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Database: UniProt
Entry: A0A2A3YDK7_9MICC
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ID   A0A2A3YDK7_9MICC        Unreviewed;       158 AA.
AC   A0A2A3YDK7;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
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=CIK74_01035 {ECO:0000313|EMBL:PCC37416.1};
OS   Glutamicibacter sp. BW77.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Glutamicibacter.
OX   NCBI_TaxID=2024402 {ECO:0000313|EMBL:PCC37416.1, ECO:0000313|Proteomes:UP000218926};
RN   [1] {ECO:0000313|EMBL:PCC37416.1, ECO:0000313|Proteomes:UP000218926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BW77 {ECO:0000313|EMBL:PCC37416.1,
RC   ECO:0000313|Proteomes:UP000218926};
RX   PubMed=28644126;
RA   Bonham K.S., Wolfe B.E., Dutton R.J.;
RT   "Extensive horizontal gene transfer in cheese-associated bacteria.";
RL   Elife 6:e22144-e22144(2017).
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=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|ARBA:ARBA00034078};
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:PCC37416.1}.
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DR   EMBL; NRGT01000008; PCC37416.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A3YDK7; -.
DR   OrthoDB; 25106at2; -.
DR   Proteomes; UP000218926; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
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; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR   InterPro; IPR014349; Rieske_Fe-S_prot.
DR   InterPro; IPR005805; Rieske_Fe-S_prot_C.
DR   InterPro; IPR006311; TAT_signal.
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; PF00355; Rieske; 1.
DR   PRINTS; PR00162; RIESKE.
DR   SUPFAM; SSF50022; ISP domain; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS51296; RIESKE; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   4: Predicted;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218926};
KW   Respiratory chain {ECO:0000256|ARBA:ARBA00022660};
KW   Transport {ECO:0000256|ARBA:ARBA00022660}.
FT   DOMAIN          77..152
FT                   /note="Rieske"
FT                   /evidence="ECO:0000259|PROSITE:PS51296"
FT   REGION          27..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..46
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   158 AA;  15976 MW;  35C6A32E3B8386D1 CRC64;
     MDSPSKPTRR TLLGAAGATG LGAALTACSP SSSPGSSEQA SAAPSPDGDG QNVMPSDQLA
     ELGKAEVTVR GPASGKDLGV LLYRPDASTV LAYSNICSHQ GCAVGTETPE ANFYCACHGS
     RYDYKDGSVL AGPAPKGLTR YAASIKGQDI VVYPPLDA
//
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