UCRI_PROMA
ID UCRI_PROMA Reviewed; 178 AA.
AC Q7VDC0;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 122.
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}; OrderedLocusNames=Pro_0460;
OS Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=167539;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARG / CCMP1375 / SS120;
RX PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT nearly minimal oxyphototrophic genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003).
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}.
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DR EMBL; AE017126; AAP99506.1; -; Genomic_DNA.
DR RefSeq; NP_874854.1; NC_005042.1.
DR RefSeq; WP_011124615.1; NC_005042.1.
DR AlphaFoldDB; Q7VDC0; -.
DR SMR; Q7VDC0; -.
DR STRING; 167539.Pro_0460; -.
DR EnsemblBacteria; AAP99506; AAP99506; Pro_0460.
DR GeneID; 54199828; -.
DR KEGG; pma:Pro_0460; -.
DR PATRIC; fig|167539.5.peg.471; -.
DR eggNOG; COG0723; Bacteria.
DR HOGENOM; CLU_055690_8_0_3; -.
DR OMA; KGDPTYI; -.
DR OrthoDB; 1632945at2; -.
DR Proteomes; UP000001420; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 Gene3D; 2.102.10.10; -; 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; PTHR10134; 1.
DR Pfam; PF00355; Rieske; 1.
DR PRINTS; PR00162; RIESKE.
DR SUPFAM; SSF50022; SSF50022; 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_0000127777"
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; 18784 MW; 9D8AE11686AAEDF2 CRC64;
MTQMSPSDVP SMGRRQFMNL LTFGTATGVA LGALYPVANF FMPLRAGGGT GGTTAKDELG
NAVTATGWLS NHPAGDRSLV QGLKGDPTYL IVDGDAAIGN FGINAICTHL GCVVPWNSGA
NKYICPCHGS QYDANGKVVR GPAPLSLALT HIDIDDDNVL VSQWTETDFR TGDKPWWA