(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 138.
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 the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   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., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., 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., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., 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 quality of
RT   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., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   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; DOI=10.1099/00221287-146-1-65;
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 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. {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 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA12507.1; Type=Frameshift; 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   SMR; P54375; -.
DR   IntAct; P54375; 1.
DR   MINT; P54375; -.
DR   STRING; 224308.BSU25020; -.
DR   iPTMnet; P54375; -.
DR   jPOST; 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;
DR   PRODOM; P54375.
DR   SWISS-2DPAGE; P54375.
KW   3D-structure; Cytoplasm; Direct protein sequencing; Manganese;
KW   Metal-binding; Oxidoreductase; Phosphoprotein; Reference proteome;
KW   Stress response.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:10658653,
FT                   ECO:0000269|PubMed:9298659"
FT   CHAIN           2..202
FT                   /note="Superoxide dismutase [Mn]"
FT                   /id="PRO_0000160019"
FT   METAL           27
FT                   /note="Manganese"
FT   METAL           82
FT                   /note="Manganese"
FT   METAL           164
FT                   /note="Manganese"
FT   METAL           168
FT                   /note="Manganese"
FT   MOD_RES         34
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:17218307"
FT   MOD_RES         70
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:17218307"
FT   CONFLICT        201
FT                   /note="A -> R (in Ref. 1; BAA12507)"
FT                   /evidence="ECO:0000305"
FT   TURN            12..18
FT                   /evidence="ECO:0000244|PDB:2RCV"
FT   HELIX           21..29
FT                   /evidence="ECO:0000244|PDB:2RCV"
FT   HELIX           31..42
FT                   /evidence="ECO:0000244|PDB:2RCV"
FT   HELIX           47..50
FT                   /evidence="ECO:0000244|PDB:2RCV"
FT   HELIX           54..59
FT                   /evidence="ECO:0000244|PDB:2RCV"
FT   HELIX           60..63
FT                   /evidence="ECO:0000244|PDB:2RCV"
FT   TURN            66..68
FT                   /evidence="ECO:0000244|PDB:2RCV"
FT   HELIX           69..87
FT                   /evidence="ECO:0000244|PDB:2RCV"
FT   HELIX           99..109
FT                   /evidence="ECO:0000244|PDB:2RCV"
FT   HELIX           112..125
FT                   /evidence="ECO:0000244|PDB:2RCV"
FT   STRAND          128..137
FT                   /evidence="ECO:0000244|PDB:2RCV"
FT   STRAND          140..147
FT                   /evidence="ECO:0000244|PDB:2RCV"
FT   HELIX           152..155
FT                   /evidence="ECO:0000244|PDB:2RCV"
FT   STRAND          158..164
FT                   /evidence="ECO:0000244|PDB:2RCV"
FT   HELIX           167..169
FT                   /evidence="ECO:0000244|PDB:2RCV"
FT   HELIX           171..174
FT                   /evidence="ECO:0000244|PDB:2RCV"
FT   HELIX           178..185
FT                   /evidence="ECO:0000244|PDB:2RCV"
FT   TURN            186..188
FT                   /evidence="ECO:0000244|PDB:2RCV"
FT   HELIX           191..200
FT                   /evidence="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
//

If you have problems or comments...

PBIL Back to PBIL home page