ID A0A371R7Q0_9PROT Unreviewed; 438 AA.
AC A0A371R7Q0;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Cytochrome b {ECO:0000256|ARBA:ARBA00013531, ECO:0000256|RuleBase:RU003385};
GN ORFNames=DX908_14485 {ECO:0000313|EMBL:RFB01491.1};
OS Parvularcula marina.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Parvularculales;
OC Parvularculaceae; Parvularcula.
OX NCBI_TaxID=2292771 {ECO:0000313|EMBL:RFB01491.1, ECO:0000313|Proteomes:UP000264589};
RN [1] {ECO:0000313|EMBL:RFB01491.1, ECO:0000313|Proteomes:UP000264589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM1705 {ECO:0000313|EMBL:RFB01491.1,
RC ECO:0000313|Proteomes:UP000264589};
RA Sun L.;
RT "Parvularcula sp. SM1705, isolated from surface water of the South Sea
RT China.";
RL Submitted (AUG-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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cytochrome b family.
CC {ECO:0000256|RuleBase:RU003385}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RFB01491.1}.
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DR EMBL; QUQO01000002; RFB01491.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371R7Q0; -.
DR InParanoid; A0A371R7Q0; -.
DR OrthoDB; 9804503at2; -.
DR Proteomes; UP000264589; Unassembled WGS sequence.
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:UP000264589};
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 42..70
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 126..148
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 241..262
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 319..338
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 350..371
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 377..402
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 13..224
FT /note="Cytochrome b/b6 N-terminal region profile"
FT /evidence="ECO:0000259|PROSITE:PS51002"
FT DOMAIN 227..411
FT /note="Cytochrome b/b6 C-terminal region profile"
FT /evidence="ECO:0000259|PROSITE:PS51003"
FT REGION 419..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 96
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 110
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 197
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 211
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 216
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000256|PIRSR:PIRSR038885-1"
SQ SEQUENCE 438 AA; 49453 MW; E913F66BF5D98A9D CRC64;
MSHESNYVPG SGLERWLDKR LPIIRLGYDT GVDFPCPKNL NYWWTFGGIL AVCLMVQIIT
GIVLAMHYVA DSQLAFKSVE HIMRDVNYGW LIRYVHMNGA SMFFLAVYLH IARGLYYGSY
KEPREVLWMI GVLIFLLMMG TAFMGYVLPW GQMSFWGATV ISGLVTALPI IGDPIHTLLL
GGFTVDSPTL NRFFALHYLL PFVIAGLVIL HIWALHIPGN SNPTGVEAQS KKDTVPFHPY
YTVKDGFAII LFLILFAAFV YFNPNALGHP DNYIPADPLV TPAHIVPEWY FLPFYAMLRA
INFNIGIPFT DIVLINSKLG GFLVMMGSIL IWFILPWLDR SKVKSMRYRP IAKLWFFLLV
IDFFILGWLG GKPAEQPFVF FSLVGTIYYF AYFLMILPIL SVMETPTEMP KSISEAVLAD
KKKSGTGETP IASPSPAE
//
