ID A0A078M181_9PSED Unreviewed; 269 AA.
AC A0A078M181;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Ubiquinol--cytochrome c reductase, cytochrome c1 {ECO:0000313|EMBL:CDZ95831.1};
GN Name=petC {ECO:0000313|EMBL:CDZ95831.1};
GN ORFNames=BN1079_03175 {ECO:0000313|EMBL:CDZ95831.1};
OS Pseudomonas saudiphocaensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1499686 {ECO:0000313|EMBL:CDZ95831.1, ECO:0000313|Proteomes:UP000053902};
RN [1] {ECO:0000313|EMBL:CDZ95831.1, ECO:0000313|Proteomes:UP000053902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=20_BN {ECO:0000313|EMBL:CDZ95831.1,
RC ECO:0000313|Proteomes:UP000053902};
RA Urmite Genomes Urmite Genomes;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000256|PIRSR:PIRSR602326-1};
CC Note=Binds 1 heme c group covalently per subunit.
CC {ECO:0000256|PIRSR:PIRSR602326-1};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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DR EMBL; CCSF01000001; CDZ95831.1; -; Genomic_DNA.
DR RefSeq; WP_037025994.1; NZ_CCSF01000001.1.
DR AlphaFoldDB; A0A078M181; -.
DR STRING; 1499686.BN1079_03175; -.
DR eggNOG; COG2857; Bacteria.
DR HOGENOM; CLU_078597_0_0_6; -.
DR OrthoDB; 9798864at2; -.
DR Proteomes; UP000053902; Unassembled WGS sequence.
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; 1.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR002326; Cyt_c1.
DR PANTHER; PTHR10266; CYTOCHROME C1; 1.
DR PANTHER; PTHR10266:SF3; CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF02167; Cytochrom_C1; 2.
DR SUPFAM; SSF46626; Cytochrome c; 1.
PE 4: Predicted;
KW Heme {ECO:0000256|PIRSR:PIRSR602326-1};
KW Iron {ECO:0000256|PIRSR:PIRSR602326-1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR602326-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053902};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..269
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001741761"
FT TRANSMEM 242..260
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 50
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR602326-1"
FT BINDING 53
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR602326-1"
FT BINDING 54
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR602326-1"
SQ SEQUENCE 269 AA; 29871 MW; 08D40C60B77F648E CRC64;
MKKQFAALIL ALVPAFGFAA GPSVALDKVD IDLTDKAALQ DGLQTFANYC MGCHSAQYQR
YERVATDLGI PEEVMMDNIV FSDAKIGDHM KIGMTPDDAK AWFGAAPPDL TLVARVRGTD
WLYSYMRGFY VDPSRPYGFN NTVFPNVGMP HVLAPLQGLQ VLPSTLPEGE SVACKQVQVV
ENGRKQFDPL TGTPITHEDC EQLTVVPGSG ELTEAEYDEK IKNLVTFLAY SANPVKLESQ
RIGTYVLLFL AVFFVFAYLL KREYWKDVH
//