UCRI_PARDE
ID UCRI_PARDE Reviewed; 190 AA.
AC P05417;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 120.
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;
OS Paracoccus denitrificans.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=266;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2820981; DOI=10.1016/s0021-9258(19)76497-7;
RA Kurowski B., Ludwig B.;
RT "The genes of the Paracoccus denitrificans bc1 complex. Nucleotide sequence
RT and homologies between bacterial and mitochondrial subunits.";
RL J. Biol. Chem. 262:13805-13811(1987).
RN [2]
RP PROTEIN SEQUENCE OF 17-23 AND 37-60.
RX PubMed=7601123; DOI=10.1111/j.1432-1033.1995.tb20571.x;
RA Kleymann G., Iwata S., Wiesmueller K.-H., Ludwig B., Haase W., Michel H.;
RT "Immunoelectron microscopy and epitope mapping with monoclonal antibodies
RT suggest the existence of an additional N-terminal transmembrane helix in
RT the cytochrome b subunit of bacterial ubiquinol:cytochrome-c
RT oxidoreductases.";
RL Eur. J. Biochem. 230:359-363(1995).
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; M17522; AAA25571.1; -; Genomic_DNA.
DR EMBL; X05799; CAA29243.1; -; Genomic_DNA.
DR PIR; A29413; A29413.
DR RefSeq; WP_074810391.1; NZ_FOYK01000005.1.
DR PDB; 2YIU; X-ray; 2.70 A; C/F=1-190.
DR PDBsum; 2YIU; -.
DR AlphaFoldDB; P05417; -.
DR SMR; P05417; -.
DR TCDB; 3.D.3.1.1; the proton-translocating quinol:cytochrome c reductase (qcr) superfamily.
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; Direct protein sequencing;
KW Disulfide bond; Electron transport; Iron; Iron-sulfur; Membrane;
KW Metal-binding; Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..190
FT /note="Ubiquinol-cytochrome c reductase iron-sulfur
FT subunit"
FT /id="PRO_0000127761"
FT TRANSMEM 18..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 95..188
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 132
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 134
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 BINDING 155
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT DISULFID 137..154
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT HELIX 19..40
FT /evidence="ECO:0007829|PDB:2YIU"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:2YIU"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:2YIU"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:2YIU"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:2YIU"
FT HELIX 83..91
FT /evidence="ECO:0007829|PDB:2YIU"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:2YIU"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:2YIU"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:2YIU"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:2YIU"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:2YIU"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:2YIU"
FT TURN 153..156
FT /evidence="ECO:0007829|PDB:2YIU"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:2YIU"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:2YIU"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:2YIU"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:2YIU"
SQ SEQUENCE 190 AA; 20300 MW; F83F5D9A9C1FBEE4 CRC64;
MSHADEHAGD HGATRRDFLY YATAGAGTVA AGAAAWTLVN QMNPSADVQA LASIQVDVSG
VETGTQLTVK WLGKPVFIRR RTEDEIQAGR EVDLGQLIDR SAQNSNKPDA PATDENRTMD
EAGEWLVMIG VCTHLGCVPI GDGAGDFGGW FCPCHGSHYD TSGRIRRGPA PQNLHIPVAE
FLDDTTIKLG
