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Database: UniProt/TrEMBL
Entry: B2INE8_STRPS
LinkDB: B2INE8_STRPS
Original site: B2INE8_STRPS 
ID   B2INE8_STRPS            Unreviewed;       201 AA.
AC   B2INE8;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   25-OCT-2017, entry version 61.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   Name=sodA {ECO:0000313|EMBL:ACB89967.1};
GN   OrderedLocusNames=SPCG_0715 {ECO:0000313|EMBL:ACB89967.1};
OS   Streptococcus pneumoniae (strain CGSP14).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=516950 {ECO:0000313|EMBL:ACB89967.1, ECO:0000313|Proteomes:UP000001682};
RN   [1] {ECO:0000313|EMBL:ACB89967.1, ECO:0000313|Proteomes:UP000001682}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGSP14 {ECO:0000313|EMBL:ACB89967.1,
RC   ECO:0000313|Proteomes:UP000001682};
RX   PubMed=19361343; DOI=10.1186/1471-2164-10-158;
RA   Ding F., Tang P., Hsu M.-H., Cui P., Hu S., Yu J., Chiu C.-H.;
RT   "Genome evolution driven by host adaptations results in a more
RT   virulent and antimicrobial-resistant Streptococcus pneumoniae serotype
RT   14.";
RL   BMC Genomics 10:158-158(2009).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000414}.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {ECO:0000256|RuleBase:RU000414}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000256|RuleBase:RU000414}.
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DR   EMBL; CP001033; ACB89967.1; -; Genomic_DNA.
DR   RefSeq; WP_000974746.1; NC_010582.1.
DR   ProteinModelPortal; B2INE8; -.
DR   SMR; B2INE8; -.
DR   EnsemblBacteria; ACB89967; ACB89967; SPCG_0715.
DR   KEGG; spw:SPCG_0715; -.
DR   HOGENOM; HOG000013583; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   Proteomes; UP000001682; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
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   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001682};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN        5     88       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       95    195       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        81     81       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       163    163       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       167    167       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
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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