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Database: UniProt/TrEMBL
Entry: C6ACA9_BARGA
LinkDB: C6ACA9_BARGA
Original site: C6ACA9_BARGA 
ID   C6ACA9_BARGA            Unreviewed;       200 AA.
AC   C6ACA9;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   25-OCT-2017, entry version 48.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   Name=sodB {ECO:0000313|EMBL:ACS50821.1};
GN   OrderedLocusNames=Bgr_04980 {ECO:0000313|EMBL:ACS50821.1};
OS   Bartonella grahamii (strain as4aup).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=634504 {ECO:0000313|EMBL:ACS50821.1, ECO:0000313|Proteomes:UP000001489};
RN   [1] {ECO:0000313|EMBL:ACS50821.1, ECO:0000313|Proteomes:UP000001489}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=as4aup {ECO:0000313|Proteomes:UP000001489};
RX   PubMed=19578403; DOI=10.1371/journal.pgen.1000546;
RA   Berglund E.C., Frank A.C., Calteau A., Vinnere Pettersson O.,
RA   Granberg F., Eriksson A.-S., Naeslund K., Holmberg M., Lindroos H.,
RA   Andersson S.G.;
RT   "Run-off replication of host-adaptability genes is associated with
RT   gene transfer agents in the genome of mouse-infecting Bartonella
RT   grahamii.";
RL   PLoS Genet. 5:E1000546-E1000546(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; CP001562; ACS50821.1; -; Genomic_DNA.
DR   RefSeq; WP_012754850.1; NC_012846.1.
DR   STRING; 634504.Bgr_04980; -.
DR   EnsemblBacteria; ACS50821; ACS50821; Bgr_04980.
DR   KEGG; bgr:Bgr_04980; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013584; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   OrthoDB; POG091H03Q7; -.
DR   Proteomes; UP000001489; 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:UP000001489};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN        3     84       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       95    191       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        77     77       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       160    160       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       164    164       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   200 AA;  23241 MW;  B3D196D60800A825 CRC64;
     MAFELPPLPY DYDALSPYMS RETLEYHHDK HHLAYLNNTN NFVKELGLEN ESLEDIVKKS
     FGKNIGLFNN AAQYYNHNHF WLWMKKDGGG QKLPEKLAKA IDADLGGYDK FRADFIAAAS
     AQFGSGWAWV AVKDGKLEIM KTPNGENPLI HNARPILGVD VWEHSYYIDY RNARPKYLES
     FVDHLINWDY VLKLYEECEF
//
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