CATA_STAA8
ID CATA_STAA8 Reviewed; 505 AA.
AC Q2FYU7;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Catalase;
DE EC=1.11.1.6;
GN Name=katA; OrderedLocusNames=SAOUHSC_01327;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [2]
RP FUNCTION, AND REGULATION BY PERR.
RX PubMed=11349039; DOI=10.1128/iai.69.6.3744-3754.2001;
RA Horsburgh M.J., Clements M.O., Crossley H., Ingham E., Foster S.J.;
RT "PerR controls oxidative stress resistance and iron storage proteins and is
RT required for virulence in Staphylococcus aureus.";
RL Infect. Immun. 69:3744-3754(2001).
RN [3]
RP INDUCTION BY HYPOCHLOROUS ACID.
RX PubMed=16514164; DOI=10.1099/mic.0.28385-0;
RA Maalej S., Dammak I., Dukan S.;
RT "The impairment of superoxide dismutase coordinates the derepression of the
RT perR regulon in the response of Staphylococcus aureus to HOCl stress.";
RL Microbiology 152:855-861(2006).
RN [4]
RP FUNCTION, AND INDUCTION BY FUR.
RX PubMed=17114262; DOI=10.1128/jb.01524-06;
RA Cosgrove K., Coutts G., Jonsson I.-M., Tarkowski A., Kokai-Kun J.F.,
RA Mond J.J., Foster S.J.;
RT "Catalase (katA) and alkyl hydroperoxide reductase (ahpC) have compensatory
RT roles in peroxide stress resistance and are required for survival,
RT persistence and nasal colonization in Staphylococcus aureus.";
RL J. Bacteriol. 189:1025-1035(2007).
CC -!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to
CC protect cells from the toxic effects of hydrogen peroxide. Involved in
CC resistance to paraquat when fur is absent and to tert-butyl
CC hydroperoxide. Is important for survival under glucose starvation and
CC desiccation conditions. Not required for virulence although is
CC necessary for nasal colonization. {ECO:0000269|PubMed:11349039,
CC ECO:0000269|PubMed:17114262}.
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; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- INDUCTION: Induced by hypochlorous acid. Positively regulated by the
CC ferric uptake regulator (fur), in a Fe(2+) dependent manner. Negatively
CC regulated by PerR. {ECO:0000269|PubMed:16514164,
CC ECO:0000269|PubMed:17114262}.
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABD30425.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000253; ABD30425.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000082539.1; NZ_LS483365.1.
DR RefSeq; YP_499857.1; NC_007795.1.
DR AlphaFoldDB; Q2FYU7; -.
DR SMR; Q2FYU7; -.
DR STRING; 1280.SAXN108_1351; -.
DR EnsemblBacteria; ABD30425; ABD30425; SAOUHSC_01327.
DR GeneID; 3920192; -.
DR KEGG; sao:SAOUHSC_01327; -.
DR PATRIC; fig|93061.5.peg.1213; -.
DR eggNOG; COG0753; Bacteria.
DR HOGENOM; CLU_010645_2_0_9; -.
DR Proteomes; UP000008816; 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 2: Evidence at transcript level;
KW Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Reference proteome.
FT CHAIN 1..505
FT /note="Catalase"
FT /id="PRO_0000278273"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT ACT_SITE 129
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT BINDING 339
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"
SQ SEQUENCE 505 AA; 58380 MW; F6A17136A32DCBCC CRC64;
MSQQDKKLTG VFGHPVSDRE NSMTAGPRGP LLMQDIYFLE QMSQFDREVI PERRMHAKGS
GAFGTFTVTK DITKYTNAKI FSEIGKQTEM FARFSTVAGE RGAADAERDI RGFALKFYTE
EGNWDLVGNN TPVFFFRDPK LFVSLNRAVK RDPRTNMRDA QNNWDFWTGL PEALHQVTIL
MSDRGIPKDL RHMHGFGSHT YSMYNDSGER VWVKFHFRTQ QGIENLTDEE AAEIIATDRD
SSQRDLFEAI EKGDYPKWTM YIQVMTEEQA KNHKDNPFDL TKVWYHDEYP LIEVGEFELN
RNPDNYFMDV EQAAFAPTNI IPGLDFSPDK MLQGRLFSYG DAQRYRLGVN HWQIPVNQPK
GVGIENICPF SRDGQMRVVD NNQGGGTHYY PNNHGKFDSQ PEYKKPPFPT DGYGYEYNQR
QDDDNYFEQP GKLFRLQSED AKERIFTNTA NAMEGVTDDV KRRHIRHCYK ADPEYGKGVA
KALGIDINSI DLETENDETY ENFEK
