UCRI_RHOCB
ID UCRI_RHOCB Reviewed; 191 AA.
AC D5ANZ2; P07055; P08500;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 67.
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; OrderedLocusNames=RCAP_rcc02768;
OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=272942;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=2821268; DOI=10.1016/0022-2836(87)90323-8;
RA Davidson E., Daldal F.;
RT "Primary structure of the bc1 complex of Rhodopseudomonas capsulata.
RT Nucleotide sequence of the pet operon encoding the Rieske cytochrome b, and
RT cytochrome c1 apoproteins.";
RL J. Mol. Biol. 195:13-24(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=20418398; DOI=10.1128/jb.00366-10;
RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA Haselkorn R.;
RT "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT Rhodobacter capsulatus SB 1003.";
RL J. Bacteriol. 192:3545-3546(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
RC STRAIN=MT1131;
RX PubMed=1323023; DOI=10.1111/j.1365-2958.1992.tb00889.x;
RA Tokito M.K., Daldal F.;
RT "petR, located upstream of the fbcFBC operon encoding the cytochrome bc1
RT complex, is homologous to bacterial response regulators and necessary for
RT photosynthetic and respiratory growth of Rhodobacter capsulatus.";
RL Mol. Microbiol. 6:1645-1654(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 {ECO:0000250}.
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}.
CC -!- MISCELLANEOUS: The Rieske protein is a high potential 2Fe-2S protein.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Rieske iron-sulfur protein family.
CC {ECO:0000305}.
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DR EMBL; X05630; CAA29116.1; -; Genomic_DNA.
DR EMBL; CP001312; ADE86497.1; -; Genomic_DNA.
DR EMBL; Z12113; CAA78099.1; -; Genomic_DNA.
DR PIR; A29336; A29336.
DR RefSeq; WP_013068475.1; NC_014034.1.
DR PDB; 6XI0; EM; 3.30 A; E/R=1-191.
DR PDB; 6XKT; EM; 3.75 A; E/R=1-191.
DR PDB; 6XKU; EM; 4.20 A; E/R=1-191.
DR PDB; 6XKV; EM; 3.50 A; E/R=1-191.
DR PDB; 6XKW; EM; 5.20 A; E/R=1-191.
DR PDB; 6XKX; EM; 6.10 A; E/R=1-191.
DR PDB; 6XKZ; EM; 7.20 A; E/R=1-191.
DR PDBsum; 6XI0; -.
DR PDBsum; 6XKT; -.
DR PDBsum; 6XKU; -.
DR PDBsum; 6XKV; -.
DR PDBsum; 6XKW; -.
DR PDBsum; 6XKX; -.
DR PDBsum; 6XKZ; -.
DR AlphaFoldDB; D5ANZ2; -.
DR SMR; D5ANZ2; -.
DR STRING; 272942.RCAP_rcc02768; -.
DR EnsemblBacteria; ADE86497; ADE86497; RCAP_rcc02768.
DR GeneID; 31491586; -.
DR KEGG; rcp:RCAP_rcc02768; -.
DR eggNOG; COG0723; Bacteria.
DR HOGENOM; CLU_055690_0_2_5; -.
DR OMA; VFHCPCH; -.
DR OrthoDB; 1632945at2; -.
DR Proteomes; UP000002361; Chromosome.
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; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..191
FT /note="Ubiquinol-cytochrome c reductase iron-sulfur
FT subunit"
FT /id="PRO_0000409865"
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 REGION 95..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 133
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 135
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 153
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 156
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT DISULFID 138..155
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT HELIX 12..36
FT /evidence="ECO:0007829|PDB:6XI0"
FT HELIX 42..45
FT /evidence="ECO:0007829|PDB:6XI0"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:6XI0"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:6XI0"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:6XI0"
FT HELIX 79..86
FT /evidence="ECO:0007829|PDB:6XI0"
FT HELIX 110..113
FT /evidence="ECO:0007829|PDB:6XI0"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:6XI0"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:6XI0"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:6XI0"
FT TURN 146..149
FT /evidence="ECO:0007829|PDB:6XI0"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:6XI0"
FT TURN 154..157
FT /evidence="ECO:0007829|PDB:6XI0"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:6XI0"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:6XI0"
FT STRAND 180..186
FT /evidence="ECO:0007829|PDB:6XI0"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:6XI0"
SQ SEQUENCE 191 AA; 20440 MW; E7D496405154D5F4 CRC64;
MSHAEDNAGT RRDFLYHATA ATGVVVTGAA VWPLINQMNA SADVKAMASI FVDVSAVEVG
TQLTVKWRGK PVFIRRRDEK DIELARSVPL GALRDTSAEN ANKPGAEATD ENRTLPAFDG
TNTGEWLVML GVCTHLGCVP MGDKSGDFGG WFCPCHGSHY DSAGRIRKGP APRNLDIPVA
AFVDETTIKL G
