ID UCRI_PROM4 Reviewed; 178 AA. AC A9BE84; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 15-JAN-2008, sequence version 1. DT 27-MAR-2024, entry version 101. DE RecName: Full=Cytochrome b6-f complex iron-sulfur subunit {ECO:0000255|HAMAP-Rule:MF_01335}; DE EC=7.1.1.6 {ECO:0000255|HAMAP-Rule:MF_01335}; DE AltName: Full=Plastohydroquinone:plastocyanin oxidoreductase iron-sulfur protein {ECO:0000255|HAMAP-Rule:MF_01335}; DE Short=ISP {ECO:0000255|HAMAP-Rule:MF_01335}; DE Short=RISP {ECO:0000255|HAMAP-Rule:MF_01335}; DE AltName: Full=Rieske iron-sulfur protein {ECO:0000255|HAMAP-Rule:MF_01335}; GN Name=petC {ECO:0000255|HAMAP-Rule:MF_01335}; GN OrderedLocusNames=P9211_04631; OS Prochlorococcus marinus (strain MIT 9211). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; OC Prochlorococcaceae; Prochlorococcus. OX NCBI_TaxID=93059; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MIT 9211; RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231; RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., RA Richardson P., Chisholm S.W.; RT "Patterns and implications of gene gain and loss in the evolution of RT Prochlorococcus."; RL PLoS Genet. 3:2515-2528(2007). CC -!- FUNCTION: Component of the cytochrome b6-f complex, which mediates CC electron transfer between photosystem II (PSII) and photosystem I CC (PSI), cyclic electron flow around PSI, and state transitions. CC {ECO:0000255|HAMAP-Rule:MF_01335}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a plastoquinol + 2 H(+)(in) + 2 oxidized [plastocyanin] = a CC plastoquinone + 4 H(+)(out) + 2 reduced [plastocyanin]; CC Xref=Rhea:RHEA:22148, Rhea:RHEA-COMP:9561, Rhea:RHEA-COMP:9562, CC Rhea:RHEA-COMP:10039, Rhea:RHEA-COMP:10040, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17757, ChEBI:CHEBI:29036, ChEBI:CHEBI:49552, CC ChEBI:CHEBI:62192; EC=7.1.1.6; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01335}; CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01335}; CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01335}; CC -!- SUBUNIT: The 4 large subunits of the cytochrome b6-f complex are CC cytochrome b6, subunit IV (17 kDa polypeptide, PetD), cytochrome f and CC the Rieske protein, while the 4 small subunits are PetG, PetL, PetM and CC PetN. The complex functions as a dimer. {ECO:0000255|HAMAP- CC Rule:MF_01335}. CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP- CC Rule:MF_01335}; Single-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01335}. Note=The transmembrane helix obliquely spans the CC membrane in one monomer, and its extrinsic C-terminal domain is part of CC the other monomer. {ECO:0000255|HAMAP-Rule:MF_01335}. CC -!- MISCELLANEOUS: The Rieske iron-sulfur protein is a high potential 2Fe- CC 2S protein. CC -!- SIMILARITY: Belongs to the Rieske iron-sulfur protein family. CC {ECO:0000255|HAMAP-Rule:MF_01335}. 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; CP000878; ABX08394.1; -; Genomic_DNA. DR RefSeq; WP_012195017.1; NC_009976.1. DR AlphaFoldDB; A9BE84; -. DR SMR; A9BE84; -. DR STRING; 93059.P9211_04631; -. DR KEGG; pmj:P9211_04631; -. DR eggNOG; COG0723; Bacteria. DR HOGENOM; CLU_055690_8_0_3; -. DR OrthoDB; 9767869at2; -. DR Proteomes; UP000000788; Chromosome. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt. DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0045158; F:electron transporter, transferring electrons within cytochrome b6/f complex of photosystem II activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009496; F:plastoquinol--plastocyanin reductase activity; IEA:UniProtKB-UniRule. DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule. DR CDD; cd03471; Rieske_cytochrome_b6f; 1. DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1. DR Gene3D; 1.20.5.700; Single helix bin; 1. DR HAMAP; MF_01335; Cytb6_f_Rieske; 1. DR InterPro; IPR023960; Cyt_b6_f_Rieske. 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 PANTHER; PTHR10134; CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL; 1. DR PANTHER; PTHR10134:SF50; CYTOCHROME B6-F COMPLEX IRON-SULFUR SUBUNIT, CHLOROPLASTIC; 1. DR Pfam; PF00355; Rieske; 1. DR PRINTS; PR00162; RIESKE. DR SUPFAM; SSF50022; ISP domain; 1. DR PROSITE; PS51296; RIESKE; 1. DR PROSITE; PS51318; TAT; 1. PE 3: Inferred from homology; KW 2Fe-2S; Disulfide bond; Electron transport; Iron; Iron-sulfur; Membrane; KW Metal-binding; Reference proteome; Thylakoid; Translocase; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..178 FT /note="Cytochrome b6-f complex iron-sulfur subunit" FT /id="PRO_1000142569" FT TRANSMEM 20..42 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01335" FT DOMAIN 71..161 FT /note="Rieske" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01335" FT BINDING 107 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01335" FT BINDING 109 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01335" FT BINDING 125 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01335" FT BINDING 128 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01335" FT DISULFID 112..127 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01335" SQ SEQUENCE 178 AA; 18858 MW; 2552824A7D1DB4E4 CRC64; MTQMTPSDVP SMGRRQFMNL LTFGTATGVA LGALYPVANY FMPLRAGGGG GGTSAKDELG NPITASGWLS NHPAGDRSLV QGLKGDPTYL IVEGSEAIGN FGINAICTHL GCVVPWNSGA NKYICPCHGS QYDANGKVVR GPAPLSLALA HIDVEDDKVF VSQWAETDFR TGEKPWWT //