2 H+ = O2 + H2O2.

Cofactori

Mn2+By similarity, Fe2+By similarityNote: Binds 1 Mn2+ or Fe2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi27Manganese or ironBy similarity1
Metal bindingi81Manganese or ironBy similarity1
Metal bindingi161Manganese or ironBy similarity1
Metal bindingi165Manganese or ironBy similarity1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Stress response

Keywords - Ligandi

Iron, Manganese, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Mn/Fe] 2 (EC:1.15.1.1)
Gene namesi
Name:sodM
Ordered Locus Names:SAOUHSC_00093
OrganismiStaphylococcus aureus (strain NCTC 8325)
Taxonomic identifieri93061 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000008816 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002939651 – 199Superoxide dismutase [Mn/Fe] 2Add BLAST199

Expressioni

Inductioni

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.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi93061.SAOUHSC_00093.

Structurei

3D structure databases

ProteinModelPortaliQ2G261.
SMRiQ2G261.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CK4. Bacteria.
COG0605. LUCA.
HOGENOMiHOG000013583.
KOiK04564.
OMAiDSLINWD.

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.

Q2G261-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFKLPNLPY AYDALEPYID QRTMEFHHDK HHNTYVTKLN ATVEGTELEH
60 70 80 90 100
QSLADMIANL DKVPEAMRMS VRNNGGGHFN HSLFWEILSP NSEEKGGVID
110 120 130 140 150
DIKAQWGTLD EFKNEFANKA TTLFGSGWTW LVVNDGKLEI VTTPNQDNPL
160 170 180 190
TEGKTPILLF DVWEHAYYLK YQNKRPDYMT AFWNIVNWKK VDELYQAAK
Length:199
Mass (Da):23,041
Last modified:March 21, 2006 - v1
Checksum:i388566FB9943C635
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti61D → G in AAG44813 (PubMed:11344148).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF273269 Genomic DNA. Translation: AAG44813.2.
CP000253 Genomic DNA. Translation: ABD29276.1.
Z49245 Genomic DNA. Translation: CAA89212.1.
PIRiS54793.
RefSeqiWP_000874681.1. NC_007795.1.
YP_498694.1. NC_007795.1.

Genome annotation databases

EnsemblBacteriaiABD29276; ABD29276; SAOUHSC_00093.
GeneIDi28379553.
3919804.
KEGGisao:SAOUHSC_00093.
PATRICi19577814. VBIStaAur99865_0083.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF273269 Genomic DNA. Translation: AAG44813.2.
CP000253 Genomic DNA. Translation: ABD29276.1.
Z49245 Genomic DNA. Translation: CAA89212.1.
PIRiS54793.
RefSeqiWP_000874681.1. NC_007795.1.
YP_498694.1. NC_007795.1.

3D structure databases

ProteinModelPortaliQ2G261.
SMRiQ2G261.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi93061.SAOUHSC_00093.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABD29276; ABD29276; SAOUHSC_00093.
GeneIDi28379553.
3919804.
KEGGisao:SAOUHSC_00093.
PATRICi19577814. VBIStaAur99865_0083.

Phylogenomic databases

eggNOGiENOG4105CK4. Bacteria.
COG0605. LUCA.
HOGENOMiHOG000013583.
KOiK04564.
OMAiDSLINWD.

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...

Entry informationi

Entry nameiSODM2_STAA8
AccessioniPrimary (citable) accession number: Q2G261
Secondary accession number(s): Q59806, Q9EZZ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: March 21, 2006
Last modified: November 2, 2016
This is version 70 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:11344148 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.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.