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Database: UniProt
Entry: Q2G261
LinkDB: Q2G261
Original site: Q2G261 
ID   SODM2_STAA8             Reviewed;         199 AA.
AC   Q2G261; Q59806; Q9EZZ2;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   13-FEB-2019, entry version 81.
DE   RecName: Full=Superoxide dismutase [Mn/Fe] 2;
DE            EC=1.15.1.1;
GN   Name=sodM; OrderedLocusNames=SAOUHSC_00093;
OS   Staphylococcus aureus (strain NCTC 8325).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, EXPRESSION, AND SOD
RP   ACTIVITY.
RX   PubMed=11344148; DOI=10.1128/JB.183.11.3399-3407.2001;
RA   Wright Valderas M., Hart M.E.;
RT   "Identification and characterization of a second superoxide dismutase
RT   gene (sodM) from Staphylococcus aureus.";
RL   J. Bacteriol. 183:3399-3407(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W.,
RA   Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press,
RL   Washington D.C. (2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-160.
RX   PubMed=7557308; DOI=10.1016/0378-1097(95)00232-T;
RA   Poyart C., Berche P., Trieu-Cuot P.;
RT   "Characterization of superoxide dismutase genes from Gram-positive
RT   bacteria by polymerase chain reaction using degenerate primers.";
RL   FEMS Microbiol. Lett. 131:41-45(1995).
RN   [4]
RP   SOD ACTIVITY, AND SUBUNIT.
RX   PubMed=11948161; DOI=10.1128/JB.184.9.2465-2472.2002;
RA   Wright Valderas M., Gatson J.W., Wreyford N., Hart M.E.;
RT   "The superoxide dismutase gene sodM is unique to Staphylococcus
RT   aureus: absence of sodM in coagulase-negative staphylococci.";
RL   J. Bacteriol. 184:2465-2472(2002).
RN   [5]
RP   FUNCTION IN OXIDATIVE STRESS RESISTANCE, EXPRESSION, AND REGULATION.
RX   PubMed=14523108; DOI=10.1099/mic.0.26353-0;
RA   Karavolos M.H., Horsburgh M.J., Ingham E., Foster S.J.;
RT   "Role and regulation of the superoxide dismutases of Staphylococcus
RT   aureus.";
RL   Microbiology 149:2749-2758(2003).
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological
CC       systems. May play a role in maintaining cell viability during the
CC       late-exponential and stationary phases of growth since it becomes
CC       a major source of activity under oxidative stress. Has a role in
CC       resisting external superoxide stress. Involved in acid tolerance
CC       and the acid-adaptive response. Mediates the derepression of perR
CC       regulon in the response to HOCl stress at low level of SOD
CC       activity (By similarity). {ECO:0000250,
CC       ECO:0000269|PubMed:11344148, ECO:0000269|PubMed:14523108}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:18421; EC=1.15.1.1;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC       Note=Binds 1 Mn(2+) or Fe(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. Can also form a heterodimer with SodA.
CC       {ECO:0000269|PubMed:11948161}.
CC   -!- INDUCTION: Transcriptionally induced by externally generated
CC       superoxide stress in a manganese-dependent way. The presence of
CC       manganese increases SodA homodimer activity and simultaneously
CC       decreases SodM homodimer activity. This occurs primarily due to
CC       post-transcriptional effects, since the expression of the gene is
CC       independent of manganese availability in the absence of superoxide
CC       generating compounds.
CC   -!- MISCELLANEOUS: According to PubMed:11344148 the levels of SodM
CC       activity and sodM expression are growth-phase dependent, occurring
CC       most during the late-exponential and stationary phases. This
CC       response is also dependent on the level of aeration with highest
CC       activity occurring under high aeration. SodM expression under low-
CC       aeration growth conditions is most abundant during the late-
CC       exponential phase while under high-aeration growth conditions is
CC       highest during the stationary phase.
CC   -!- MISCELLANEOUS: Transcribed from a single sigmaA-type promoter
CC       (PM). Transcriptional data show an indirect repression of PM
CC       promoter by sigmaB which can also be involved in the post-
CC       transcriptional regulation of SodM homodimer activity.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; AF273269; AAG44813.2; -; Genomic_DNA.
DR   EMBL; CP000253; ABD29276.1; -; Genomic_DNA.
DR   EMBL; Z49245; CAA89212.1; -; Genomic_DNA.
DR   PIR; S54793; S54793.
