ID   A7H2J0_CAMJD            Unreviewed;       374 AA.
AC   A7H2J0;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   SubName: Full=Ubiquinol--cytochrome c reductase, cytochrome c1 subunit {ECO:0000313|EMBL:ABS43627.1};
DE            EC=1.10.2.2 {ECO:0000313|EMBL:ABS43627.1};
GN   Name=petC {ECO:0000313|EMBL:ABS43627.1};
GN   OrderedLocusNames=JJD26997_0545 {ECO:0000313|EMBL:ABS43627.1};
OS   Campylobacter jejuni subsp. doylei (strain ATCC BAA-1458 / RM4099 /
OS   269.97).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360109 {ECO:0000313|EMBL:ABS43627.1, ECO:0000313|Proteomes:UP000002302};
RN   [1] {ECO:0000313|Proteomes:UP000002302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1458 / RM4099 / 269.97
RC   {ECO:0000313|Proteomes:UP000002302};
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT   "Complete genome sequence of Campylobacter jejuni subsp doylei 269.97
RT   isolated from human blood.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP000768; ABS43627.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7H2J0; -.
DR   KEGG; cjd:JJD26997_0545; -.
DR   HOGENOM; CLU_043937_0_0_7; -.
DR   Proteomes; UP000002302; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   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; IPR021195; Ubol_Cyt_c_Rdtase_Cyt_c_su_prd.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PIRSF; PIRSF019225; Ubol_Cyt_c_Rdtase_Cyt_c_su_prd; 1.
DR   SUPFAM; SSF46626; Cytochrome c; 2.
DR   PROSITE; PS51007; CYTC; 2.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00433}; Oxidoreductase {ECO:0000313|EMBL:ABS43627.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        348..365
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          103..208
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   DOMAIN          244..337
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   COILED          64..91
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   374 AA;  41538 MW;  FB0E4AD9AA864722 CRC64;
     MREIKIFLVV VVFTALVYWG VEPYAHSVMK PHVVPANFDF AVEDTTFAKG IVEAKELALK
     DAQASGDAKR IESANKELEK AKEELSKVET LWADVAKIDF AKGDAKKGKE FFENNCFACH
     GVKEDGIAAN ITDSSMGVIP PDLSAAGAIF DEKFLAALIM HPAFALKVDH KFGDAFIMTA
     YNKDTSGESE ETTNANIANV IAYLKDVSVK FEANEDATIK KDVEAKYAKM ENSAQKTALM
     EKDIKFAKDK ATFIEACGRC HDMKYDSFFT PSNQNDLKTY LGSVPPDLSM MIRSRGEQYL
     HDFINNTQKL LPGTAMPRVG LTEAAQAKVV SYIDQVGDSK KEERKTTGIY VMIFFVILSI
     FAIGWKRSVW SKLH
//