ID   UCRI_RHORU              Reviewed;         183 AA.
AC   P23136;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Ubiquinol-cytochrome c reductase iron-sulfur subunit;
DE            EC=7.1.1.8;
DE   AltName: Full=Rieske iron-sulfur protein;
DE            Short=RISP;
GN   Name=petA; Synonyms=fbcF;
OS   Rhodospirillum rubrum.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=1085;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-35.
RC   STRAIN=FR1;
RX   PubMed=2176269; DOI=10.1007/bf00262431;
RA   Majewski C., Trebst A.;
RT   "The pet genes of Rhodospirillum rubrum: cloning and sequencing of the
RT   genes for the cytochrome bc1-complex.";
RL   Mol. Gen. Genet. 224:373-382(1990).
CC   -!- FUNCTION: Component of the ubiquinol-cytochrome c reductase complex
CC       (complex III or cytochrome b-c1 complex), which is a respiratory chain
CC       that generates an electrochemical potential coupled to ATP synthesis.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2
CC         Fe(II)-[cytochrome c](out) + 2 H(+)(out); Xref=Rhea:RHEA:11484,
CC         Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC         ChEBI:CHEBI:132124; EC=7.1.1.8;
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00628};
CC       Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU00628};
CC   -!- SUBUNIT: The main subunits of complex b-c1 are: cytochrome b,
CC       cytochrome c1 and the Rieske protein.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane
CC       protein.
CC   -!- MISCELLANEOUS: The Rieske protein is a high potential 2Fe-2S protein.
CC   -!- SIMILARITY: Belongs to the Rieske iron-sulfur protein family.
CC       {ECO:0000305}.
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DR   EMBL; X55387; CAA39058.1; -; Genomic_DNA.
DR   PIR; S12256; RDQFBR.
DR   AlphaFoldDB; P23136; -.
DR   SMR; P23136; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:UniProtKB-EC.
DR   Gene3D; 2.102.10.10; -; 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   InterPro; IPR019546; TAT_signal_bac_arc.
DR   InterPro; IPR019470; Ubiq_cytC_Rdtase_Fe-S_su_TAT.
DR   InterPro; IPR006317; Ubiquinol_cyt_c_Rdtase_Fe-S-su.
DR   PANTHER; PTHR10134; PTHR10134; 1.
DR   Pfam; PF00355; Rieske; 1.
DR   Pfam; PF10399; UCR_Fe-S_N; 1.
DR   PRINTS; PR00162; RIESKE.
DR   SUPFAM; SSF50022; SSF50022; 1.
DR   TIGRFAMs; TIGR01416; Rieske_proteo; 1.
DR   TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR   PROSITE; PS51296; RIESKE; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   1: Evidence at protein level;
KW   2Fe-2S; Cell inner membrane; Cell membrane; Direct protein sequencing;
KW   Disulfide bond; Electron transport; Iron; Iron-sulfur; Membrane;
KW   Metal-binding; Translocase; Transmembrane; Transmembrane helix; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2176269"
FT   CHAIN           2..183
FT                   /note="Ubiquinol-cytochrome c reductase iron-sulfur
FT                   subunit"
FT                   /id="PRO_0000127763"
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          88..181
FT                   /note="Rieske"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         121
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         123
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         145
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         148
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   DISULFID        126..147
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
SQ   SEQUENCE   183 AA;  19513 MW;  915729F04701D7F9 CRC64;
     MAEAEHTAST PGGESSRRDF LIYGTTAVGA VGVALAVWPF IDFMNPAADT LALASTEVDV
     SAIAEGQAIT VTWRGKPVFV RHRTQKEIVV ARAVDPASLR DPQTDEARVQ QAQWLVMVGV
     CTHLGCIPLG QKAGDPKGDF DGWFCPCHGS HYDSAGRIRK GPAPLNLPVP PYAFTDDTTV
     LIG