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Database: UniProt/SWISS-PROT
Entry: SODM_STRPN
LinkDB: SODM_STRPN
Original site: SODM_STRPN 
ID   SODM_STRPN              Reviewed;         201 AA.
AC   P0A4J6; O33757; O54268; O54269; Q59949; Q9R3B6; Q9R3B8; Q9S175;
AC   Q9S176; Q9S177; Q9S447;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   05-DEC-2018, entry version 81.
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
RT   and 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.,
RA   Hickey E.K., Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C.,
RA   Dougherty B.A., 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
RT   bacteria 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;
RA   Poyart C., Quesne G., Coulon S., Berche P., Trieu-Cuot P.;
RT   "Identification of streptococci to species level by sequencing the
RT   gene 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
RT   the 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
CC       systems. May play a critical role against oxidative stress,
CC       affecting both the 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       Q97SE5:gatC; NbExp=2; IntAct=EBI-2207137, EBI-2207053;
CC       Q97NV3:groS; NbExp=2; IntAct=EBI-2207137, EBI-2206949;
CC       Q97NX6:scpB; NbExp=2; IntAct=EBI-2207137, EBI-2206697;
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
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   ProteinModelPortal; P0A4J6; -.
DR   SMR; P0A4J6; -.
DR   IntAct; P0A4J6; 3.
DR   PRIDE; P0A4J6; -.
DR   EnsemblBacteria; AAK74904; AAK74904; SP_0766.
DR   KEGG; spn:SP_0766; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   BioCyc; SPNE170187:G1FZB-782-MONOMER; -.
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; 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   Complete proteome; Manganese; Metal-binding; Oxidoreductase.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    201       Superoxide dismutase [Mn].
FT                                /FTId=PRO_0000160097.
FT   METAL        27     27       Manganese. {ECO:0000250}.
FT   METAL        81     81       Manganese. {ECO:0000250}.
FT   METAL       163    163       Manganese. {ECO:0000250}.
FT   METAL       167    167       Manganese. {ECO:0000250}.
FT   VARIANT      42     42       A -> V (in strain: NEM1278).
FT   VARIANT      61     65       ESIPA -> DLSQH (in strain: NEM667 and
FT                                D39).
FT   VARIANT     100    100       A -> T (in strain: 1510).
FT   VARIANT     110    110       F -> L (in strain: NEM1122).
FT   VARIANT     143    143       T -> I (in strain: 1510).
FT   VARIANT     148    148       Q -> L (in strain: 872).
FT   VARIANT     148    148       Q -> P (in strain: 1293, 1454, 1565,
FT                                1639, 3051 and 3203).
FT   VARIANT     152    152       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
//
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