CYCR_RUBGI
ID CYCR_RUBGI Reviewed; 366 AA.
AC P51758; I0HUL3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Photosynthetic reaction center cytochrome c subunit;
DE Flags: Precursor;
GN Name=pufC; OrderedLocusNames=RGE_33610;
OS Rubrivivax gelatinosus (strain NBRC 100245 / IL144).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Rubrivivax.
OX NCBI_TaxID=983917;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NBRC 100245 / IL144;
RX PubMed=8300574; DOI=10.1016/s0021-9258(17)41970-3;
RA Nagashima K.V.P., Matsuura K., Ohyama S., Shimada K.;
RT "Primary structure and transcription of genes encoding B870 and
RT photosynthetic reaction center apoproteins from Rubrivivax gelatinosus.";
RL J. Biol. Chem. 269:2477-2484(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100245 / IL144;
RX PubMed=22689232; DOI=10.1128/jb.00511-12;
RA Nagashima S., Kamimura A., Shimizu T., Nakamura-Isaki S., Aono E.,
RA Sakamoto K., Ichikawa N., Nakazawa H., Sekine M., Yamazaki S., Fujita N.,
RA Shimada K., Hanada S., Nagashima K.V.;
RT "Complete genome sequence of phototrophic betaproteobacterium Rubrivivax
RT gelatinosus IL144.";
RL J. Bacteriol. 194:3541-3542(2012).
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:0000250|UniProtKB:P07173}.
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:0000250|UniProtKB:D2Z0P5}.
CC -!- SUBCELLULAR LOCATION: Cellular chromatophore membrane
CC {ECO:0000250|UniProtKB:P07173}; Lipid-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00303}.
CC -!- PTM: Binds 4 heme groups per subunit. {ECO:0000250|UniProtKB:P07173}.
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DR EMBL; D16822; BAA04102.1; -; Genomic_DNA.
DR EMBL; AP012320; BAL96700.1; -; Genomic_DNA.
DR PIR; G49964; G49964.
DR RefSeq; WP_014429561.1; NC_017075.1.
DR AlphaFoldDB; P51758; -.
DR SMR; P51758; -.
DR STRING; 983917.RGE_33610; -.
DR EnsemblBacteria; BAL96700; BAL96700; RGE_33610.
DR KEGG; rge:RGE_33610; -.
DR PATRIC; fig|983917.3.peg.3288; -.
DR eggNOG; ENOG502Z7SF; Bacteria.
DR HOGENOM; CLU_050380_0_0_4; -.
DR OMA; CTYCHNT; -.
DR OrthoDB; 374575at2; -.
DR Proteomes; UP000007883; Chromosome.
DR GO; GO:0030077; C:plasma membrane light-harvesting complex; IEA:InterPro.
DR GO; GO:0042717; C:plasma membrane-derived chromatophore membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Electron transport; Heme; Iron; Lipoprotein; Membrane; Metal-binding;
KW Palmitate; Photosynthesis; Reaction center; Reference proteome; Repeat;
KW Signal; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 23..366
FT /note="Photosynthetic reaction center cytochrome c subunit"
FT /id="PRO_0000006550"
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:0000250|UniProtKB:P07173"
FT BINDING 107
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P07173"
FT BINDING 110
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P07173"
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:0000250|UniProtKB:P07173"
FT BINDING 129
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:0000250|UniProtKB:P07173"
FT BINDING 143
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:0000250|UniProtKB:P07173"
FT BINDING 151
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P07173"
FT BINDING 154
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P07173"
FT BINDING 155
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:0000250|UniProtKB:P07173"
FT BINDING 238
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:0000250|UniProtKB:P07173"
FT BINDING 249
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P07173"
FT BINDING 252
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P07173"
FT BINDING 253
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:0000250|UniProtKB:P07173"
FT BINDING 309
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P07173"
FT BINDING 312
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P07173"
FT BINDING 313
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:0000250|UniProtKB:P07173"
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 98
FT /note="T -> N (in Ref. 1; BAA04102)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="Q -> H (in Ref. 1; BAA04102)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 366 AA; 39174 MW; 655C941DCE182D9E CRC64;
MALAVRISTL TVAVTAAALL AGCERPPVDA VQRGYRGTGM QHIVNPRTLA EQIPTQQAPV
ATPVADNSGP RANQVFQNVK VLGHLSVAEF TRQMAAITEW VAPTEGCNYC HTENLADDSK
YQKVVSRRML EMTQKVNTQW TQHVAATGVT CYTCHRGNPV PKEIWFTAVP QNKRADFIGN
LDGQNQAAKV VGLTSLPYDP FTTFLKEETN VRVYGTTALP TGTSKADIKQ AEKTYGLMMH
FSGALGVNCT YCHNTNGFGS WDNAAPQRAT AWYGIRMARD LNNNFMEGLT KTFPAHRLGP
TGDVAKINCS TCHQGAYKPL YGAQMAKDYP GLKPAPAAAA ASAVEAAPVD AAASAAPVAT
VATAAK
