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Database: UniProt
Entry: Z9JXI6_9MICO
LinkDB: Z9JXI6_9MICO
Original site: Z9JXI6_9MICO 
ID   Z9JXI6_9MICO            Unreviewed;       352 AA.
AC   Z9JXI6;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
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=BF93_07750 {ECO:0000313|EMBL:EWS82904.1};
OS   Brachybacterium phenoliresistens.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC   Brachybacterium.
OX   NCBI_TaxID=396014 {ECO:0000313|EMBL:EWS82904.1, ECO:0000313|Proteomes:UP000023067};
RN   [1] {ECO:0000313|EMBL:EWS82904.1, ECO:0000313|Proteomes:UP000023067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W13A50 {ECO:0000313|EMBL:EWS82904.1,
RC   ECO:0000313|Proteomes:UP000023067};
RA   Wang X.;
RT   "Genome sequence of Brachybacterium phenoliresistens strain W13A50.";
RL   Submitted (FEB-2014) 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=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|ARBA:ARBA00034078};
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:EWS82904.1}.
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DR   EMBL; JDYK01000002; EWS82904.1; -; Genomic_DNA.
DR   RefSeq; WP_038370581.1; NZ_KK069988.1.
DR   AlphaFoldDB; Z9JXI6; -.
DR   STRING; 396014.BF93_07750; -.
DR   PATRIC; fig|396014.3.peg.546; -.
DR   eggNOG; COG0723; Bacteria.
DR   HOGENOM; CLU_050668_0_0_11; -.
DR   OrthoDB; 9802613at2; -.
DR   Proteomes; UP000023067; 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: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   InterPro; IPR005805; Rieske_Fe-S_prot_C.
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   PRINTS; PR00162; RIESKE.
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   Reference proteome {ECO:0000313|Proteomes:UP000023067};
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        51..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        91..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        160..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          268..332
FT                   /note="Rieske"
FT                   /evidence="ECO:0000259|PROSITE:PS51296"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   352 AA;  37974 MW;  D0111EDCEB2FC6C3 CRC64;
     MTDNLDGTTP AKGVSAIAPK EGGGFPNPGL PPHVHRQADT DKRAEKRAEK IVAGMFVLSI
     LGTVLFIASY FVFTPMDTNL LAEGGTLRAV FWSNLFTGLG LAIAVFFIGA AAVHWAKTLM
     PDDEMVEERH ATRSSDESRD RAVEIITGGL QESGIARRPV IVTAMVGALA ALPIAVLAPL
     STLGPLPGNK LHHTFWKPGM RLTRDHDGTP IRADEVAMNS IFHVMPEGLT EETPHFLNER
     AKAAAVIVRI DPAIGKNEES LANGHQGILA FSKICTHVGC PVALYEQQTH HMLCPCHQST
     FDVTDAAKVI FGPAHRPLPQ LPIEVDAEGY LVATGDFPEP IGPSFWDLHK DK
//
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