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   27-MAR-2024, entry version 106.
DE   RecName: Full=Superoxide dismutase [Mn/Fe] 2;
DE            EC=1.15.1.1 {ECO:0000305|PubMed:11344148, ECO:0000305|PubMed:11948161};
GN   Name=sodM; OrderedLocusNames=SAOUHSC_00093;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   INDUCTION.
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 gene
RT   (sodM) from Staphylococcus aureus.";
RL   J. Bacteriol. 183:3399-3407(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., 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, Washington
RL   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 bacteria
RT   by polymerase chain reaction using degenerate primers.";
RL   FEMS Microbiol. Lett. 131:41-45(1995).
RN   [4]
RP   CATALYTIC 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 aureus:
RT   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 systems.
CC       Catalyzes the dismutation of superoxide anion radicals into O2 and H2O2
CC       by successive reduction and oxidation of the transition metal ion at
CC       the active site. May play a role in maintaining cell viability during
CC       the late-exponential and stationary phases of growth since it becomes a
CC       major source of activity under oxidative stress. Has a role in
CC       resisting external superoxide stress. Involved in acid tolerance and
CC       the acid-adaptive response. Mediates the derepression of perR regulon
CC       in the response to HOCl stress at low level of SOD activity (By
CC       similarity). {ECO:0000250, ECO:0000269|PubMed:11344148,
CC       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         Evidence={ECO:0000305|PubMed:11344148, ECO:0000305|PubMed:11948161};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20697;
CC         Evidence={ECO:0000305|PubMed:11344148, ECO:0000305|PubMed:11948161};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:P80293};
CC       Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC         Evidence={ECO:0000250|UniProtKB:P80293};
CC       Note=Binds 1 Mn(2+) or Fe(3+) ion per subunit.
CC       {ECO:0000250|UniProtKB:P80293};
CC   -!- SUBUNIT: Homodimer. Can also form a heterodimer with SodA.
CC       {ECO:0000269|PubMed:11948161}.
CC   -!- INDUCTION: Transcriptionally induced by externally generated superoxide
CC       stress in a manganese-dependent way. The presence of manganese
CC       increases SodA homodimer activity and simultaneously decreases SodM
CC       homodimer activity. This occurs primarily due to post-transcriptional
CC       effects, since the expression of the gene is independent of manganese
CC       availability in the absence of superoxide generating compounds.
CC   -!- MISCELLANEOUS: According to PubMed:11344148 the levels of SodM activity
CC       and sodM expression are growth-phase dependent, occurring most during
CC       the late-exponential and stationary phases. This response is also
CC       dependent on the level of aeration with highest activity occurring
CC       under high aeration. SodM expression under low-aeration growth
CC       conditions is most abundant during the late-exponential phase while
CC       under high-aeration growth conditions is highest during the stationary
CC       phase.
CC   -!- MISCELLANEOUS: Transcribed from a single sigmaA-type promoter (PM).
CC       Transcriptional data show an indirect repression of PM promoter by
CC       sigmaB which can also be involved in the post-transcriptional
CC       regulation of SodM homodimer activity.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000305}.
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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   PDB; 6EX4; X-ray; 2.40 A; A/B=1-199.
DR   PDB; 6EX5; X-ray; 1.75 A; A/B=2-199.
DR   PDB; 6QV8; X-ray; 1.50 A; A/B=1-199.
DR   PDBsum; 5N57; -.
DR   PDBsum; 6EX4; -.
DR   PDBsum; 6EX5; -.
DR   PDBsum; 6QV8; -.
DR   AlphaFoldDB; Q2G261; -.
DR   SMR; Q2G261; -.
DR   STRING; 93061.SAOUHSC_00093; -.
DR   PaxDb; 1280-SAXN108_0119; -.
DR   GeneID; 3919804; -.
DR   KEGG; sao:SAOUHSC_00093; -.
DR   PATRIC; fig|93061.5.peg.83; -.
DR   eggNOG; COG0605; Bacteria.
DR   HOGENOM; CLU_031625_0_0_9; -.
DR   OrthoDB; 9803125at2; -.
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; Fe,Mn superoxide dismutase (SOD) domain; 1.
DR   Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 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   PANTHER; PTHR43595; 37S RIBOSOMAL PROTEIN S26, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43595:SF2; 37S RIBOSOMAL PROTEIN S26, MITOCHONDRIAL; 1.
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; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1.
DR   SUPFAM; SSF46609; Fe,Mn superoxide dismutase (SOD), N-terminal domain; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Iron; Manganese; Metal-binding; Oxidoreductase;
KW   Reference proteome; Stress response.
FT   CHAIN           1..199
FT                   /note="Superoxide dismutase [Mn/Fe] 2"
FT                   /id="PRO_0000293965"
FT   BINDING         27
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000250|UniProtKB:P80293"
FT   BINDING         27
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P80293"
FT   BINDING         81
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000250|UniProtKB:P80293"
FT   BINDING         81
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P80293"
FT   BINDING         161
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000250|UniProtKB:P80293"
FT   BINDING         161
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P80293"
FT   BINDING         165
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000250|UniProtKB:P80293"
FT   BINDING         165
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P80293"
FT   CONFLICT        61
FT                   /note="D -> G (in Ref. 1; AAG44813)"
FT                   /evidence="ECO:0000305"
FT   TURN            12..18
FT                   /evidence="ECO:0007829|PDB:6QV8"
FT   HELIX           21..29
FT                   /evidence="ECO:0007829|PDB:6QV8"
FT   HELIX           31..43
FT                   /evidence="ECO:0007829|PDB:6QV8"
FT   TURN            47..50
FT                   /evidence="ECO:0007829|PDB:6QV8"
FT   HELIX           53..58
FT                   /evidence="ECO:0007829|PDB:6QV8"
FT   HELIX           60..62
FT                   /evidence="ECO:0007829|PDB:6QV8"
FT   HELIX           65..87
FT                   /evidence="ECO:0007829|PDB:6QV8"
FT   HELIX           97..106
FT                   /evidence="ECO:0007829|PDB:6QV8"
FT   HELIX           109..122
FT                   /evidence="ECO:0007829|PDB:6QV8"
FT   STRAND          125..134
FT                   /evidence="ECO:0007829|PDB:6QV8"
FT   STRAND          137..144
FT                   /evidence="ECO:0007829|PDB:6QV8"
FT   HELIX           149..152
FT                   /evidence="ECO:0007829|PDB:6QV8"
FT   STRAND          155..161
FT                   /evidence="ECO:0007829|PDB:6QV8"
FT   HELIX           164..166
FT                   /evidence="ECO:0007829|PDB:6QV8"
FT   HELIX           168..171
FT                   /evidence="ECO:0007829|PDB:6QV8"
FT   HELIX           175..182
FT                   /evidence="ECO:0007829|PDB:6QV8"
FT   HELIX           183..185
FT                   /evidence="ECO:0007829|PDB:6QV8"
FT   HELIX           188..198
FT                   /evidence="ECO:0007829|PDB:6QV8"
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
//