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 03-AUG-2022, entry version 147.
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};
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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 AlphaFoldDB; P54375; -.
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; BSU_25020.
DR GeneID; 938052; -.
DR KEGG; bsu:BSU25020; -.
DR PATRIC; fig|224308.179.peg.2721; -.
DR eggNOG; COG0605; Bacteria.
DR InParanoid; P54375; -.
DR OMA; KWGSFDK; -.
DR PhylomeDB; P54375; -.
DR BioCyc; BSUB:BSU25020-MON; -.
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; 3.55.40.20; -; 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; 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 BINDING 27
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 82
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 164
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 168
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
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:0007829|PDB:2RCV"
FT HELIX 21..29
FT /evidence="ECO:0007829|PDB:2RCV"
FT HELIX 31..42
FT /evidence="ECO:0007829|PDB:2RCV"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:2RCV"
FT HELIX 54..59
FT /evidence="ECO:0007829|PDB:2RCV"
FT HELIX 60..63
FT /evidence="ECO:0007829|PDB:2RCV"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:2RCV"
FT HELIX 69..87
FT /evidence="ECO:0007829|PDB:2RCV"
FT HELIX 99..109
FT /evidence="ECO:0007829|PDB:2RCV"
FT HELIX 112..125
FT /evidence="ECO:0007829|PDB:2RCV"
FT STRAND 128..137
FT /evidence="ECO:0007829|PDB:2RCV"
FT STRAND 140..147
FT /evidence="ECO:0007829|PDB:2RCV"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:2RCV"
FT STRAND 158..164
FT /evidence="ECO:0007829|PDB:2RCV"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:2RCV"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:2RCV"
FT HELIX 178..185
FT /evidence="ECO:0007829|PDB:2RCV"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:2RCV"
FT HELIX 191..200
FT /evidence="ECO:0007829|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
