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Database: UniProt/SWISS-PROT
Entry: SODM_BACSU
LinkDB: SODM_BACSU
Original site: SODM_BACSU 
ID   SODM_BACSU              Reviewed;         202 AA.
AC   P54375;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 5.
DT   05-DEC-2018, entry version 132.
DE   RecName: Full=Superoxide dismutase [Mn];
DE            EC=1.15.1.1;
DE   AltName: Full=General stress protein 24;
DE            Short=GSP24;
GN   Name=sodA; Synonyms=yqgD; OrderedLocusNames=BSU25020;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of
RT   the Bacillus subtilis genome containing the skin element and many
RT   sporulation genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   SEQUENCE REVISION.
RX   PubMed=10568751; DOI=10.1101/gr.9.11.1116;
RA   Medigue C., Rose M., Viari A., Danchin A.;
RT   "Detecting and analyzing DNA sequencing errors: toward a higher
RT   quality of the Bacillus subtilis genome sequence.";
RL   Genome Res. 9:1116-1127(1999).
RN   [4]
RP   SEQUENCE REVISION TO 201.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G.,
RA   Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus
RT   subtilis 168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-36.
RC   STRAIN=168 / IS58;
RX   PubMed=9298659; DOI=10.1002/elps.1150180820;
RA   Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.;
RT   "First steps from a two-dimensional protein index towards a response-
RT   regulation map for Bacillus subtilis.";
RL   Electrophoresis 18:1451-1463(1997).
RN   [6]
RP   PROTEIN SEQUENCE OF 2-12, AND SUBCELLULAR LOCATION.
RC   STRAIN=168;
RX   PubMed=10658653;
RA   Hirose I., Sano K., Shioda I., Kumano M., Nakamura K., Yamane K.;
RT   "Proteome analysis of Bacillus subtilis extracellular proteins: a two-
RT   dimensional protein electrophoretic study.";
RL   Microbiology 146:65-75(2000).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-34 AND THR-70, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=168;
RX   PubMed=17218307; DOI=10.1074/mcp.M600464-MCP200;
RA   Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
RA   Mann M.;
RT   "The serine/threonine/tyrosine phosphoproteome of the model bacterium
RT   Bacillus subtilis.";
RL   Mol. Cell. Proteomics 6:697-707(2007).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS,
RP   SUBUNIT, AND COFACTOR.
RX   PubMed=18084079; DOI=10.1107/S1744309107054127;
RA   Liu P., Ewis H.E., Huang Y.J., Lu C.D., Tai P.C., Weber I.T.;
RT   "Structure of Bacillus subtilis superoxide dismutase.";
RL   Acta Crystallogr. F 63:1003-1007(2007).
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological
CC       systems.
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;
CC         Evidence={ECO:0000269|PubMed:18084079};
CC       Note=Binds 1 Mn(2+) ion per subunit.
CC       {ECO:0000269|PubMed:18084079};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18084079}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10658653}.
CC   -!- INDUCTION: By heat shock, salt stress, oxidative stress, glucose
CC       limitation and oxygen limitation.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA12507.1; Type=Frameshift; Positions=200; Evidence={ECO:0000305};
DR   EMBL; D84432; BAA12507.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AL009126; CAB14432.3; -; Genomic_DNA.
DR   PIR; B69709; B69709.
DR   RefSeq; NP_390381.3; NC_000964.3.
DR   RefSeq; WP_004398583.1; NZ_JNCM01000036.1.
DR   PDB; 2RCV; X-ray; 1.60 A; A/B/C/D/E/F/G/H=1-200.
DR   PDBsum; 2RCV; -.
DR   ProteinModelPortal; P54375; -.
DR   SMR; P54375; -.
DR   IntAct; P54375; 1.
DR   MINT; P54375; -.
DR   STRING; 224308.Bsubs1_010100013696; -.
DR   iPTMnet; P54375; -.
DR   PaxDb; P54375; -.
DR   PRIDE; P54375; -.
DR   EnsemblBacteria; CAB14432; CAB14432; BSU25020.
DR   GeneID; 938052; -.
DR   KEGG; bsu:BSU25020; -.
DR   PATRIC; fig|224308.179.peg.2721; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013583; -.
DR   InParanoid; P54375; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   PhylomeDB; P54375; -.
DR   BioCyc; BSUB:BSU25020-MONOMER; -.
DR   EvolutionaryTrace; P54375; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
KW   Manganese; Metal-binding; Oxidoreductase; Phosphoprotein;
KW   Reference proteome; Stress response.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:10658653,
FT                                ECO:0000269|PubMed:9298659}.
FT   CHAIN         2    202       Superoxide dismutase [Mn].
FT                                /FTId=PRO_0000160019.
FT   METAL        27     27       Manganese.
FT   METAL        82     82       Manganese.
FT   METAL       164    164       Manganese.
FT   METAL       168    168       Manganese.
FT   MOD_RES      34     34       Phosphothreonine.
FT                                {ECO:0000269|PubMed:17218307}.
FT   MOD_RES      70     70       Phosphothreonine.
FT                                {ECO:0000269|PubMed:17218307}.
FT   CONFLICT    201    201       A -> R (in Ref. 1; BAA12507).
FT                                {ECO:0000305}.
FT   TURN         12     18       {ECO:0000244|PDB:2RCV}.
FT   HELIX        21     29       {ECO:0000244|PDB:2RCV}.
FT   HELIX        31     42       {ECO:0000244|PDB:2RCV}.
FT   HELIX        47     50       {ECO:0000244|PDB:2RCV}.
FT   HELIX        54     59       {ECO:0000244|PDB:2RCV}.
FT   HELIX        60     63       {ECO:0000244|PDB:2RCV}.
FT   TURN         66     68       {ECO:0000244|PDB:2RCV}.
FT   HELIX        69     87       {ECO:0000244|PDB:2RCV}.
FT   HELIX        99    109       {ECO:0000244|PDB:2RCV}.
FT   HELIX       112    125       {ECO:0000244|PDB:2RCV}.
FT   STRAND      128    137       {ECO:0000244|PDB:2RCV}.
FT   STRAND      140    147       {ECO:0000244|PDB:2RCV}.
FT   HELIX       152    155       {ECO:0000244|PDB:2RCV}.
FT   STRAND      158    164       {ECO:0000244|PDB:2RCV}.
FT   HELIX       167    169       {ECO:0000244|PDB:2RCV}.
FT   HELIX       171    174       {ECO:0000244|PDB:2RCV}.
FT   HELIX       178    185       {ECO:0000244|PDB:2RCV}.
FT   TURN        186    188       {ECO:0000244|PDB:2RCV}.
FT   HELIX       191    200       {ECO:0000244|PDB:2RCV}.
SQ   SEQUENCE   202 AA;  22490 MW;  16BE475DE137A88E CRC64;
     MAYELPELPY AYDALEPHID KETMTIHHTK HHNTYVTNLN KAVEGNTALA NKSVEELVAD
     LDSVPENIRT AVRNNGGGHA NHKLFWTLLS PNGGGEPTGA LAEEINSVFG SFDKFKEQFA
     AAAAGRFGSG WAWLVVNNGK LEITSTPNQD SPLSEGKTPI LGLDVWEHAY YLNYQNRRPD
     YISAFWNVVN WDEVARLYSE AK
//
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