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Database: UniProt/TrEMBL
Entry: G7SJI7_STRSU
LinkDB: G7SJI7_STRSU
Original site: G7SJI7_STRSU 
ID   G7SJI7_STRSU            Unreviewed;       201 AA.
AC   G7SJI7;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   25-OCT-2017, entry version 30.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=SSUST1_1420 {ECO:0000313|EMBL:AER21772.1};
OS   Streptococcus suis ST1.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1004951 {ECO:0000313|EMBL:AER21772.1, ECO:0000313|Proteomes:UP000008846};
RN   [1] {ECO:0000313|EMBL:AER21772.1, ECO:0000313|Proteomes:UP000008846}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ST1 {ECO:0000313|EMBL:AER21772.1};
RX   PubMed=22026465; DOI=10.1186/1471-2164-12-523;
RA   Zhang A., Yang M., Hu P., Wu J., Chen B., Hua Y., Yu J., Chen H.,
RA   Xiao J., Jin M.;
RT   "Comparative Genomic Analysis of Streptococcus suis reveals
RT   significant genomic diversity among different serotypes.";
RL   BMC Genomics 12:523-523(2011).
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; CP002651; AER21772.1; -; Genomic_DNA.
DR   RefSeq; WP_013730459.1; NC_017950.1.
DR   ProteinModelPortal; G7SJI7; -.
DR   EnsemblBacteria; AER21772; AER21772; SSUST1_1420.
DR   KEGG; srp:SSUST1_1420; -.
DR   PATRIC; fig|1004951.3.peg.1376; -.
DR   KO; K04564; -.
DR   BioCyc; SSUI1004951:GLLP-1405-MONOMER; -.
DR   Proteomes; UP000008846; 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:UP000008846};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN        5     89       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       97    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;  22433 MW;  39185A74AE02B0F1 CRC64;
     MAIILPDLPY AYDALEPHID AETMTLHHDK HHATYVANAN AALEKHPEIG EDLVALLSDV
     EQIPADIRQA LINNGGGHLN HALFWELLSP EKTEISAELA ADIDATFGSF DAFKEAFTAA
     ATTRFGSGWA FLVVNKEGKL EVISTANQDT PIMQGLKPIL ALDVWEHAYY LNYRNVRPNY
     IKAFFEVINW DKVNELYKAA K
//
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