ID A0A2R8BJZ9_9RHOB Unreviewed; 448 AA.
AC A0A2R8BJZ9;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Cytochrome b {ECO:0000256|ARBA:ARBA00013531, ECO:0000256|RuleBase:RU003385};
GN Name=petB {ECO:0000313|EMBL:SPH23716.1};
GN ORFNames=DEA8626_02783 {ECO:0000313|EMBL:SPH23716.1};
OS Defluviimonas aquaemixtae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Defluviimonas.
OX NCBI_TaxID=1542388 {ECO:0000313|EMBL:SPH23716.1, ECO:0000313|Proteomes:UP000244924};
RN [1] {ECO:0000313|EMBL:SPH23716.1, ECO:0000313|Proteomes:UP000244924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8626 {ECO:0000313|EMBL:SPH23716.1,
RC ECO:0000313|Proteomes:UP000244924};
RA Keele B.F.;
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the ubiquinol-cytochrome c reductase complex
CC (complex III or cytochrome b-c1 complex), which is a respiratory chain
CC that generates an electrochemical potential coupled to ATP synthesis.
CC {ECO:0000256|ARBA:ARBA00002444, ECO:0000256|RuleBase:RU003385}.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|RuleBase:RU003385};
CC Note=Binds 2 heme groups non-covalently.
CC {ECO:0000256|RuleBase:RU003385};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|PIRSR:PIRSR038885-2};
CC Note=Binds 2 heme groups non-covalently.
CC {ECO:0000256|PIRSR:PIRSR038885-2};
CC -!- SUBUNIT: The main subunits of complex b-c1 are: cytochrome b,
CC cytochrome c1 and the Rieske protein. {ECO:0000256|ARBA:ARBA00011649,
CC ECO:0000256|RuleBase:RU003385}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cytochrome b family.
CC {ECO:0000256|RuleBase:RU003385}.
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DR EMBL; OMOQ01000002; SPH23716.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R8BJZ9; -.
DR OrthoDB; 9804503at2; -.
DR Proteomes; UP000244924; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045275; C:respiratory chain complex III; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:InterPro.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR CDD; cd00290; cytochrome_b_C; 1.
DR CDD; cd00284; Cytochrome_b_N; 1.
DR InterPro; IPR005798; Cyt_b/b6_C.
DR InterPro; IPR036150; Cyt_b/b6_C_sf.
DR InterPro; IPR005797; Cyt_b/b6_N.
DR InterPro; IPR027387; Cytb/b6-like_sf.
DR InterPro; IPR030689; Cytochrome_b.
DR InterPro; IPR048260; Cytochrome_b_C_euk/bac.
DR InterPro; IPR048259; Cytochrome_b_N_euk/bac.
DR InterPro; IPR016174; Di-haem_cyt_TM.
DR PANTHER; PTHR19271; CYTOCHROME B; 1.
DR PANTHER; PTHR19271:SF16; CYTOCHROME B; 1.
DR Pfam; PF00032; Cytochrom_B_C; 1.
DR Pfam; PF00033; Cytochrome_B; 1.
DR PIRSF; PIRSF038885; COB; 1.
DR SUPFAM; SSF81648; a domain/subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase); 1.
DR SUPFAM; SSF81342; Transmembrane di-heme cytochromes; 1.
DR PROSITE; PS51003; CYTB_CTER; 1.
DR PROSITE; PS51002; CYTB_NTER; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW ECO:0000256|RuleBase:RU003385};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR038885-2};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR038885-2};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR038885-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000244924};
KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660,
KW ECO:0000256|RuleBase:RU003385};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003385};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003385}.
FT TRANSMEM 44..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 95..117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 155..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 194..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 253..275
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 296..318
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 388..411
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 15..225
FT /note="Cytochrome b/b6 N-terminal region profile"
FT /evidence="ECO:0000259|PROSITE:PS51002"
FT DOMAIN 234..422
FT /note="Cytochrome b/b6 C-terminal region profile"
FT /evidence="ECO:0000259|PROSITE:PS51003"
FT BINDING 97
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="b562"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR038885-2"
FT BINDING 111
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="b566"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR038885-2"
FT BINDING 198
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="b562"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR038885-2"
FT BINDING 212
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="b566"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR038885-2"
FT BINDING 217
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000256|PIRSR:PIRSR038885-1"
SQ SEQUENCE 448 AA; 50699 MW; BFBC1E005EB4D753 CRC64;
MAGIPHDHYE PKSGFEQWLH RRLPIVGLMY DTLMIPTPKN LNWWWIWGIV LTFCLVLQIV
TGIVLAMHYT PHVDQAFASI EHIMRNVNGG HMLRYIHANG ASLFFLAVYI HIFRGLFYGS
YKSPREVTWI IGILIFVAMM GTAFMGYVLP WGQMSFWGAT VITGLFGAIP GIGEPIQTWL
LGGPAVENAT LNRFFSLHYL LPFVIAALVA VHIWAFHTTG NNNPTGVEVR RGSKAEAEKD
TLPFWPYFVM KDLFALSLIL VVFFAIVGFM PNYLGHPDNY IEANPLATPA HIVPEWYFLP
FYAILRAFTG DVWLVQLVQF ITFGIVDAKF FGVVAMFGAI IVMALAPWLD TSSVRSGQYR
PMFRWWFYLL IIDFVVLMWV GAQPAEGIYT WISLIASAYW FAYFLVILPL LGVIEKPSAP
PATIEEDFKA HYAGAETPPP YVSQKPAE
//
