ID E1WN90_BACF6 Unreviewed; 463 AA.
AC E1WN90;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Cytochrome-C peroxidase {ECO:0000313|EMBL:CBW22884.1};
GN Name=ccp {ECO:0000313|EMBL:CBW22884.1};
GN OrderedLocusNames=BF638R_2374 {ECO:0000313|EMBL:CBW22884.1};
OS Bacteroides fragilis (strain 638R).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=862962 {ECO:0000313|EMBL:CBW22884.1, ECO:0000313|Proteomes:UP000008560};
RN [1] {ECO:0000313|EMBL:CBW22884.1, ECO:0000313|Proteomes:UP000008560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=638R {ECO:0000313|EMBL:CBW22884.1,
RC ECO:0000313|Proteomes:UP000008560};
RX PubMed=20829291; DOI=10.1099/mic.0.042978-0;
RA Patrick S., Blakely G.W., Houston S., Moore J., Abratt V.R., Bertalan M.,
RA Cerdeno-Tarraga A.M., Quail M.A., Corton N., Corton C., Bignell A.,
RA Barron A., Clark L., Bentley S.D., Parkhill J.;
RT "Twenty-eight divergent polysaccharide loci specifying within- and amongst-
RT strain capsule diversity in three strains of Bacteroides fragilis.";
RL Microbiology 156:3255-3269(2010).
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DR EMBL; FQ312004; CBW22884.1; -; Genomic_DNA.
DR RefSeq; WP_005793956.1; NC_016776.1.
DR AlphaFoldDB; E1WN90; -.
DR KEGG; bfg:BF638R_2374; -.
DR PATRIC; fig|862962.3.peg.2419; -.
DR HOGENOM; CLU_034652_2_0_10; -.
DR Proteomes; UP000008560; Chromosome.
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; IPR025992; Haem-bd.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR PANTHER; PTHR30600; CYTOCHROME C PEROXIDASE-RELATED; 1.
DR PANTHER; PTHR30600:SF7; CYTOCHROME C PEROXIDASE-RELATED; 1.
DR Pfam; PF03150; CCP_MauG; 1.
DR Pfam; PF14376; Haem_bd; 1.
DR SMART; SM01235; Haem_bd; 1.
DR SUPFAM; SSF46626; Cytochrome c; 2.
DR SUPFAM; SSF48695; Multiheme cytochromes; 1.
DR PROSITE; PS51007; CYTC; 2.
PE 4: Predicted;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00433};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00433}; Oxidoreductase {ECO:0000313|EMBL:CBW22884.1};
KW Peroxidase {ECO:0000313|EMBL:CBW22884.1}.
FT DOMAIN 35..144
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 326..446
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
SQ SEQUENCE 463 AA; 51157 MW; 7AEDA896E613E318 CRC64;
MKKSTKFIIA LLVTVGALAI TYRVVNQAPS KDLAADAQMQ EIITSGGCLQ CHSGSPDLPF
YANWPVASGM VQKDVTQGYR AFDMTEMAEA LKAGKPVGKV ALAKVEKVIM DGTMPKHAYY
MVHWGSSVTD AKKEMAMAWV KQHRLAHYAN GLAAAEFANE PIRPIADSIP VDMRKVILGD
MLYHDTRLSA DNTVSCASCH GLNTGGVDNK QYSEGVGGQF GGVNAPTVYN AAYNFVQFWD
GRAGTLAEQA AGPPLNPVEM ACQSFDEIIA KLEQDANFTK AFLAVYPDGY SEQNITNAIE
EFEKTLLTPN SRFDLYLKGE KTAINDIELA GYELFKKYDC ATCHVGETLG GQSYELMGVK
RDYFADRGIE LTEEDNGRFK QTRNERDKHR FKVPGLRNIA LTAPYFHDGS MKTMKEAVDY
MAKYQMDLNL PEDELNKIVA FLETLTGEYK GKPLTNDNQT KAL
//
