SODM1_STAA8
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 03-AUG-2022, entry version 96.
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; 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; 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; 1280.SAXN108_1575; -.
DR EnsemblBacteria; ABD30729; ABD30729; SAOUHSC_01653.
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 OMA; KWGSFDK; -.
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; 3.55.40.20; -; 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; 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
