ID S5ABE4_9ALTE Unreviewed; 210 AA. AC S5ABE4; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 24-JAN-2024, entry version 53. DE RecName: Full=Ubiquinol-cytochrome c reductase iron-sulfur subunit {ECO:0000256|ARBA:ARBA00019816, ECO:0000256|RuleBase:RU004494}; DE EC=7.1.1.8 {ECO:0000256|ARBA:ARBA00012951, ECO:0000256|RuleBase:RU004494}; GN ORFNames=I633_03930 {ECO:0000313|EMBL:AGP77055.1}; OS Alteromonas mediterranea 615. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas. OX NCBI_TaxID=1300253 {ECO:0000313|EMBL:AGP77055.1, ECO:0000313|Proteomes:UP000014909}; RN [1] {ECO:0000313|EMBL:AGP77055.1, ECO:0000313|Proteomes:UP000014909} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN='English Channel 615' {ECO:0000313|Proteomes:UP000014909}; RX PubMed=23729633; DOI=10.1093/gbe/evt089; RA Lopez-Perez M., Gonzaga A., Rodriguez-Valera F.; RT "Genomic Diversity of "Deep Ecotype" Alteromonas macleodii Isolates: RT Evidence for Pan-Mediterranean Clonal Frames."; RL Genome Biol. Evol. 5:1220-1232(2013). 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:0000256|ARBA:ARBA00002444}. 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 Evidence={ECO:0000256|ARBA:ARBA00029351, CC ECO:0000256|RuleBase:RU004494}; CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; CC Evidence={ECO:0000256|RuleBase:RU004494}; CC Note=Binds 1 [2Fe-2S] cluster per subunit. CC {ECO:0000256|RuleBase:RU004494}; CC -!- SUBUNIT: The main subunits of complex b-c1 are: cytochrome b, CC cytochrome c1 and the Rieske protein. {ECO:0000256|ARBA:ARBA00011649, CC ECO:0000256|RuleBase:RU004497}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. CC -!- MISCELLANEOUS: The Rieske protein is a high potential 2Fe-2S protein. CC {ECO:0000256|RuleBase:RU004494}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP004846; AGP77055.1; -; Genomic_DNA. DR AlphaFoldDB; S5ABE4; -. DR KEGG; amh:I633_03930; -. DR PATRIC; fig|1300253.3.peg.811; -. DR HOGENOM; CLU_055690_0_2_6; -. DR BioCyc; AMAC1300253:G12YX-632-MONOMER; -. DR Proteomes; UP000014909; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProt. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. 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 CDD; cd03470; Rieske_cytochrome_bc1; 1. DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1. DR Gene3D; 1.20.5.510; Single helix bin; 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; IPR019470; Ubiq_cytC_Rdtase_Fe-S_su_TAT. DR InterPro; IPR006317; Ubiquinol_cyt_c_Rdtase_Fe-S-su. DR NCBIfam; TIGR01416; Rieske_proteo; 1. DR PANTHER; PTHR10134; CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL; 1. DR PANTHER; PTHR10134:SF20; CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL-RELATED; 1. DR Pfam; PF00355; Rieske; 1. DR Pfam; PF10399; UCR_Fe-S_N; 1. DR PRINTS; PR00162; RIESKE. DR SUPFAM; SSF50022; ISP domain; 1. DR PROSITE; PS51296; RIESKE; 1. DR PROSITE; PS51318; TAT; 1. PE 4: Predicted; KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Electron transport {ECO:0000256|RuleBase:RU004494}; KW Iron {ECO:0000256|ARBA:ARBA00023004}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU004494}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU004494}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|RuleBase:RU004494}; Transport {ECO:0000256|RuleBase:RU004494}. FT TRANSMEM 26..48 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004494" FT DOMAIN 97..202 FT /note="Rieske" FT /evidence="ECO:0000259|PROSITE:PS51296" FT REGION 1..23 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 210 AA; 22872 MW; 4DDBCF3AEB1BB61B CRC64; MSNVSVDATE SAHNENQPEN NTRRRFLTVA TSVVGGVGVV GAAVPFIASW NPSAKAKAAG ADVEVDISGI EPGQLVRVMW RSKPVWIVRR TPEILEELGT HEDKLKDPNS EAEQQPTFAQ NRFRSMKEEY LILVGICTHL GCSPQHLKDG AFEEVVEGVP DGFFCPCHGS KFDMAGRVFQ NVPAPLNLVV PPYQFVDDNT VIIGSEAEVA //