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Database: UniProt
Entry: B9KEG9_CAMLR
LinkDB: B9KEG9_CAMLR
Original site: B9KEG9_CAMLR 
ID   B9KEG9_CAMLR            Unreviewed;       306 AA.
AC   B9KEG9;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 81.
DE   SubName: Full=Cytochrome c peroxidase {ECO:0000313|EMBL:ACM63454.1};
GN   OrderedLocusNames=Cla_0088 {ECO:0000313|EMBL:ACM63454.1};
OS   Campylobacter lari (strain RM2100 / D67 / ATCC BAA-1060).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=306263 {ECO:0000313|EMBL:ACM63454.1, ECO:0000313|Proteomes:UP000007727};
RN   [1] {ECO:0000313|EMBL:ACM63454.1, ECO:0000313|Proteomes:UP000007727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM2100 / D67 / ATCC BAA-1060
RC   {ECO:0000313|Proteomes:UP000007727};
RX   PubMed=18713059; DOI=10.1089/fpd.2008.0101;
RA   Miller W.G., Wang G., Binnewies T.T., Parker C.T.;
RT   "The complete genome sequence and analysis of the human pathogen
RT   Campylobacter lari.";
RL   Foodborne Pathog. Dis. 5:371-386(2008).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000294-1};
CC       Note=Binds 2 heme groups. {ECO:0000256|PIRSR:PIRSR000294-1};
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC   -!- PTM: Binds 2 heme groups per subunit. {ECO:0000256|PIRSR:PIRSR000294-
CC       1}.
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DR   EMBL; CP000932; ACM63454.1; -; Genomic_DNA.
DR   RefSeq; WP_012660840.1; NC_012039.1.
DR   AlphaFoldDB; B9KEG9; -.
DR   STRING; 306263.Cla_0088; -.
DR   GeneID; 7411320; -.
DR   KEGG; cla:CLA_0088; -.
DR   PATRIC; fig|306263.5.peg.87; -.
DR   eggNOG; COG1858; Bacteria.
DR   HOGENOM; CLU_034652_1_0_7; -.
DR   OMA; CGFCHIQ; -.
DR   Proteomes; UP000007727; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.760.10; Cytochrome c-like domain; 2.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR004852; Di-haem_cyt_c_peroxidsae.
DR   InterPro; IPR026259; MauG/Cytc_peroxidase.
DR   PANTHER; PTHR30600; CYTOCHROME C PEROXIDASE-RELATED; 1.
DR   PANTHER; PTHR30600:SF7; CYTOCHROME C PEROXIDASE-RELATED; 1.
DR   Pfam; PF03150; CCP_MauG; 1.
DR   PIRSF; PIRSF000294; Cytochrome-c_peroxidase; 1.
DR   SUPFAM; SSF46626; Cytochrome c; 2.
DR   PROSITE; PS51007; CYTC; 1.
PE   4: Predicted;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000294-1};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000294-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000294-2};
KW   Oxidoreductase {ECO:0000313|EMBL:ACM63454.1};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Peroxidase {ECO:0000313|EMBL:ACM63454.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007727}.
FT   DOMAIN          184..298
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   BINDING         54
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000294-1"
FT   BINDING         57
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000294-1"
FT   BINDING         58
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000294-2"
FT   BINDING         198
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000294-1"
FT   BINDING         201
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000294-1"
FT   BINDING         202
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000294-2"
FT   BINDING         273
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000294-2"
SQ   SEQUENCE   306 AA;  34711 MW;  26EF6EDEA5BCFD8E CRC64;
     MKTFIILIFS LLPLLALEMI TPLPESIPYD KEKAILGKKL YMDTSLSKDK KVSCNTCHDI
     TKFGVDNKTF STGINGIIDE PFHTPTNFNA VFNLSQFWRG NAKDLQDQAK HPLLNPKEMG
     LKDESEVIQI VKANPIYEKE FKKLYGEVNF ENITHALAEF QKTLLTPNSP FDRYLKGEKN
     AISEQAKRGY NAFLSNGCIA CHQGQNIGGN MYQKMGVFVP YDNGTNWKGR YEITQDPHDQ
     FVVKVPSLRN IAKTAPYFHD GSMPTLDACV QFMAYYQLGK FLEQNVVDDI VAFLNSLTGE
     YHDPLK
//
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