ID   SODM1_STAA8             Reviewed;         199 AA.
AC   P0A0J3; Q2FY20; Q9Z5W5;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   RecName: Full=Superoxide dismutase [Mn] 1;
DE            EC=1.15.1.1;
GN   Name=sodA; OrderedLocusNames=SAOUHSC_01653;
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], EXPRESSION, ENZYMATIC ACTIVITY,
RP   COFACTOR, AND FUNCTION.
RX   PubMed=10383955; DOI=10.1128/jb.181.13.3898-3903.1999;
RA   Clements M.O., Watson S.P., Foster S.J.;
RT   "Characterization of the major superoxide dismutase of Staphylococcus
RT   aureus and its role in starvation survival, stress resistance, and
RT   pathogenicity.";
RL   J. Bacteriol. 181:3898-3903(1999).
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   ENZYMATIC 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 gene
RT   (sodM) from Staphylococcus aureus.";
RL   J. Bacteriol. 183:3399-3407(2001).
RN   [4]
RP   ENZYMATIC 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).
RN   [6]
RP   FUNCTION IN REGULATION OF PERR REGULON.
RX   PubMed=16514164; DOI=10.1099/mic.0.28385-0;
RA   Maalej S., Dammak I., Dukan S.;
RT   "The impairment of superoxide dismutase coordinates the derepression of the
RT   perR regulon in the response of Staphylococcus aureus to HOCl stress.";
RL   Microbiology 152:855-861(2006).
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological systems.
CC       May play a role in maintaining cell viability throughout all stages of
CC       growth, but may be the major SOD activity in the exponential growth-
CC       phase. Has a role in resisting external superoxide stress. Involved in
CC       acid tolerance and the acid-adaptive response. Mediates the
CC       derepression of perR regulon in the response to HOCl stress when the
CC       level of SOD activity is low. {ECO:0000269|PubMed:10383955,
CC       ECO:0000269|PubMed:14523108, ECO:0000269|PubMed:16514164}.
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:0000269|PubMed:10383955, ECO:0000269|PubMed:11344148,
CC         ECO:0000269|PubMed:11948161};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. Can also form a heterodimer with SodM.
CC       {ECO:0000269|PubMed:11948161}.
CC   -!- INDUCTION: Transcriptionally induced by internally 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:10383955 the levels of SodA activity
CC       and sodA expression are growth-phase dependent, occurring most during
CC       post-exponential phase. This response was also dependent on the level
CC       of aeration, with highest activity and expression occurring under high
CC       aeration.
CC   -!- MISCELLANEOUS: Transcribed from two sigma-A-type promoters (PA1 and
CC       PA2). Transcriptional data show an indirect repression of PA1 promoter
CC       by sigma-B.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000305}.
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DR   EMBL; AF121672; AAD17309.1; -; Genomic_DNA.
DR   EMBL; CP000253; ABD30729.1; -; Genomic_DNA.
DR   RefSeq; WP_000863556.1; NZ_LS483365.1.
DR   RefSeq; YP_500165.1; NC_007795.1.
DR   PDB; 5N56; X-ray; 2.07 A; A/B=1-199.
DR   PDB; 6EX3; X-ray; 2.20 A; A/B/C/D=1-199.
DR   PDB; 6QV9; X-ray; 1.80 A; A/B=1-199.
DR   PDBsum; 5N56; -.
DR   PDBsum; 6EX3; -.
DR   PDBsum; 6QV9; -.
DR   AlphaFoldDB; P0A0J3; -.
DR   SMR; P0A0J3; -.
DR   STRING; 93061.SAOUHSC_01653; -.
DR   PaxDb; 1280-SAXN108_1575; -.
DR   GeneID; 3920105; -.
DR   KEGG; sao:SAOUHSC_01653; -.
DR   PATRIC; fig|93061.5.peg.1504; -.
DR   eggNOG; COG0605; Bacteria.
DR   HOGENOM; CLU_031625_0_1_9; -.
DR   OrthoDB; 9803125at2; -.
DR   PRO; PR:P0A0J3; -.
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; Manganese; Metal-binding; Oxidoreductase; Reference proteome;
KW   Stress response.
FT   CHAIN           1..199
FT                   /note="Superoxide dismutase [Mn] 1"
FT                   /id="PRO_0000160075"
FT   BINDING         27
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         81
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         161
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         165
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   TURN            12..18
FT                   /evidence="ECO:0007829|PDB:6QV9"
FT   HELIX           21..29
FT                   /evidence="ECO:0007829|PDB:6QV9"
FT   HELIX           31..43
FT                   /evidence="ECO:0007829|PDB:6QV9"
FT   STRAND          44..46
FT                   /evidence="ECO:0007829|PDB:6EX3"
FT   HELIX           47..50
FT                   /evidence="ECO:0007829|PDB:6QV9"
FT   HELIX           53..58
FT                   /evidence="ECO:0007829|PDB:6QV9"
FT   HELIX           60..62
FT                   /evidence="ECO:0007829|PDB:6QV9"
FT   HELIX           65..86
FT                   /evidence="ECO:0007829|PDB:6QV9"
FT   HELIX           97..106
FT                   /evidence="ECO:0007829|PDB:6QV9"
FT   HELIX           109..121
FT                   /evidence="ECO:0007829|PDB:6QV9"
FT   STRAND          125..134
FT                   /evidence="ECO:0007829|PDB:6QV9"
FT   STRAND          137..144
FT                   /evidence="ECO:0007829|PDB:6QV9"
FT   HELIX           149..152
FT                   /evidence="ECO:0007829|PDB:6QV9"
FT   STRAND          155..161
FT                   /evidence="ECO:0007829|PDB:6QV9"
FT   HELIX           164..166
FT                   /evidence="ECO:0007829|PDB:6QV9"
FT   HELIX           168..171
FT                   /evidence="ECO:0007829|PDB:6QV9"
FT   HELIX           175..182
FT                   /evidence="ECO:0007829|PDB:6QV9"
FT   HELIX           183..185
FT                   /evidence="ECO:0007829|PDB:6QV9"
FT   HELIX           188..196
FT                   /evidence="ECO:0007829|PDB:6QV9"
SQ   SEQUENCE   199 AA;  22711 MW;  F2CEC7B4701AC559 CRC64;
     MAFELPKLPY AFDALEPHFD KETMEIHHDR HHNTYVTKLN AAVEGTDLES KSIEEIVANL
     DSVPANIQTA VRNNGGGHLN HSLFWELLSP NSEEKGTVVE KIKEQWGSLE EFKKEFADKA
     AARFGSGWAW LVVNNGQLEI VTTPNQDNPL TEGKTPILGL DVWEHAYYLK YQNKRPDYIG
     AFWNVVNWEK VDELYNATK
//