ID A0A3S0BH56_9CORY Unreviewed; 406 AA.
AC A0A3S0BH56;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Cytochrome bc1 complex Rieske iron-sulfur subunit {ECO:0000256|ARBA:ARBA00015816};
DE AltName: Full=Cytochrome bc1 reductase complex subunit QcrA {ECO:0000256|ARBA:ARBA00029586};
DE AltName: Full=Rieske iron-sulfur protein {ECO:0000256|ARBA:ARBA00032409};
GN ORFNames=EAH68_09005 {ECO:0000313|EMBL:RSZ62707.1};
OS Corynebacterium hylobatis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1859290 {ECO:0000313|EMBL:RSZ62707.1, ECO:0000313|Proteomes:UP000274907};
RN [1] {ECO:0000313|EMBL:RSZ62707.1, ECO:0000313|Proteomes:UP000274907}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 101343 {ECO:0000313|EMBL:RSZ62707.1,
RC ECO:0000313|Proteomes:UP000274907};
RA Chen X.;
RT "YIM 101343 draft genome.";
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Iron-sulfur subunit of the cytochrome bc1 complex, an
CC essential component of the respiratory electron transport chain
CC required for ATP synthesis. The bc1 complex catalyzes the oxidation of
CC menaquinol and the reduction of cytochrome c in the respiratory chain.
CC The bc1 complex operates through a Q-cycle mechanism that couples
CC electron transfer to generation of the proton gradient that drives ATP
CC synthesis. {ECO:0000256|ARBA:ARBA00002494}.
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962};
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 -!- 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:RSZ62707.1}.
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DR EMBL; RXHJ01000010; RSZ62707.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S0BH56; -.
DR OrthoDB; 9802613at2; -.
DR Proteomes; UP000274907; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProt.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR CDD; cd03467; Rieske; 1.
DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR InterPro; IPR045603; QcrA_N.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR014349; Rieske_Fe-S_prot.
DR PANTHER; PTHR10134; CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR10134:SF20; CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF19297; QcrA_N; 1.
DR Pfam; PF00355; Rieske; 1.
DR SUPFAM; SSF50022; ISP domain; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Electron transport {ECO:0000256|ARBA:ARBA00022660};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022660}.
FT TRANSMEM 56..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 97..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 294..388
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 406 AA; 44977 MW; 8C7B5037C1F548AB CRC64;
MSNEVKKNYT AQELNAMSND ELARLGTELD DVTVAYRKER FPVPNDPAEK RAARNVGIWL
VVGIIAAIAF LGVYIFWPWE FRNLGEEGHM WHTFYTPMLG LTSGISILGL GMAVILYVKN
IIPEEISVQR RHDGPSSEVD RRTLTALLND SWTTSTLGRR KALQGLLGGA GILAGLVIVA
PLGGMIKNPW KRGEMNIMGD GTLWTSGWTL QEQGVKLYLA RDTGAIAENH TGEAGSHWST
VGVSRLVRVR PEDLDAGGME TVYPLPESLV NDGDLFDPQA SVYTEQMHSI HGPRNPVMLI
RLRTEDAQKA IERQGQEDFH YGDYYAYSKI CTHIGCPTSL FEAQTNRILC PCHQSQFDAL
QYGKPVFGPA ARALPQLPIE VDEEGYLIAA GNFVESVGAA FWERRS
//
