ID   CYCY_RHOCB              Reviewed;         199 AA.
AC   Q05389; D5AMF5;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Cytochrome c-type cyt cy;
GN   Name=cycY; OrderedLocusNames=RCAP_rcc02501;
OS   Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=272942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MT1131;
RX   PubMed=8385603; DOI=10.1002/j.1460-2075.1993.tb05773.x;
RA   Jenney F.E. Jr., Daldal F.;
RT   "A novel membrane-associated c-type cytochrome, cyt cy, can mediate the
RT   photosynthetic growth of Rhodobacter capsulatus and Rhodobacter
RT   sphaeroides.";
RL   EMBO J. 12:1283-1292(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX   PubMed=20418398; DOI=10.1128/jb.00366-10;
RA   Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA   Haselkorn R.;
RT   "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT   Rhodobacter capsulatus SB 1003.";
RL   J. Bacteriol. 192:3545-3546(2010).
CC   -!- FUNCTION: Electron transfer pathways that operates during
CC       photosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein.
CC   -!- PTM: Binds 1 heme c group covalently per subunit. {ECO:0000305}.
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DR   EMBL; Z21797; CAA79860.1; -; Genomic_DNA.
DR   EMBL; CP001312; ADE86231.1; -; Genomic_DNA.
DR   PIR; S31938; S31938.
DR   PDB; 6XKW; EM; 5.20 A; Y=1-199.
DR   PDB; 6XKX; EM; 6.10 A; p=31-199.
DR   PDB; 6XKZ; EM; 7.20 A; p=31-199.
DR   PDBsum; 6XKW; -.
DR   PDBsum; 6XKX; -.
DR   PDBsum; 6XKZ; -.
DR   AlphaFoldDB; Q05389; -.
DR   SMR; Q05389; -.
DR   STRING; 272942.RCAP_rcc02501; -.
DR   EnsemblBacteria; ADE86231; ADE86231; RCAP_rcc02501.
DR   KEGG; rcp:RCAP_rcc02501; -.
DR   eggNOG; COG3474; Bacteria.
DR   HOGENOM; CLU_060944_4_1_5; -.
DR   OMA; VDFATIM; -.
DR   Proteomes; UP000002361; 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; IMP:CACAO.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Electron transport; Heme; Iron; Membrane;
KW   Metal-binding; Photosynthesis; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..199
FT                   /note="Cytochrome c-type cyt cy"
FT                   /id="PRO_0000108421"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          69..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         112
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         115
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         116
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         148
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
SQ   SEQUENCE   199 AA;  20659 MW;  7606E351A6D9FBC3 CRC64;
     MLVKTHITKI GVTLFAVALF YGFIYMLSNS LFATRPATAV AVGADGKALL PSVDEAAMPA
     KAPAAAAPAA ETAEAAAPAE PAAPPPPAYV EVDPATITGD AKAGEEKFNK TCKACHKIDG
     KNAVGPHLNG VIGRATATVE GFKYSTAMKN HVGNWTPERL DIYLVSPKAE VPGTKMSFVG
     LPEAADRANV IAYLNTLPR