ID M1UG94_9CORY Unreviewed; 408 AA.
AC M1UG94;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=H924_09235 {ECO:0000313|EMBL:AGG67285.1};
OS Corynebacterium callunae DSM 20147.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1121353 {ECO:0000313|EMBL:AGG67285.1, ECO:0000313|Proteomes:UP000011760};
RN [1] {ECO:0000313|EMBL:AGG67285.1, ECO:0000313|Proteomes:UP000011760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20147 {ECO:0000313|EMBL:AGG67285.1,
RC ECO:0000313|Proteomes:UP000011760};
RA Ruckert C., Albersmeier A., Kalinowski J.;
RT "The complete genome sequence of Corynebacterium callunae DSM 20147.";
RL Submitted (FEB-2013) 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}.
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DR EMBL; CP004354; AGG67285.1; -; Genomic_DNA.
DR RefSeq; WP_015651716.1; NZ_ATVF01000003.1.
DR AlphaFoldDB; M1UG94; -.
DR STRING; 1121353.H924_09235; -.
DR KEGG; ccn:H924_09235; -.
DR PATRIC; fig|1121353.3.peg.1883; -.
DR eggNOG; COG0723; Bacteria.
DR HOGENOM; CLU_050668_0_0_11; -.
DR OrthoDB; 9802613at2; -.
DR Proteomes; UP000011760; Chromosome.
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 58..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 89..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 162..183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 296..390
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 408 AA; 45390 MW; 0022307A7342EACC CRC64;
MSNNINKQYT KQELNAMSNE DLARLGTELD DVTIAYRKER FPIANDPAEK RASRLINFWL
ILGIIGGLGF LATYIFWPWH YKGHGDEGLF LYTLYTPMLG ITSGLCILGL GFAVTLYVKK
FIPEEIAVQR RHDGPSEEVD RRTLVALLND SWQTSTLGRR KLLMGLAGGG AVLAGLTIIA
PLGGMIKNPW KPKEGPMDVQ GDGTLWTSGW TLIENNVKVY LGRDTAAIAE SHTDATGEHW
STTGVSRLVR MRPEDLAAAS METVFPLPEE MVNDGAEYDP AKDVYEHQMH SVHGPRNAVM
LIRLRTADAE KVVEREGQET FHYGDYYAYS KICTHIGCPT SLYEAQTNRI LCPCHQSQFD
ALHYGKPVFG PAARALPQLP ITVDEEGYLV AAGNFIEPVG PAFWERKS
//
