ID A0A249KFZ5_9ACTN Unreviewed; 137 AA.
AC A0A249KFZ5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=A1sIA56_02110 {ECO:0000313|EMBL:ASY15714.1};
OS Candidatus Planktophila sulfonica.
OC Bacteria; Actinomycetota; Actinomycetes; Candidatus Nanopelagicales;
OC Candidatus Nanopelagicaceae; Planktophila.
OX NCBI_TaxID=1884904 {ECO:0000313|EMBL:ASY15714.1, ECO:0000313|Proteomes:UP000217215};
RN [1] {ECO:0000313|EMBL:ASY15714.1, ECO:0000313|Proteomes:UP000217215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMS-IA-56 {ECO:0000313|EMBL:ASY15714.1};
RA Neuenschwander S.M., Salcher M., Ghai R., Pernthaler J.;
RT "High microdiversification within the ubiquitous acI lineage of
RT Actinobacteria.";
RL Submitted (JUL-2016) 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}.
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DR EMBL; CP016773; ASY15714.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A249KFZ5; -.
DR KEGG; psuf:A1sIA56_02110; -.
DR OrthoDB; 9767869at2; -.
DR Proteomes; UP000217215; Chromosome.
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; 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 SUPFAM; SSF50022; ISP domain; 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:UP000217215};
KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660};
KW Transport {ECO:0000256|ARBA:ARBA00022660}.
FT DOMAIN 44..136
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 137 AA; 13971 MW; A7097BDCC2C96306 CRC64;
MAQVSRREVL AGVCGIAALS VAGAPQASAS AVKKLADGRL SVNIKALPAL KEVGGSVRVG
SLKGQPVGLS RTGPSTFIAF SLMCPHQGVT VVKSETGWEC KAHGSQFESD GELTFGPATT
RLPQVRAKVS GSKVIIG
//
