ID   CATB_STAAU              Reviewed;         455 AA.
AC   Q9L4S2;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Catalase-like protein;
GN   Name=katB;
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND LACK OF CATALASE ACTIVITY.
RC   STRAIN=Subsp. anaerobius / MVF 213;
RX   PubMed=10708385; DOI=10.1099/00221287-146-2-465;
RA   Sanz R., Marin I., Ruiz-Santa-Quiteria J.A., Orden J.A., Cid D., Diez R.M.,
RA   Silhadi K.S., Amils R., de la Fuente R.;
RT   "Catalase deficiency in Staphylococcus aureus subsp. anaerobius is
RT   associated with natural loss-of-function mutations within the structural
RT   gene.";
RL   Microbiology 146:465-475(2000).
CC   -!- FUNCTION: Catalytically inactive.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
CC   -!- CAUTION: Although a transcript has been detected, this protein has no
CC       catalase activity. Comparison with orthologs shows that the last 50 C-
CC       terminal amino acids, which seem to be essential for activity, are
CC       missing due to a natural frameshift in position 446. The sequence also
CC       contains six missense mutations, including the replacement of Pro-317
CC       with Ser, which could modify the structure of the protein. Both
CC       alterations seem to contribute to the lack of catalase activity.
CC       {ECO:0000305}.
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DR   EMBL; AJ000471; CAB76840.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9L4S2; -.
DR   SMR; Q9L4S2; -.
DR   GO; GO:0004096; F:catalase activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:InterPro.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
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; IPR020835; Catalase_sf.
DR   PANTHER; PTHR11465; PTHR11465; 1.
DR   Pfam; PF00199; Catalase; 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   3: Inferred from homology;
FT   CHAIN           1..455
FT                   /note="Catalase-like protein"
FT                   /id="PRO_0000279382"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   455 AA;  52618 MW;  E29A5B259D642CAC CRC64;
     MSQQDKKLTG VFGHPVSDRE NSMTAGPRGP LLMQDIYFLE QMSQFDREVI PERRMHAKGS
     GAFGTFTVTK DITKYTNAKI FSEIGKQTEM FARFSTVAGE RGAADAESDI RGFALKFYTE
     EGNWDLVGNN TPVFFFRDPK LFVSLNRAVK RDPRTNMRDA QNNWDFWTGL PEALHQVTIL
     MSDRGIPKDL RHMHGFGSHT YSMYNDSGER VWVKLHFRTQ QGIENLTDEE AAEIIATGRD
     SSQRDLFEAI EKGDYPKWTM YIQVMTEEQA KNHKDNPFDL TKVWYHDEYP LIEVGEFELN
     RNPDNYFMDV EQVAFASTNI IPGLDFSPDK MLQGRLFSYG DAQRYRLGVN HWQIPVNQPK
     GVGIENICPF SRDGQMRVVD NNQGGGTHYY PNNHGKFDSQ PEYKKPPFPT DGYGYEYNQR
     QDDDNYFEQP GKLFRLQSEG AKERILQIQQ MQWKA