UCRI_CHLTE
ID UCRI_CHLTE Reviewed; 181 AA.
AC Q9F722;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Cytochrome b6-f complex iron-sulfur subunit;
DE EC=7.1.1.6;
DE AltName: Full=Plastohydroquinone:plastocyanin oxidoreductase iron-sulfur protein;
DE AltName: Full=Rieske iron-sulfur protein;
DE Short=ISP;
DE Short=RISP;
GN Name=petC; OrderedLocusNames=CT0302;
OS Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
OS (Chlorobium tepidum).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX NCBI_TaxID=194439;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS;
RX PubMed=10976061; DOI=10.1126/science.289.5485.1724;
RA Xiong J., Fischer W.M., Inoue K., Nakahara M., Bauer C.E.;
RT "Molecular evidence for the early evolution of photosynthesis.";
RL Science 289:1724-1730(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS;
RX PubMed=12093901; DOI=10.1073/pnas.132181499;
RA Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J.,
RA DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D.,
RA Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M.,
RA Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V.,
RA Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M.,
RA White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A.,
RA Fraser C.M.;
RT "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic,
RT anaerobic, green-sulfur bacterium.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
CC -!- FUNCTION: Component of the green S-bacteria bc-complex which consists
CC of the Rieske protein and cytochrome b subunit and which appears to
CC lack a cytochrome c1-equivalent. This complex has a comparatively low
CC redox potential.
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;
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 -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
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; AF287480; AAG12194.1; -; Genomic_DNA.
DR EMBL; AE006470; AAM71548.1; -; Genomic_DNA.
DR RefSeq; NP_661206.1; NC_002932.3.
DR RefSeq; WP_010931994.1; NC_002932.3.
DR AlphaFoldDB; Q9F722; -.
DR SMR; Q9F722; -.
DR STRING; 194439.CT0302; -.
DR EnsemblBacteria; AAM71548; AAM71548; CT0302.
DR KEGG; cte:CT0302; -.
DR PATRIC; fig|194439.7.peg.292; -.
DR eggNOG; COG0723; Bacteria.
DR HOGENOM; CLU_055690_1_1_10; -.
DR OMA; IFCPCHG; -.
DR OrthoDB; 1632945at2; -.
DR Proteomes; UP000001007; 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:0009496; F:plastoquinol--plastocyanin 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 PANTHER; PTHR10134; PTHR10134; 1.
DR Pfam; PF00355; Rieske; 1.
DR PRINTS; PR00162; RIESKE.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 3: Inferred from homology;
KW 2Fe-2S; Cell inner membrane; Cell membrane; Disulfide bond;
KW Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..181
FT /note="Cytochrome b6-f complex iron-sulfur subunit"
FT /id="PRO_0000127773"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 85..178
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 124
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 126
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 142
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 145
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT DISULFID 129..144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT CONFLICT 68
FT /note="V -> F (in Ref. 1; AAG12194)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="T -> R (in Ref. 1; AAG12194)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 181 AA; 18864 MW; 487FB49275EC289B CRC64;
MAQTGNFKSP ARMSSLGQGA APASAGAVTG GKPREEGLKG VDFERRGFLQ KIVGGVGAVV
AVSTLYPVVR YIVPPAKKIK IVNELAVGPA SDVPNGTGKI YQFNDDKVIV VNHGGSLTAV
SAICTHLGCL VHWDEAADMI ACPCHGAKYT QDGKIISGPQ PLPLKQYKVK IEDGKIVVSI
A
