UCRI_RHOCA
ID UCRI_RHOCA Reviewed; 191 AA.
AC P0CY48; P07055; P08500;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 40.
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 Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=1061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=GA;
RX PubMed=3004982; DOI=10.1111/j.1432-1033.1986.tb09437.x;
RA Gabellini N., Sebald W.;
RT "Nucleotide sequence and transcription of the fbc operon from
RT Rhodopseudomonas sphaeroides. Evaluation of the deduced amino acid
RT sequences of the FeS protein, cytochrome b and cytochrome c1.";
RL Eur. J. Biochem. 154:569-579(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-95, AND SHOWS THAT SEQUENCE
RP DESCRIBED IN PUBMED:3004982 ORIGINATES FROM RHODOBACTER CAPSULATUS.
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).
RN [3]
RP MUTAGENESIS OF CYS-133; HIS-135; CYS-138; CYS-153; CYS-155; HIS-156 AND
RP HIS-159.
RC STRAIN=MT0-404;
RX PubMed=1313292; DOI=10.1021/bi00128a006;
RA Davidson E., Ohnishi T., Atta-Asafo-Adjei E., Daldal F.;
RT "Potential ligands to the [2Fe-2S] Rieske cluster of the cytochrome bc1
RT complex of Rhodobacter capsulatus probed by site-directed mutagenesis.";
RL Biochemistry 31:3342-3351(1992).
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 Note=Binds 1 [2Fe-2S] cluster per subunit.;
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}.
CC -!- CAUTION: The sequence reported in PubMed:3004982 was thought to
CC originate from R.sphaeroides but was later shown to be derived from
CC R.capsulatus. {ECO:0000305|PubMed:2821272}.
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DR EMBL; X03476; CAA27194.1; -; Genomic_DNA.
DR EMBL; M18576; AAA26151.1; -; Genomic_DNA.
DR PIR; A29336; A29336.
DR RefSeq; WP_055209364.1; NZ_QKZO01000001.1.
DR PDB; 1ZRT; X-ray; 3.50 A; E/R=1-191.
DR PDBsum; 1ZRT; -.
DR AlphaFoldDB; P0CY48; -.
DR SMR; P0CY48; -.
DR TCDB; 3.D.3.1.2; the proton-translocating quinol:cytochrome c reductase (qcr) superfamily.
DR EvolutionaryTrace; P0CY48; -.
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..191
FT /note="Ubiquinol-cytochrome c reductase iron-sulfur
FT subunit"
FT /id="PRO_0000127762"
FT TRANSMEM 18..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 94..189
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 133
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 135
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 153
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 156
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT DISULFID 138..155
FT MUTAGEN 133
FT /note="C->R,S: Photosynthetically incompetent."
FT /evidence="ECO:0000269|PubMed:1313292"
FT MUTAGEN 135
FT /note="H->L,P: Photosynthetically incompetent."
FT /evidence="ECO:0000269|PubMed:1313292"
FT MUTAGEN 138
FT /note="C->F,R,S: Photosynthetically incompetent."
FT /evidence="ECO:0000269|PubMed:1313292"
FT MUTAGEN 153
FT /note="C->R,S: Photosynthetically incompetent."
FT /evidence="ECO:0000269|PubMed:1313292"
FT MUTAGEN 155
FT /note="C->D,G,S: Photosynthetically incompetent."
FT /evidence="ECO:0000269|PubMed:1313292"
FT MUTAGEN 156
FT /note="H->L,P,F: Photosynthetically incompetent."
FT /evidence="ECO:0000269|PubMed:1313292"
FT MUTAGEN 156
FT /note="H->T,Y: Photosynthetically incompetent."
FT /evidence="ECO:0000269|PubMed:1313292"
FT MUTAGEN 159
FT /note="H->A,S: Photosynthetically competent."
FT /evidence="ECO:0000269|PubMed:1313292"
FT CONFLICT 48
FT /note="S -> A (in Ref. 2; AAA26151)"
FT /evidence="ECO:0000305"
FT HELIX 12..37
FT /evidence="ECO:0007829|PDB:1ZRT"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:1ZRT"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:1ZRT"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:1ZRT"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:1ZRT"
FT HELIX 79..86
FT /evidence="ECO:0007829|PDB:1ZRT"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:1ZRT"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:1ZRT"
FT HELIX 110..114
FT /evidence="ECO:0007829|PDB:1ZRT"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:1ZRT"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:1ZRT"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:1ZRT"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:1ZRT"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:1ZRT"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:1ZRT"
FT STRAND 179..186
FT /evidence="ECO:0007829|PDB:1ZRT"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:1ZRT"
SQ SEQUENCE 191 AA; 20416 MW; 5E6DC7E551591CC7 CRC64;
MSHAEDNAGT RRDFLYHATA ATGVVVTGAA VWPLINQMNA SADVKAMSSI FVDVSAVEVG
TQLTVKWRGK PVFIRRRDEK DIELARSVPL GALRDTSAEN ANKPGAEATD ENRSLAAFDG
TNTGEWLVML GVCTHLGCVP MGDKSGDFGG WFCPCHGSHY DSAGRIRKGP APRNLDIPVA
AFVDETTIKL G
