ID   CATA_BACSU              Reviewed;         483 AA.
AC   P26901; P77838;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   25-NOV-2008, entry version 71.
DE   RecName: Full=Vegetative catalase;
DE            EC=1.11.1.6;
GN   Name=katA; Synonyms=kat, kat-19; OrderedLocusNames=BSU08820;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / YB886;
RX   MEDLINE=92097949; PubMed=1756979; DOI=10.1016/0378-1119(91)90585-Y;
RA   Bol D.K., Yasbin R.E.;
RT   "The isolation, cloning and identification of a vegetative catalase
RT   gene from Bacillus subtilis.";
RL   Gene 109:31-37(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   MEDLINE=97346037; PubMed=9202460;
RA   Cummings N.J., Connerton I.F.;
RT   "The Bacillus subtilis 168 chromosome from sspE to katA.";
RL   Microbiology 143:1855-1859(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   MEDLINE=98044033; 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   [4]
RP   PROTEIN SEQUENCE OF 2-19.
RC   STRAIN=168 / YB886;
RX   MEDLINE=94236234; PubMed=8180695;
RA   Hartford O.M., Dowds B.C.A.;
RT   "Isolation and characterization of a hydrogen peroxide resistant
RT   mutant of Bacillus subtilis.";
RL   Microbiology 140:297-304(1994).
CC   -!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen;
CC       serves to protect cells from the toxic effects of hydrogen
CC       peroxide.
CC   -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O.
CC   -!- COFACTOR: Heme group.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- DEVELOPMENTAL STAGE: Elevated levels of expression during entry
CC       into the stationary phase of the growth cycle.
CC   -!- INDUCTION: By hydrogen peroxide.
CC   -!- SIMILARITY: Belongs to the catalase family.
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DR   EMBL; M80796; AAA22402.1; -; Genomic_DNA.
DR   EMBL; Z82044; CAB04807.1; -; Genomic_DNA.
DR   EMBL; Z99108; CAB12710.1; -; Genomic_DNA.
DR   PIR; JH0532; JH0532.
DR   RefSeq; NP_388762.1; -.
DR   HSSP; P00432; 4BLC.
DR   PeroxiBase; 4082; BsKat01_168.
DR   GeneID; 939240; -.
DR   GenomeReviews; AL009126_GR; BSU08820.
DR   KEGG; bsu:BSU08820; -.
DR   NMPDR; fig|224308.1.peg.881; -.
DR   SubtiList; BG10849; katA.
DR   HOGENOM; P26901; -.
DR   BioCyc; BSUB224308:BSU0881-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0004096; F:catalase activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR002226; Catalase.
DR   InterPro; IPR011614; Catalase_N.
DR   Gene3D; G3DSA:2.40.180.10; Catalase_N; 1.
DR   PANTHER; PTHR11465; Catalase; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   PRINTS; PR00067; CATALASE.
DR   ProDom; PD000510; Catalase; 1.
DR   PROSITE; PS00437; CATALASE_1; 1.
DR   PROSITE; PS00438; CATALASE_2; 1.
DR   PROSITE; PS51402; CATALASE_3; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Cytoplasm; Direct protein sequencing; Heme;
KW   Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    483       Vegetative catalase.
FT                                /FTId=PRO_0000084975.
FT   ACT_SITE     54     54       By similarity.
FT   ACT_SITE    127    127       By similarity.
FT   METAL       337    337       Iron (heme axial ligand) (By similarity).
FT   CONFLICT    206    206       G -> P (in Ref. 1; AAA22402).
FT   CONFLICT    373    373       G -> D (in Ref. 1; AAA22402).
SQ   SEQUENCE   483 AA;  54733 MW;  456772956F870DE6 CRC64;
     MSSNKLTTSW GAPVGDNQNS MTAGSRGPTL IQDVHLLEKL AHFNRERVPE RVVHAKGAGA
     HGYFEVTNDV TKYTKAAFLS EVGKRTPLFI RFSTVAGELG SADTVRDPRG FAVKFYTEEG
     NYDIVGNNTP VFFIRDAIKF PDFIHTQKRD PKTHLKNPTA VWDFWSLSPE SLHQVTILMS
     DRGIPATLRH MHGFGSHTFK WTNAEGEGVW IKYHFKTEQG VKNLDVNTAA KIAGENPDYH
     TEDLFNAIEN GDYPAWKLYV QIMPLEDANT YRFDPFDVTK VWSQKDYPLI EVGRMVLDRN
     PENYFAEVEQ ATFSPGTLVP GIDVSPDKML QGRLFAYHDA HRYRVGANHQ ALPINRARNK
     VNNYQRDGQM RFGDNGGGSV YYEPNSFGGP KESPEDKQAA YPVQGIADSV SYDHYDHYTQ
     AGDLYRLMSE DERTRLVENI VNAMKPVEKE EIKLRQIEHF YKADPEYGKR VAEGLGLPIK
     KDS
//