SODM_STRPN
ID SODM_STRPN Reviewed; 201 AA.
AC P0A4J6; O33757; O54268; O54269; Q59949; Q9R3B6; Q9R3B8; Q9S175; Q9S176;
AC Q9S177; Q9S447;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Superoxide dismutase [Mn];
DE EC=1.15.1.1;
GN Name=sodA; OrderedLocusNames=SP_0766;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=D39 / NCTC 7466 / Serotype 2;
RX PubMed=10768978; DOI=10.1128/iai.68.5.2819-2826.2000;
RA Yesilkaya H., Kadioglu A., Gingles N., Alexander J.E., Mitchell T.J.,
RA Andrew P.W.;
RT "Role of manganese-containing superoxide dismutase in oxidative stress and
RT virulence of Streptococcus pneumoniae.";
RL Infect. Immun. 68:2819-2826(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-162.
RC STRAIN=NEM667;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-162.
RC STRAIN=Various strains;
RX PubMed=9431917; DOI=10.1128/jcm.36.1.41-47.1998;
RA Poyart C., Quesne G., Coulon S., Berche P., Trieu-Cuot P.;
RT "Identification of streptococci to species level by sequencing the gene
RT encoding the manganese-dependent superoxide dismutase.";
RL J. Clin. Microbiol. 36:41-47(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-154.
RC STRAIN=1293, 1454, 1510, 1565, 1639, 3051, 3203, 653, 661, 872,
RC GTC261T / NCTC 7465T, YK-11, YK-12, YK-14, YK-20, and YK-5;
RX PubMed=10517614; DOI=10.1099/00221287-145-9-2605;
RA Kawamura Y., Whiley R.A., Shu S.E., Ezaki T., Hardie J.M.;
RT "Genetic approaches to the identification of the mitis group within the
RT genus Streptococcus.";
RL Microbiology 145:2605-2613(1999).
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 critical role against oxidative stress, affecting both the
CC survival and the virulence of S.pneumoniae.
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 -!- 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. {ECO:0000250}.
CC -!- INTERACTION:
CC P0A4J6; Q97SE5: gatC; NbExp=2; IntAct=EBI-2207137, EBI-2207053;
CC P0A4J6; Q97NV3: groES; NbExp=2; IntAct=EBI-2207137, EBI-2206949;
CC P0A4J6; Q97NX6: scpB; NbExp=2; IntAct=EBI-2207137, EBI-2206697;
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; AF162664; AAD50778.1; -; Genomic_DNA.
DR EMBL; AE005672; AAK74904.1; -; Genomic_DNA.
DR EMBL; Z49246; CAA89213.1; -; Genomic_DNA.
DR EMBL; Z95914; CAB09367.1; -; Genomic_DNA.
DR EMBL; Z99200; CAB16344.1; -; Genomic_DNA.
DR EMBL; Z99201; CAB16345.1; -; Genomic_DNA.
DR EMBL; Z99202; CAB16346.1; -; Genomic_DNA.
DR EMBL; Z99203; CAB16347.1; -; Genomic_DNA.
DR EMBL; Z99204; CAB16348.1; -; Genomic_DNA.
DR EMBL; Z99205; CAB16349.1; -; Genomic_DNA.
DR EMBL; Z99206; CAB16350.1; -; Genomic_DNA.
DR EMBL; AB021544; BAA85492.1; -; Genomic_DNA.
DR EMBL; AB021605; BAA85553.1; -; Genomic_DNA.
DR EMBL; AB021606; BAA85554.1; -; Genomic_DNA.
DR EMBL; AB021607; BAA85555.1; -; Genomic_DNA.
DR EMBL; AB021608; BAA85556.1; -; Genomic_DNA.
DR EMBL; AB021609; BAA85557.1; -; Genomic_DNA.
DR EMBL; AB021610; BAA85558.1; -; Genomic_DNA.
DR EMBL; AB021611; BAA85559.1; -; Genomic_DNA.
DR EMBL; AB021612; BAA85560.1; -; Genomic_DNA.
DR EMBL; AB021613; BAA85561.1; -; Genomic_DNA.
DR EMBL; AB021614; BAA85562.1; -; Genomic_DNA.
DR EMBL; AB021615; BAA85563.1; -; Genomic_DNA.
DR EMBL; AB021616; BAA85564.1; -; Genomic_DNA.
DR EMBL; AB021617; BAA85565.1; -; Genomic_DNA.
DR EMBL; AB021618; BAA85566.1; -; Genomic_DNA.
DR EMBL; AB021619; BAA85567.1; -; Genomic_DNA.
DR PIR; G95088; G95088.
DR PIR; S54795; S54795.
DR RefSeq; WP_000974746.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; P0A4J6; -.
DR SMR; P0A4J6; -.
DR IntAct; P0A4J6; 3.
DR STRING; 170187.SP_0766; -.
DR PRIDE; P0A4J6; -.
DR EnsemblBacteria; AAK74904; AAK74904; SP_0766.
DR GeneID; 60232924; -.
DR GeneID; 66805911; -.
DR KEGG; spn:SP_0766; -.
DR eggNOG; COG0605; Bacteria.
DR OMA; KWGSFDK; -.
DR BioCyc; SPNE170187:G1FZB-782-MON; -.
DR Proteomes; UP000000585; 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 Manganese; Metal-binding; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..201
FT /note="Superoxide dismutase [Mn]"
FT /id="PRO_0000160097"
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 163
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT VARIANT 42
FT /note="A -> V (in strain: NEM1278)"
FT VARIANT 61..65
FT /note="ESIPA -> DLSQH (in strain: NEM667 and D39)"
FT VARIANT 100
FT /note="A -> T (in strain: 1510)"
FT VARIANT 110
FT /note="F -> L (in strain: NEM1122)"
FT VARIANT 143
FT /note="T -> I (in strain: 1510)"
FT VARIANT 148
FT /note="Q -> L (in strain: 872)"
FT VARIANT 148
FT /note="Q -> P (in strain: 1293, 1454, 1565, 1639, 3051 and
FT 3203)"
FT VARIANT 152
FT /note="I -> F (in strain: 661)"
SQ SEQUENCE 201 AA; 22397 MW; DBC86690C8D76CD0 CRC64;
MAIILPELPY AYDALEPYID AETMHLHHDK HHQTYVNNAN AALEKHPEIG EDLEALLADV
ESIPADIRQA LINNGGGHLN HALFWELMTP EKTAPSAELA AAIDATFGSF EEFQAAFTAA
ATTRFGSGWA WLVVNKEGKL EVTSTANQDT PISEGKKPIL GLDVWEHAYY VKYRNVRPDY
IKAFFSVINW NKVDELYAAA K
