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Database: UniProt
Entry: B5GI52_STRSH
LinkDB: B5GI52_STRSH
Original site: B5GI52_STRSH 
ID   B5GI52_STRSH            Unreviewed;       350 AA.
AC   B5GI52;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2008, sequence version 1.
DT   27-MAR-2024, entry version 67.
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=SSBG_03856 {ECO:0000313|EMBL:EDY45998.2};
OS   Streptomyces sp. (strain SPB074).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=465543 {ECO:0000313|EMBL:EDY45998.2, ECO:0000313|Proteomes:UP000002779};
RN   [1] {ECO:0000313|Proteomes:UP000002779}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SPB074 {ECO:0000313|Proteomes:UP000002779};
RG   The Broad Institute Genome Sequencing Platform;
RA   Fischbach M., Ward D., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D.,
RA   Hepburn T., Sykes S., Alvarado L., Kodira C.D., Straight P., Clardy J.,
RA   Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T., Lander E.,
RA   Galagan J., Nusbaum C., Birren B.;
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EDY45998.2, ECO:0000313|Proteomes:UP000002779}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SPB074 {ECO:0000313|Proteomes:UP000002779};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "The genome sequence of Streptomyces sp. strain SPB74.";
RL   Submitted (OCT-2009) 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}.
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DR   EMBL; GG770539; EDY45998.2; -; Genomic_DNA.
DR   RefSeq; WP_008748410.1; NZ_GG770539.1.
DR   AlphaFoldDB; B5GI52; -.
DR   OrthoDB; 9802613at2; -.
DR   Proteomes; UP000002779; 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   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        55..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        96..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        161..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          262..333
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   350 AA;  38542 MW;  0F1CBE9DBC67C241 CRC64;
     MSSQDNPEEN LPAGQGAEEH SAELVKNPFA DPGLPPHEHR IQDLDERAAK RSERVVAFLF
     TLSMLATAGF IASYVIFKPG KIVYIWPFGH VSALNFSLGL TLGLALFSIG AGAVHWARTL
     MSDVELVDER HDIEADNDTR AKVIADFKQG AKDSVIGRRK LIRNSMFGAL ALVPLSGVVL
     LRDLGPLPEK KLRSTMWKKG SVIVNMNTNE PLRPEDVITG SLTFAKPEGL EETNHDFQTQ
     IAKAALMIIR IAPENIKDKR ELDWSHQGIV AYSKICTHVG CPISLYEQQT HHVLCPCHQS
     TFDLSDGARV IFGPAGHPLP QLRIGVNDEG YLEALGDFDQ PVGPAFWERG
//
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