ID A0A1G7A2S2_9ACTN Unreviewed; 516 AA.
AC A0A1G7A2S2;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Cytochrome bc1 complex cytochrome b subunit {ECO:0000256|ARBA:ARBA00016116};
DE EC=7.1.1.8 {ECO:0000256|ARBA:ARBA00012951};
DE AltName: Full=Cytochrome bc1 reductase complex subunit QcrB {ECO:0000256|ARBA:ARBA00029568};
GN ORFNames=SAMN04489747_2480 {ECO:0000313|EMBL:SDE08913.1};
OS Auraticoccus monumenti.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Auraticoccus.
OX NCBI_TaxID=675864 {ECO:0000313|EMBL:SDE08913.1, ECO:0000313|Proteomes:UP000198546};
RN [1] {ECO:0000313|EMBL:SDE08913.1, ECO:0000313|Proteomes:UP000198546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MON 2.2 {ECO:0000313|EMBL:SDE08913.1,
RC ECO:0000313|Proteomes:UP000198546};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2
CC Fe(II)-[cytochrome c](out) + 2 H(+)(out); Xref=Rhea:RHEA:11484,
CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:132124; EC=7.1.1.8;
CC Evidence={ECO:0000256|ARBA:ARBA00029351};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
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DR EMBL; LT629688; SDE08913.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7A2S2; -.
DR STRING; 675864.SAMN04489747_2480; -.
DR OrthoDB; 9804503at2; -.
DR Proteomes; UP000198546; Chromosome i.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR InterPro; IPR005797; Cyt_b/b6_N.
DR InterPro; IPR027387; Cytb/b6-like_sf.
DR InterPro; IPR016174; Di-haem_cyt_TM.
DR PANTHER; PTHR19271; CYTOCHROME B; 1.
DR PANTHER; PTHR19271:SF16; CYTOCHROME B; 1.
DR Pfam; PF13631; Cytochrom_B_N_2; 1.
DR SUPFAM; SSF81342; Transmembrane di-heme cytochromes; 1.
DR PROSITE; PS51002; CYTB_NTER; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000198546};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 47..73
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 117..138
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 214..237
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 257..280
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 336..358
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 415..434
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 23..245
FT /note="Cytochrome b/b6 N-terminal region profile"
FT /evidence="ECO:0000259|PROSITE:PS51002"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 516 AA; 55131 MW; 2283EF04A48F72BA CRC64;
MLTADRASGH GAAPKRSTTS VRVDDTAGGR LGRLVARLRA RAVPNRWSGY LGVVSGASLG
VLLVTGVVLM VFYDPSSALV RYHGSYEPLR GVEVSEAYAS TLRISLDLRG GLVLRQAHHW
AALVLPASVL LQLASLFFTG GFRRPRQWGW VLLVGVLLLA MVSGWSGYAL PDDSLSGTGL
RIVQGVALGV PVIGTWVTFV LFDGEFPGRI IENLYLVHLA APALLVVLVV VRLRMAWRDG
PAQLPGPGRS ESTVVGLPLW PAATVRAGGM FLITTGLLVL MAGTMTISPV WLYGPASPAA
ASAGSQPDWY MGFLDGALRL VPPGWEVVWL GRTWTLAVLV PLAAVGVFFT LLISYPFLES
RLTRDRQEHH LLDRPRHTPN RTGTGAAGIT FYGALWAAAS ADVIATQFHV SFEGVIWVLR
VVTVLGPLAA FVIARGACLA LQDDDHELLA HGAESGRVVR DPGGGYSEIH RPVEGRRRLG
LTRPETSPHP VLDGPPAPQA ADADQEPAVP AAGHRR
//
