ID A0A3A9Z1C7_9ACTN Unreviewed; 355 AA.
AC A0A3A9Z1C7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=D7294_12475 {ECO:0000313|EMBL:RKN42262.1};
OS Streptomyces hoynatensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1141874 {ECO:0000313|EMBL:RKN42262.1, ECO:0000313|Proteomes:UP000272474};
RN [1] {ECO:0000313|EMBL:RKN42262.1, ECO:0000313|Proteomes:UP000272474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 29097 {ECO:0000313|EMBL:RKN42262.1,
RC ECO:0000313|Proteomes:UP000272474};
RX PubMed=24243968; DOI=10.1099/ijs.0.055640-0;
RA Veyisoglu A., Sahin N.;
RT "Streptomyces hoynatensis sp. nov., isolated from deep marine sediment.";
RL Int. J. Syst. Evol. Microbiol. 64:819-826(2014).
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:RKN42262.1}.
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DR EMBL; RBAL01000006; RKN42262.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A9Z1C7; -.
DR OrthoDB; 9802613at2; -.
DR Proteomes; UP000272474; 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:SF43; CYTOCHROME BC1 COMPLEX RIESKE IRON-SULFUR SUBUNIT; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000272474};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 61..82
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 248..338
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 355 AA; 38990 MW; 0C246B501913DFE5 CRC64;
MSSHTDEPEP SPHEGEHLPS QRDEHSAVPA DDPFANPGLP PHEPRRQDID EQAAKRSERS
VSLLFALSTL ATVGFIACYV AIPIDKIVYI WPFGHVSGLN FGLGLTLGLA LFCIGAGAIH
WARTLMSDEE IVEERHAIQA PPEVKAHVLA EFRKGAAESQ IGRRRLLRNS MLGALSVVPL
AGLVLLRDLG PLPHEKLRHT RWKKGTLIVN ESTAQPLRPE DIVVGSLTQA RPDGLDPHDE
NFANEIAKAA VMLVRLQPED IKDQRSAEWG HEGILCFSKI CTHIGCPATL YEQQTHHALC
PCHQSTFDLS DGARVLFGPA GHPLPQLRIT VNDDGYLEAL GDFEEPPGPS FWERG
//