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CY551_CHLP8
ID   CY551_CHLP8             Reviewed;         206 AA.
AC   B3QM18; P42426;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Photosynthetic reaction center cytochrome c-551 {ECO:0000303|PubMed:1383218};
DE            Short=Cytochrome c551 {ECO:0000303|PubMed:1383218};
GN   Name=pscC; Synonyms=cycA {ECO:0000303|PubMed:1383218};
GN   OrderedLocusNames=Cpar_0549;
OS   Chlorobaculum parvum (strain DSM 263 / NCIMB 8327) (Chlorobium vibrioforme
OS   subsp. thiosulfatophilum).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX   NCBI_TaxID=517417;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-33, FUNCTION, AND
RP   PTM.
RX   PubMed=1383218; DOI=10.1016/s0021-9258(19)36808-5;
RA   Okkels J.S., Kjaer B., Hansson O., Svendsen I., Moeller B.L.,
RA   Scheller H.V.;
RT   "A membrane-bound monoheme cytochrome c551 of a novel type is the immediate
RT   electron donor to P840 of the Chlorobium vibrioforme photosynthetic
RT   reaction center complex.";
RL   J. Biol. Chem. 267:21139-21145(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 263 / NCIMB 8327;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Zhao F., Li T., Liu Z., Overmann J.,
RA   Bryant D.A., Richardson P.;
RT   "Complete sequence of Chlorobaculum parvum NCIB 8327.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Monoheme cytochrome which is the immediate electron donor to
CC       P840 of the photosynthetic reaction center complex.
CC       {ECO:0000269|PubMed:1383218}.
CC   -!- SUBUNIT: Component of the photosynthetic reaction center. The reaction
CC       center interacts with the Fenna-Matthews-Olson (FMO, fmoA) complex.
CC       {ECO:0000250|UniProtKB:O07091}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:O07091}; Multi-pass membrane protein
CC       {ECO:0000305}.
CC   -!- PTM: Binds 1 heme group per subunit. {ECO:0000269|PubMed:1383218}.
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DR   EMBL; M95751; AAA23110.1; -; Genomic_DNA.
DR   EMBL; CP001099; ACF10971.1; -; Genomic_DNA.
DR   PIR; A45079; A45079.
DR   RefSeq; WP_012501804.1; NC_011027.1.
DR   AlphaFoldDB; B3QM18; -.
DR   SMR; B3QM18; -.
DR   EnsemblBacteria; ACF10971; ACF10971; Cpar_0549.
DR   KEGG; cpc:Cpar_0549; -.
DR   eggNOG; COG3245; Bacteria.
DR   HOGENOM; CLU_1293374_0_0_10; -.
DR   OMA; TKYKKTG; -.
DR   OrthoDB; 1450807at2; -.
DR   Proteomes; UP000008811; 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:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR019604; Cytochrome-c551.
DR   Pfam; PF10643; Cytochrome-c551; 1.
DR   PIRSF; PIRSF000009; Cytochrome_c551; 1.
DR   SUPFAM; SSF46626; SSF46626; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Direct protein sequencing;
KW   Electron transport; Heme; Iron; Membrane; Metal-binding; Photosynthesis;
KW   Reaction center; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..206
FT                   /note="Photosynthetic reaction center cytochrome c-551"
FT                   /id="PRO_0000351515"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        76..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         152
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250|UniProtKB:O07091"
FT   BINDING         155
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250|UniProtKB:O07091"
FT   BINDING         156
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:O07091"
FT   BINDING         182
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:O07091"
SQ   SEQUENCE   206 AA;  22858 MW;  563427E9BA74B82B CRC64;
     MDNKSNGKLI ALAIGGAVLM GTLFFLVSFL TGYSPAPNHS AILTPLRSFM GWFLLIFCAS
     LIIMGLGKMS GAISDKWFLS FPLSIFVIVM VMFFSLRFYW EKGRTTTVDG KYIRSVEQLN
     DFLNKPAATS DLPPVPADFD FAAAEKLTDA KCNKCHTLGS VADLFRTKYK KTGQVKLIVK
     RMQGFPGANI SDDEVIEIGT WLQEKF
 
 
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