ID   CATE_BACSU              Reviewed;         686 AA.
AC   P42234; P42309;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 2.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Catalase-2;
DE            EC=1.11.1.6;
GN   Name=katE; Synonyms=katB; OrderedLocusNames=BSU39050; ORFNames=N15D;
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 / BGSC1A1;
RX   PubMed=8969509; DOI=10.1099/13500872-142-11-3113;
RA   Yoshida K., Shindo K., Sano H., Seki S., Fujimura M., Yanai N., Miwa Y.,
RA   Fujita Y.;
RT   "Sequencing of a 65 kb region of the Bacillus subtilis genome containing
RT   the lic and cel loci, and creation of a 177 kb contig covering the gnt-
RT   sacXY region.";
RL   Microbiology 142:3113-3123(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 TO 524.
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-536.
RX   PubMed=7559348; DOI=10.1128/jb.177.19.5598-5605.1995;
RA   Engelmann S., Lindner C., Hecker M.;
RT   "Cloning, nucleotide sequence, and regulation of katE encoding a sigma B-
RT   dependent catalase in Bacillus subtilis.";
RL   J. Bacteriol. 177:5598-5605(1995).
CC   -!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to
CC       protect cells from the toxic effects of hydrogen peroxide. Involved in
CC       sporulation.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10013};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC   -!- SIMILARITY: Belongs to the catalase family. HPII subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA59465.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; D83026; BAA11699.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15931.2; -; Genomic_DNA.
DR   EMBL; X85182; CAA59465.1; ALT_FRAME; Genomic_DNA.
DR   PIR; D69647; D69647.
DR   RefSeq; NP_391784.2; NC_000964.3.
DR   RefSeq; WP_003243331.1; NZ_JNCM01000034.1.
DR   AlphaFoldDB; P42234; -.
DR   SMR; P42234; -.
DR   STRING; 224308.BSU39050; -.
DR   PeroxiBase; 4059; BsKat02_168.
DR   PaxDb; P42234; -.
DR   PRIDE; P42234; -.
DR   EnsemblBacteria; CAB15931; CAB15931; BSU_39050.
DR   GeneID; 937481; -.
DR   KEGG; bsu:BSU39050; -.
DR   PATRIC; fig|224308.179.peg.4228; -.
DR   eggNOG; COG0693; Bacteria.
DR   eggNOG; COG0753; Bacteria.
DR   InParanoid; P42234; -.
DR   OMA; VMWQMSD; -.
DR   PhylomeDB; P42234; -.
DR   BioCyc; BSUB:BSU39050-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004096; F:catalase activity; IBA:GO_Central.
DR   GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR   GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   CDD; cd03132; GATase1_catalase; 1.
DR   Gene3D; 1.20.1370.20; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR024708; Catalase_AS.
DR   InterPro; IPR024712; Catalase_clade2.
DR   InterPro; IPR043156; Catalase_clade2_helical.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR002226; Catalase_haem_BS.
DR   InterPro; IPR010582; Catalase_immune_responsive.
DR   InterPro; IPR041399; Catalase_large_C.
DR   InterPro; IPR020835; Catalase_sf.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   PANTHER; PTHR42821; PTHR42821; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   Pfam; PF06628; Catalase-rel; 1.
DR   Pfam; PF18011; Catalase_C; 1.
DR   PIRSF; PIRSF038927; Catalase_clade2; 1.
DR   PRINTS; PR00067; CATALASE.
DR   SMART; SM01060; Catalase; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   SUPFAM; SSF56634; SSF56634; 1.
DR   PROSITE; PS00437; CATALASE_1; 1.
DR   PROSITE; PS00438; CATALASE_2; 1.
DR   PROSITE; PS51402; CATALASE_3; 1.
PE   3: Inferred from homology;
KW   Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW   Reference proteome; Sporulation.
FT   CHAIN           1..686
FT                   /note="Catalase-2"
FT                   /id="PRO_0000084970"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        78
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   ACT_SITE        151
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   BINDING         365
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        524
FT                   /note="I -> N (in Ref. 1; BAA11699)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   686 AA;  77480 MW;  1C74405B4310E091 CRC64;
     MSDDQNKRVN EHSKDEQLEQ YRTDNSGKKM TTNQGLRVSE DEHSLKAGVR GPTLMEDFHF
     REKMTHFDHE RIPERVVHAR GFGVHGFFQV YEPMTEYTRA KFLQDPSVKT PVFVRFSTVA
     GSKGSADTVR DARGFATKFY TEEGNYDLVG NNIPVFFIQD AIKFPDLVHA FKPEPHNEMP
     QAATAHDTFW DFVANNPESA HMVMWTMSDR GIPRSYRMME GFGVHTFRFV NEQGKARFVK
     FHWKPVLGVH SLVWDEAQKI AGKDPDFHRR DLWETIENGG KVEYELGVQM IDEEDEFKFD
     FDILDPTKLW PEELVPVKII GKMTLNRNQD NVFAETEQVA FHPGNVVPGI DFTNDPLLQG
     RLFSYTDTQL IRLGGPNFHE IPINRPVCPF HNNQYDGYHR MTINKGPVAY HKNSLQNNDP
     SPATAEEGGY VHYQEKVEGK KIRQRSDSFN DYYSQAKLFW NSMSPVEKQH IISAFCFEVG
     KVKSKDVQRQ VVDVFSNVDA DLAEEIAKGV GVAAPAKRKA SKEILTSPAL SQARTVKTAS
     TRKVAVLAGN GFHEKELQTV LEALKQEGIT VDIISQNLGY MTSGSGQQLE ASGTFLTVDS
     VLYDAVYAAG GLELKDNKQA MAFIREAYNH YKAIGAANEG IDLLQSSVGT TEGLGIVTAK
     DEPDYTAFSK AFIDAVAAHR HWDRRI