DR   RefSeq; WP_000874681.1; NZ_LS483365.1.
DR   RefSeq; YP_498694.1; NC_007795.1.
DR   PDB; 5N57; X-ray; 2.30 A; A/B=1-199.
DR   PDBsum; 5N57; -.
DR   ProteinModelPortal; Q2G261; -.
DR   SMR; Q2G261; -.
DR   STRING; 93061.SAOUHSC_00093; -.
DR   EnsemblBacteria; ABD29276; ABD29276; SAOUHSC_00093.
DR   GeneID; 3919804; -.
DR   KEGG; sao:SAOUHSC_00093; -.
DR   PATRIC; fig|93061.5.peg.83; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013583; -.
DR   KO; K04564; -.
DR   OMA; HNQFWEM; -.
DR   BioCyc; GCF_000013425:G1I0R-87-MONOMER; -.
DR   BioCyc; SAUR93061:G1G5Y-87-MONOMER; -.
DR   PRO; PR:Q2G261; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.287.990; -; 1.
DR   Gene3D; 2.40.500.20; -; 1.
DR   InterPro; IPR001189; Mn/Fe_SOD.
DR   InterPro; IPR019833; Mn/Fe_SOD_BS.
DR   InterPro; IPR019832; Mn/Fe_SOD_C.
DR   InterPro; IPR019831; Mn/Fe_SOD_N.
DR   InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR   InterPro; IPR036314; SOD_C_sf.
DR   Pfam; PF02777; Sod_Fe_C; 1.
DR   Pfam; PF00081; Sod_Fe_N; 1.
DR   PIRSF; PIRSF000349; SODismutase; 1.
DR   PRINTS; PR01703; MNSODISMTASE.
DR   SUPFAM; SSF46609; SSF46609; 1.
DR   SUPFAM; SSF54719; SSF54719; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Iron; Manganese; Metal-binding;
KW   Oxidoreductase; Reference proteome; Stress response.
FT   CHAIN         1    199       Superoxide dismutase [Mn/Fe] 2.
FT                                /FTId=PRO_0000293965.
FT   METAL        27     27       Manganese or iron. {ECO:0000250}.
FT   METAL        81     81       Manganese or iron. {ECO:0000250}.
FT   METAL       161    161       Manganese or iron. {ECO:0000250}.
FT   METAL       165    165       Manganese or iron. {ECO:0000250}.
FT   CONFLICT     61     61       D -> G (in Ref. 1; AAG44813).
FT                                {ECO:0000305}.
FT   TURN         12     18       {ECO:0000244|PDB:5N57}.
FT   HELIX        21     29       {ECO:0000244|PDB:5N57}.
FT   HELIX        31     43       {ECO:0000244|PDB:5N57}.
FT   HELIX        47     50       {ECO:0000244|PDB:5N57}.
FT   HELIX        53     58       {ECO:0000244|PDB:5N57}.
FT   HELIX        59     62       {ECO:0000244|PDB:5N57}.
FT   HELIX        65     86       {ECO:0000244|PDB:5N57}.
FT   HELIX        97    106       {ECO:0000244|PDB:5N57}.
FT   HELIX       109    121       {ECO:0000244|PDB:5N57}.
FT   STRAND      125    134       {ECO:0000244|PDB:5N57}.
FT   STRAND      137    144       {ECO:0000244|PDB:5N57}.
FT   HELIX       149    152       {ECO:0000244|PDB:5N57}.
FT   STRAND      155    161       {ECO:0000244|PDB:5N57}.
FT   HELIX       164    166       {ECO:0000244|PDB:5N57}.
FT   HELIX       168    171       {ECO:0000244|PDB:5N57}.
FT   HELIX       175    183       {ECO:0000244|PDB:5N57}.
FT   HELIX       188    198       {ECO:0000244|PDB:5N57}.
SQ   SEQUENCE   199 AA;  23041 MW;  388566FB9943C635 CRC64;
     MAFKLPNLPY AYDALEPYID QRTMEFHHDK HHNTYVTKLN ATVEGTELEH QSLADMIANL
     DKVPEAMRMS VRNNGGGHFN HSLFWEILSP NSEEKGGVID DIKAQWGTLD EFKNEFANKA
     TTLFGSGWTW LVVNDGKLEI VTTPNQDNPL TEGKTPILLF DVWEHAYYLK YQNKRPDYMT
     AFWNIVNWKK VDELYQAAK
//
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