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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//
