CYCR_THETI
ID CYCR_THETI Reviewed; 404 AA.
AC D2Z0P5; A8ASG7;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Photosynthetic reaction center cytochrome c subunit {ECO:0000255|PIRNR:PIRNR000017, ECO:0000303|PubMed:24670637, ECO:0000312|EMBL:BAF80147.2};
DE Flags: Precursor;
GN Name=pufC {ECO:0000312|EMBL:BAF80147.2, ECO:0000312|EMBL:BAI67784.1};
OS Thermochromatium tepidum (Chromatium tepidum).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thermochromatium.
OX NCBI_TaxID=1050 {ECO:0000312|EMBL:BAI67784.1};
RN [1] {ECO:0000312|EMBL:BAI67784.1, ECO:0007744|PDB:3WMM, ECO:0007744|PDB:4V8K}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS)
RP IN COMPLEX WITH HEME; PHOTOSYNTHETIC REACTION CENTER SUBUNITS PUFL; PUFM
RP AND PUHA; LIGHT-HARVESTING COMPLEX LH1 ALPHA AND BETA SUBUNITS, AND
RP SUBCELLULAR LOCATION.
RX PubMed=24670637; DOI=10.1038/nature13197;
RA Niwa S., Yu L.J., Takeda K., Hirano Y., Kawakami T., Wang-Otomo Z.Y.,
RA Miki K.;
RT "Structure of the LH1-RC complex from Thermochromatium tepidum at 3.0A.";
RL Nature 508:228-232(2014).
RN [2] {ECO:0000312|EMBL:BAF80147.2}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-311.
RA Fathir I., Ashikaga M., Tanaka K., Katano T., Nirasawa T., Kobayashi M.,
RA Wang Z., Nozawa T.;
RT "Biochemical and spectral characterization of the core light harvesting
RT complex 1 (LH1) from the thermophilic purple sulfur bacterium Chromatium
RT tepidum.";
RL Photosyn. Res. 58:193-202(1998).
CC -!- FUNCTION: The reaction center of purple bacteria contains a tightly
CC bound cytochrome molecule which re-reduces the photo oxidized primary
CC electron donor. {ECO:0000255|PIRNR:PIRNR000017}.
CC -!- SUBUNIT: Component of the photosynthetic reaction center composed of
CC protein subunits L (PufL), M (PufM), H (PuhA) and cytochrome C (PufC).
CC The reaction center interacts with light-harvesting antenna complex
CC LH1. {ECO:0000269|PubMed:24670637}.
CC -!- SUBCELLULAR LOCATION: Cellular chromatophore membrane
CC {ECO:0000269|PubMed:24670637}; Lipid-anchor
CC {ECO:0000305|PubMed:24670637}.
CC -!- PTM: Binds 4 heme groups per subunit. {ECO:0000255|PIRNR:PIRNR000017,
CC ECO:0000255|PIRSR:PIRSR000017-2, ECO:0000269|PubMed:24670637}.
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; AB543090; BAI67784.1; -; Genomic_DNA.
DR EMBL; D85518; BAF80147.2; -; Genomic_DNA.
DR PDB; 3WMM; X-ray; 3.01 A; C=1-404.
DR PDB; 4V8K; X-ray; 3.01 A; AC/BC=1-404.
DR PDB; 5B5M; X-ray; 3.30 A; C/o=1-333.
DR PDB; 5B5N; X-ray; 3.30 A; C/o=1-333.
DR PDB; 5Y5S; X-ray; 1.90 A; C=1-404.
DR PDB; 7C52; X-ray; 2.89 A; C=23-333.
DR PDBsum; 3WMM; -.
DR PDBsum; 4V8K; -.
DR PDBsum; 5B5M; -.
DR PDBsum; 5B5N; -.
DR PDBsum; 5Y5S; -.
DR PDBsum; 7C52; -.
DR AlphaFoldDB; D2Z0P5; -.
DR SMR; D2Z0P5; -.
DR DIP; DIP-60696N; -.
DR IntAct; D2Z0P5; 1.
DR TCDB; 3.E.2.1.2; the photosynthetic reaction center (prc) family.
DR GO; GO:0030077; C:plasma membrane light-harvesting complex; IEA:InterPro.
DR GO; GO:0042717; C:plasma membrane-derived chromatophore membrane; IDA:UniProtKB.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0015979; P:photosynthesis; ISS:UniProtKB.
DR GO; GO:0019684; P:photosynthesis, light reaction; IEA:InterPro.
DR CDD; cd09224; CytoC_RC; 1.
DR Gene3D; 1.10.468.10; -; 2.
DR InterPro; IPR023119; Multihaem_cyt_PRC_cyt_su-like.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR InterPro; IPR003158; Photosyn_RC_cyt_c-su.
DR Pfam; PF02276; CytoC_RC; 1.
DR PIRSF; PIRSF000017; RC_cytochrome; 1.
DR SUPFAM; SSF48695; SSF48695; 1.
