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Database: UniProt
Entry: P0A0J3
LinkDB: P0A0J3
Original site: P0A0J3 
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   13-FEB-2019, entry version 80.
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).
OC   Bacteria; Firmicutes; 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;
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;
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   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
RT   gene (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
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).
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
RT   of the perR regulon in the response of Staphylococcus aureus to HOCl
RT   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
CC       systems. May play a role in maintaining cell viability throughout
CC       all stages of growth, but may be the major SOD activity in the
CC       exponential growth-phase. Has a role in resisting external
CC       superoxide stress. Involved in acid tolerance and the acid-
CC       adaptive response. Mediates the derepression of perR regulon in
CC       the response to HOCl stress when the level of SOD activity is low.
CC       {ECO:0000269|PubMed:10383955, ECO:0000269|PubMed:14523108,
CC       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,
CC         ECO:0000269|PubMed:11344148, 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
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:10383955 the levels of SodA
CC       activity and sodA expression are growth-phase dependent, occurring
CC       most during post-exponential phase. This response was also
CC       dependent on the level of aeration, with highest activity and
CC       expression occurring under high aeration.
CC   -!- MISCELLANEOUS: Transcribed from two sigma-A-type promoters (PA1
CC       and PA2). Transcriptional data show an indirect repression of PA1
CC       promoter by sigma-B.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
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   PDBsum; 5N56; -.
DR   ProteinModelPortal; P0A0J3; -.
DR   SMR; P0A0J3; -.
DR   STRING; 93061.SAOUHSC_01653; -.
DR   EnsemblBacteria; ABD30729; ABD30729; SAOUHSC_01653.
DR   GeneID; 3920105; -.
DR   KEGG; sao:SAOUHSC_01653; -.
DR   PATRIC; fig|93061.5.peg.1504; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013583; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   BioCyc; GCF_000013425:G1I0R-1537-MONOMER; -.
DR   BioCyc; SAUR93061:G1G5Y-1537-MONOMER; -.
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; -; 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; Manganese; Metal-binding;
KW   Oxidoreductase; Reference proteome; Stress response.
FT   CHAIN         1    199       Superoxide dismutase [Mn] 1.
FT                                /FTId=PRO_0000160075.
FT   METAL        27     27       Manganese. {ECO:0000250}.
FT   METAL        81     81       Manganese. {ECO:0000250}.
FT   METAL       161    161       Manganese. {ECO:0000250}.
FT   METAL       165    165       Manganese. {ECO:0000250}.
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
//
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