UCRI_CERSP
ID UCRI_CERSP Reviewed; 187 AA.
AC Q02762; P72327;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 126.
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 Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=1063;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2176595; DOI=10.1111/j.1432-1033.1990.tb15633.x;
RA Yun C.-H., Beci R., Crofts A.R., Kaplan S., Gennis R.B.;
RT "Cloning and DNA sequencing of the fbc operon encoding the cytochrome bc1
RT complex from Rhodobacter sphaeroides. Characterization of fbc deletion
RT mutants and complementation by a site-specific mutational variant.";
RL Eur. J. Biochem. 194:399-411(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-95.
RX PubMed=2821272; DOI=10.1016/0022-2836(87)90324-x;
RA Davidson E., Daldal F.;
RT "fbc operon, encoding the Rieske Fe-S protein cytochrome b, and cytochrome
RT c1 apoproteins previously described from Rhodopseudomonas sphaeroides, is
RT from Rhodopseudomonas capsulata.";
RL J. Mol. Biol. 195:25-29(1987).
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 membrane; Single-pass membrane 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; X56157; CAA39623.1; -; Genomic_DNA.
DR EMBL; M18577; AAA26150.1; -; Genomic_DNA.
DR PIR; S13868; S13868.
DR RefSeq; WP_002722009.1; NZ_QXDK01000004.1.
DR PDB; 2FYN; X-ray; 3.20 A; C/F/I/L/O/R=1-187.
DR PDB; 2NUK; X-ray; 1.20 A; A=47-187.
DR PDB; 2NUM; X-ray; 1.50 A; A=47-187.
DR PDB; 2NVE; X-ray; 1.50 A; A=47-187.
DR PDB; 2NVF; X-ray; 1.50 A; A=47-187.
DR PDB; 2NVG; X-ray; 1.35 A; A=47-187.
DR PDB; 2NWF; X-ray; 1.10 A; A=47-187.
DR PDB; 2QJK; X-ray; 3.10 A; C/F/I/L/O/R=9-187.
DR PDB; 2QJP; X-ray; 2.60 A; C/F/I/L=9-187.
DR PDB; 2QJY; X-ray; 2.40 A; C/F/I/L/O/R=1-187.
DR PDB; 5KKZ; X-ray; 2.97 A; C/G/M/Q=1-187.
DR PDB; 5KLI; X-ray; 3.00 A; C/G/M/Q=1-187.
DR PDBsum; 2FYN; -.
DR PDBsum; 2NUK; -.
DR PDBsum; 2NUM; -.
DR PDBsum; 2NVE; -.
DR PDBsum; 2NVF; -.
DR PDBsum; 2NVG; -.
DR PDBsum; 2NWF; -.
DR PDBsum; 2QJK; -.
DR PDBsum; 2QJP; -.
DR PDBsum; 2QJY; -.
DR PDBsum; 5KKZ; -.
DR PDBsum; 5KLI; -.
DR AlphaFoldDB; Q02762; -.
DR SMR; Q02762; -.
DR DIP; DIP-61258N; -.
DR IntAct; Q02762; 1.
DR DrugBank; DB03152; B-2-Octylglucoside.
DR DrugBank; DB08690; Ubiquinone Q2.
DR TCDB; 3.E.2.1.1; the photosynthetic reaction center (prc) family.
DR GeneID; 57468753; -.
DR GeneID; 67448165; -.
DR OMA; KRTWLIA; -.
DR OrthoDB; 1632945at2; -.
DR EvolutionaryTrace; Q02762; -.
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; 3D-structure; Cell membrane; Disulfide bond; Electron transport;
KW Iron; Iron-sulfur; Membrane; Metal-binding; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..187
FT /note="Ubiquinol-cytochrome c reductase iron-sulfur
FT subunit"
FT /id="PRO_0000127764"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 89..185
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 129
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 131
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 149
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 152
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT DISULFID 134..151
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT HELIX 10..36
FT /evidence="ECO:0007829|PDB:2QJY"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:2QJY"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:2NWF"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:2NWF"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:2NWF"
FT HELIX 79..86
FT /evidence="ECO:0007829|PDB:2NWF"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:2NWF"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:2QJP"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:2NWF"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:2NWF"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:2NWF"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:2NWF"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:2NWF"
FT TURN 142..145
FT /evidence="ECO:0007829|PDB:2NWF"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:2NWF"
FT TURN 150..153
FT /evidence="ECO:0007829|PDB:2NWF"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:2NWF"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:2NWF"
FT STRAND 175..186
FT /evidence="ECO:0007829|PDB:2NWF"
SQ SEQUENCE 187 AA; 19910 MW; 575B47EEEECD74D2 CRC64;
MSNAEDHAGT RRDFLYYATA GAGAVATGAA VWPLINQMNP SADVQALASI FVDVSSVEPG
VQLTVKFLGK PIFIRRRTEA DIELGRSVQL GQLVDTNARN ANIDAGAEAT DQNRTLDEAG
EWLVMWGVCT HLGCVPIGGV SGDFGGWFCP CHGSHYDSAG RIRKGPAPEN LPIPLAKFID
ETTIQLG