DR PROSITE; PS51008; MULTIHEME_CYTC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Electron transport; Heme; Iron; Lipoprotein; Membrane;
KW Metal-binding; Palmitate; Photosynthesis; Reaction center; Signal;
KW Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..404
FT /note="Photosynthetic reaction center cytochrome c subunit"
FT /id="PRO_0000437124"
FT REGION 346..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 94
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PIRSR:PIRSR000017-2,
FT ECO:0000269|PubMed:24670637, ECO:0007744|PDB:3WMM"
FT BINDING 107
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000255|PIRSR:PIRSR000017-1,
FT ECO:0000269|PubMed:24670637, ECO:0007744|PDB:3WMM"
FT BINDING 110
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000255|PIRSR:PIRSR000017-1,
FT ECO:0000269|PubMed:24670637, ECO:0007744|PDB:3WMM"
FT BINDING 111
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PIRSR:PIRSR000017-2,
FT ECO:0000269|PubMed:24670637, ECO:0007744|PDB:3WMM"
FT BINDING 130
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PIRSR:PIRSR000017-2,
FT ECO:0000269|PubMed:24670637, ECO:0007744|PDB:3WMM"
FT BINDING 144
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PIRSR:PIRSR000017-2,
FT ECO:0000269|PubMed:24670637, ECO:0007744|PDB:3WMM"
FT BINDING 152
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000255|PIRSR:PIRSR000017-1,
FT ECO:0000269|PubMed:24670637, ECO:0007744|PDB:3WMM"
FT BINDING 155
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000255|PIRSR:PIRSR000017-1,
FT ECO:0000269|PubMed:24670637, ECO:0007744|PDB:3WMM"
FT BINDING 156
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PIRSR:PIRSR000017-2,
FT ECO:0000269|PubMed:24670637, ECO:0007744|PDB:3WMM"
FT BINDING 236
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PIRSR:PIRSR000017-2,
FT ECO:0000269|PubMed:24670637, ECO:0007744|PDB:3WMM"
FT BINDING 247
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000255|PIRSR:PIRSR000017-1,
FT ECO:0000269|PubMed:24670637, ECO:0007744|PDB:3WMM"
FT BINDING 250
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000255|PIRSR:PIRSR000017-1,
FT ECO:0000269|PubMed:24670637, ECO:0007744|PDB:3WMM"
FT BINDING 251
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PIRSR:PIRSR000017-2,
FT ECO:0000269|PubMed:24670637, ECO:0007744|PDB:3WMM"
FT BINDING 307
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000255|PIRSR:PIRSR000017-1,
FT ECO:0000269|PubMed:24670637, ECO:0007744|PDB:3WMM"
FT BINDING 310
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000255|PIRSR:PIRSR000017-1,
FT ECO:0000269|PubMed:24670637, ECO:0007744|PDB:3WMM"
FT BINDING 311
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PIRSR:PIRSR000017-2,
FT ECO:0000269|PubMed:24670637, ECO:0007744|PDB:3WMM"
FT LIPID 23
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 23
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CONFLICT 308
FT /note="M -> S (in Ref. 2; BAF80147)"
FT /evidence="ECO:0000305"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:5Y5S"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:5Y5S"
FT HELIX 46..55
FT /evidence="ECO:0007829|PDB:5Y5S"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:5Y5S"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:5Y5S"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:5Y5S"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:5Y5S"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:3WMM"
FT HELIX 87..101
FT /evidence="ECO:0007829|PDB:5Y5S"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:5Y5S"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:5Y5S"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:5Y5S"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:5Y5S"
FT HELIX 122..140
FT /evidence="ECO:0007829|PDB:5Y5S"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:5Y5S"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:5Y5S"
FT HELIX 152..156
FT /evidence="ECO:0007829|PDB:5Y5S"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:5Y5S"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:5Y5S"
FT STRAND 215..221
FT /evidence="ECO:0007829|PDB:5Y5S"
FT HELIX 226..243
FT /evidence="ECO:0007829|PDB:5Y5S"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:5Y5S"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:3WMM"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:5Y5S"
FT HELIX 264..282
FT /evidence="ECO:0007829|PDB:5Y5S"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:5Y5S"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:5Y5S"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:5Y5S"
FT HELIX 307..311
FT /evidence="ECO:0007829|PDB:5Y5S"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:5Y5S"
FT HELIX 317..320
FT /evidence="ECO:0007829|PDB:5Y5S"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:5Y5S"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:5Y5S"
SQ SEQUENCE 404 AA; 43140 MW; 8C60811DBFC1E27C CRC64;
MSPAQQLTLP AVIVVASVML LGCEGPPPGT EQIGYRGVGM ENYYNKRQRA LSIQANQPVE
SLPAADSTGP KASEVYQNVQ VLKDLSVGEF TRTMVAVTTW VSPKEGCNYC HVPGNWASDD
IYTKVVSRRM FELVRAANSD WKAHVAETGV TCYTCHRGNP VPKYAWVTDP GPKYPSGLKP
TGQNYGSKTV AYASLPFDPL TPFLDQANEI RITGNAALAG SNPASLKQAE WTFGLMMNIS
DSLGVGCTFC HNTRAFNDWT QSTPKRTTAW YAIRHVRDIN QNYIWPLNDV LPASRKGPYG
DPLRVSCMTC HQAVNKPLYG AQMAKDYPGL YKTAVTQEAL AGSAPASEAA PAAATEAAPE
APAQEVPAAE AVPAAAEPGA AEAAGSVEPA PVEEVAPAPA AQRL
