CATA_BACSU
ID CATA_BACSU Reviewed; 483 AA.
AC P26901; P77838;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 5.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Vegetative catalase {ECO:0000303|PubMed:1756979};
DE EC=1.11.1.6 {ECO:0000269|PubMed:8180695};
GN Name=katA {ECO:0000303|PubMed:1756979}; Synonyms=kat, kat-19;
GN OrderedLocusNames=BSU08820;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / YB886 / BG214;
RX 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 gene
RT from Bacillus subtilis.";
RL Gene 109:31-37(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9202460; DOI=10.1099/00221287-143-6-1855;
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 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 [4]
RP SEQUENCE REVISION TO 373.
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 2-19, FUNCTION, CATALYTIC ACTIVITY, DEVELOPMENTAL
RP STAGE, AND INDUCTION.
RC STRAIN=168 / YB886 / BG214;
RX PubMed=8180695; DOI=10.1099/13500872-140-2-297;
RA Hartford O.M., Dowds B.C.A.;
RT "Isolation and characterization of a hydrogen peroxide resistant mutant of
RT Bacillus subtilis.";
RL Microbiology 140:297-304(1994).
RN [6]
RP PROTEIN SEQUENCE OF 2-11.
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 PROTEIN SEQUENCE OF 2-11.
RC STRAIN=KIBGE-HAS;
RA Bano S., Qader S.A.U., Aman A., Azhar A.;
RL Submitted (AUG-2009) to UniProtKB.
RN [8]
RP IRON-BINDING, COFACTOR, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=ATCC 21332 / IAM 1213;
RX PubMed=21744456; DOI=10.1002/cbic.201100190;
RA Albrecht A.G., Landmann H., Nette D., Burghaus O., Peuckert F., Seubert A.,
RA Miethke M., Marahiel M.A.;
RT "The frataxin homologue Fra plays a key role in intracellular iron
RT channeling in Bacillus subtilis.";
RL ChemBioChem 12:2052-2061(2011).
CC -!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to
CC protect cells from the toxic effects of hydrogen peroxide.
CC {ECO:0000305|PubMed:1756979, ECO:0000305|PubMed:8180695}.
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:0000269|PubMed:8180695};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000269|PubMed:21744456};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21744456}.
CC -!- DEVELOPMENTAL STAGE: Elevated levels of expression during entry into
CC the stationary phase of the growth cycle. {ECO:0000269|PubMed:8180695}.
CC -!- INDUCTION: By hydrogen peroxide. {ECO:0000269|PubMed:8180695}.
CC -!- DISRUPTION PHENOTYPE: Insertion mutant shows increased sensitivity to
CC H(2)0(2), reduced catalase expression and an absence of induced
CC protection of the cell. {ECO:0000269|PubMed:1756979}.
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR EMBL; M80796; AAA22402.1; -; Genomic_DNA.
DR EMBL; Z82044; CAB04807.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12710.2; -; Genomic_DNA.
DR PIR; JH0532; JH0532.
DR RefSeq; NP_388762.2; NC_000964.3.
DR RefSeq; WP_003245322.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P26901; -.
DR SMR; P26901; -.
DR STRING; 224308.BSU08820; -.
DR PeroxiBase; 4082; BsKat01_168.
DR PaxDb; P26901; -.
DR PRIDE; P26901; -.
DR EnsemblBacteria; CAB12710; CAB12710; BSU_08820.
DR GeneID; 939240; -.
DR KEGG; bsu:BSU08820; -.
DR PATRIC; fig|224308.179.peg.952; -.
DR eggNOG; COG0753; Bacteria.
DR InParanoid; P26901; -.
DR OMA; WTCYVQV; -.
DR PhylomeDB; P26901; -.
DR BioCyc; BSUB:BSU08820-MON; -.
DR BRENDA; 1.11.1.6; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; 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:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
DR CDD; cd08156; catalase_clade_3; 1.
DR InterPro; IPR018028; Catalase.
DR InterPro; IPR040333; Catalase_3.
DR InterPro; IPR024708; Catalase_AS.
DR InterPro; IPR024711; Catalase_clade1/3.
DR InterPro; IPR011614; Catalase_core.
DR InterPro; IPR002226; Catalase_haem_BS.
DR InterPro; IPR010582; Catalase_immune_responsive.
DR InterPro; IPR020835; Catalase_sf.
DR PANTHER; PTHR11465; PTHR11465; 1.
DR Pfam; PF00199; Catalase; 1.
DR Pfam; PF06628; Catalase-rel; 1.
DR PIRSF; PIRSF038928; Catalase_clade1-3; 1.
DR PRINTS; PR00067; CATALASE.
DR SMART; SM01060; Catalase; 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 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Heme; Hydrogen peroxide; Iron;
KW Metal-binding; Oxidoreductase; Peroxidase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10658653,
FT ECO:0000269|PubMed:8180695, ECO:0000269|Ref.7"
FT CHAIN 2..483
FT /note="Vegetative catalase"
FT /id="PRO_0000084975"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 54
FT /evidence="ECO:0000250|UniProtKB:P15202,
FT ECO:0000255|PROSITE-ProRule:PRU10013"
FT ACT_SITE 127
FT /evidence="ECO:0000250|UniProtKB:P15202"
FT BINDING 337
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|UniProtKB:P15202"
FT CONFLICT 206
FT /note="G -> P (in Ref. 1; AAA22402)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="D -> G (in Ref. 2; CAB04807)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 483 AA; 54791 MW; 63BC1F23B6A39E16 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 RFDDNGGGSV YYEPNSFGGP KESPEDKQAA YPVQGIADSV SYDHYDHYTQ
AGDLYRLMSE DERTRLVENI VNAMKPVEKE EIKLRQIEHF YKADPEYGKR VAEGLGLPIK
KDS
