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KATG2_ECO57
ID   KATG2_ECO57             Reviewed;         736 AA.
AC   Q7BSW8; P77038;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Catalase-peroxidase 2 {ECO:0000255|HAMAP-Rule:MF_01961};
DE            Short=CP 2 {ECO:0000255|HAMAP-Rule:MF_01961};
DE            EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_01961};
DE   AltName: Full=Peroxidase/catalase 2 {ECO:0000255|HAMAP-Rule:MF_01961};
DE   Flags: Precursor;
GN   Name=katG2 {ECO:0000255|HAMAP-Rule:MF_01961}; Synonyms=katP;
GN   OrderedLocusNames=L7017, ECO57PM75;
OS   Escherichia coli O157:H7.
OG   Plasmid pO157.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC; PLASMID=pO157;
RX   PubMed=8969527; DOI=10.1099/13500872-142-11-3305;
RA   Brunder W., Schmidt H., Karch H.;
RT   "KatP, a novel catalase-peroxidase encoded by the large plasmid of
RT   enterohaemorrhagic Escherichia coli O157:H7.";
RL   Microbiology 142:3305-3315(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC; PLASMID=pO157;
RX   PubMed=9722640; DOI=10.1093/nar/26.18.4196;
RA   Burland V., Shao Y., Perna N.T., Plunkett G. III, Sofia H.J.,
RA   Blattner F.R.;
RT   "The complete DNA sequence and analysis of the large virulence plasmid of
RT   Escherichia coli O157:H7.";
RL   Nucleic Acids Res. 26:4196-4204(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC; PLASMID=pO157;
RX   PubMed=9628576; DOI=10.1093/dnares/5.1.1;
RA   Makino K., Ishii K., Yasunaga T., Hattori M., Yokoyama K., Yatsudo H.C.,
RA   Kubota Y., Yamaichi Y., Iida T., Yamamoto K., Honda T., Han C.G.,
RA   Ohtsubo A., Kasamatsu M., Hayashi T., Kuhara S., Shinagawa H.;
RT   "Complete nucleotide sequences of 93-kb and 3.3-kb plasmids of an
RT   enterohemorrhagic Escherichia coli O157:H7 derived from Sakai outbreak.";
RL   DNA Res. 5:1-9(1998).
CC   -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC       peroxidase activity. {ECO:0000255|HAMAP-Rule:MF_01961,
CC       ECO:0000269|PubMed:8969527}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:17499; EC=1.11.1.21; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01961};
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=1.11.1.21;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01961};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01961};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
CC       {ECO:0000255|HAMAP-Rule:MF_01961};
CC   -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000255|HAMAP-Rule:MF_01961}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:8969527}.
CC   -!- PTM: Formation of the three residue Trp-Tyr-Met cross-link is important
CC       for the catalase, but not the peroxidase activity of the enzyme.
CC       {ECO:0000255|HAMAP-Rule:MF_01961}.
CC   -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01961}.
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DR   EMBL; X89017; CAA61429.1; -; Genomic_DNA.
DR   EMBL; AF074613; AAC70085.1; -; Genomic_DNA.
DR   EMBL; AB011549; BAA31832.1; -; Genomic_DNA.
DR   PIR; T00313; T00313.
DR   RefSeq; WP_000592771.1; NZ_SEKS01000027.1.
DR   RefSeq; YP_002756743.1; NC_012487.1.
DR   AlphaFoldDB; Q7BSW8; -.
DR   SMR; Q7BSW8; -.
DR   STRING; 155864.EDL933_p0015; -.
DR   PeroxiBase; 2386; EcoH7CP02_EDL933.
DR   EnsemblBacteria; AAC70085; AAC70085; Z_L7017.
DR   EnsemblBacteria; BAA31832; BAA31832; BAA31832.
DR   KEGG; ece:Z_L7017; -.
DR   PATRIC; fig|83334.175.peg.3529; -.
DR   eggNOG; COG0376; Bacteria.
DR   HOGENOM; CLU_025424_2_0_6; -.
DR   OMA; EEIFWGP; -.
DR   Proteomes; UP000000558; Plasmid pO157.
DR   Proteomes; UP000002519; Plasmid pO157.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   HAMAP; MF_01961; Catal_peroxid; 1.
DR   InterPro; IPR000763; Catalase_peroxidase.
DR   InterPro; IPR002016; Haem_peroxidase.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR019794; Peroxidases_AS.
DR   InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR   PANTHER; PTHR30555; PTHR30555; 1.
DR   Pfam; PF00141; peroxidase; 2.
DR   PRINTS; PR00460; BPEROXIDASE.
DR   PRINTS; PR00458; PEROXIDASE.
DR   SUPFAM; SSF48113; SSF48113; 2.
DR   TIGRFAMs; TIGR00198; cat_per_HPI; 1.
DR   PROSITE; PS00435; PEROXIDASE_1; 1.
DR   PROSITE; PS00436; PEROXIDASE_2; 1.
DR   PROSITE; PS50873; PEROXIDASE_4; 1.
PE   3: Inferred from homology;
KW   Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Periplasm;
KW   Peroxidase; Plasmid; Reference proteome; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CHAIN           24..736
FT                   /note="Catalase-peroxidase 2"
FT                   /id="PRO_0000354782"
FT   ACT_SITE        103
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   BINDING         264
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   SITE            99
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CROSSLNK        102..223
FT                   /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT                   249)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CROSSLNK        223..249
FT                   /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT                   102)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ   SEQUENCE   736 AA;  81794 MW;  F3EA593D3FDEDB8D CRC64;
     MIKKTLPVLI LLALSGSFST AVAADKKETQ NFYYPETLDL TPLRLHSPES NPWGADFDYA
     TRFQQLDMEA LKKDIKDLLT TSQDWWPADY GHYGPFFIRM AWHGAGTYRT YDGRGGASGG
     QQRFEPLNSW PDNVNLDKAR RLLWPVKKKY GSSISWGDLM VLTGNVALES MGFKTLGFAG
     GREDDWESDL VYWGPDNKPL ADNRDKNGKL QKPLAATQMG LIYVNPEGPG GKPDPLASAK
     DIREAFSRMA MDDEETVALI AGGHTFGKAH GAASPEKCIG AGPDGAPVEE QGLGWKNKCG
     TGNGKYTITS GLEGAWSTSP TQFTMQYLKN LYKYEWELHK SPAGAYQWKP KKAANIVQDA
     HDPSVLHPLM MFTTDIALKV DPEYKKITTR FLNDPKAFEQ AFARAWFKLT HRDMGPAARY
     LGNEVPAESF IWQDPLPAAD YTMIDGKDIK SLKEQVMDLG IPASELIKTA WASASTFRVT
     DYRGGNNGAR IRLQPEINWE VNEPEKLKKV LASLTSLQRE FNKKQSDGKK VSLADLIVLS
     GNAAIEDAAR KAGVELEIPF TPGRTDASQE QTDVASFSVL EPTADGFRNY YSKSRSHISP
     VESLIDKASQ LDLTVPEMTA LLGGLRVMDI NTNNSSLGVF TDTPGVLDNK FFVNLLDMST
     RWSKADKEDT YNGFDRKTGA LKWKASSVDL IFSSNPELRA VAEVYASDDA RNKFIHDFVK
     SWNKVMNSDR FDLNNK
 
 
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