ID   CYC2_RHORU              Reviewed;         112 AA.
AC   P0C189; P00092;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Cytochrome c2;
GN   Name=cycA;
OS   Rhodospirillum rubrum.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=1085;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=4883098; DOI=10.1016/s0021-9258(18)97813-0;
RA   Dus K., Sletten K., Kamen M.D.;
RT   "Cytochrome c2 of Rhodospirillum rubrum. II. Complete amino acid sequence
RT   and phylogenetic relationships.";
RL   J. Biol. Chem. 243:5507-5518(1968).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS).
RX   PubMed=4350650; DOI=10.2210/pdb1c2c/pdb;
RA   Salemme F.R., Freer S.T., Xuong N.H., Alden R.A., Kraut J.;
RT   "The structure of oxidized cytochrome c2 of Rhodospirillum rubrum.";
RL   J. Biol. Chem. 248:3910-3921(1973).
RN   [3]
RP   CRYSTALLIZATION.
RX   PubMed=4200400; DOI=10.1016/0006-291x(73)90886-3;
RA   Salemme F.R., Freer S.T., Alden R.A., Kraut J.;
RT   "Atomic coordinates for ferricytochrome c2 of Rhodospirillum rubrum.";
RL   Biochem. Biophys. Res. Commun. 54:47-52(1973).
CC   -!- FUNCTION: Cytochrome c2 is found mainly in purple, non-sulfur,
CC       photosynthetic bacteria where it functions as the electron donor to the
CC       oxidized bacteriochlorophyll in the photophosphorylation pathway.
CC       However, it may also have a role in the respiratory chain and is found
CC       in some non-photosynthetic bacteria.
CC   -!- PTM: Binds 1 heme c group covalently per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
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DR   PIR; S08213; CCQF2R.
DR   PDB; 2C2C; X-ray; 2.00 A; A=1-112.
DR   PDB; 3C2C; X-ray; 1.68 A; A=1-112.
DR   PDBsum; 2C2C; -.
DR   PDBsum; 3C2C; -.
DR   AlphaFoldDB; P0C189; -.
DR   BMRB; P0C189; -.
DR   SMR; P0C189; -.
DR   EvolutionaryTrace; P0C189; -.
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; 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; Direct protein sequencing; Electron transport; Heme; Iron;
KW   Metal-binding; Photosynthesis; Transport.
FT   CHAIN           1..112
FT                   /note="Cytochrome c2"
FT                   /id="PRO_0000006498"
FT   BINDING         14
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         17
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         18
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   BINDING         91
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   HELIX           4..10
FT                   /evidence="ECO:0007829|PDB:3C2C"
FT   HELIX           11..14
FT                   /evidence="ECO:0007829|PDB:3C2C"
FT   TURN            15..17
FT                   /evidence="ECO:0007829|PDB:3C2C"
FT   STRAND          27..29
FT                   /evidence="ECO:0007829|PDB:3C2C"
FT   STRAND          38..41
FT                   /evidence="ECO:0007829|PDB:3C2C"
FT   HELIX           50..57
FT                   /evidence="ECO:0007829|PDB:3C2C"
FT   HELIX           64..72
FT                   /evidence="ECO:0007829|PDB:3C2C"
FT   HELIX           74..82
FT                   /evidence="ECO:0007829|PDB:3C2C"
FT   HELIX           98..108
FT                   /evidence="ECO:0007829|PDB:3C2C"
SQ   SEQUENCE   112 AA;  12242 MW;  2928DC2935ED35FD CRC64;
     EGDAAAGEKV SKKCLACHTF DQGGANKVGP NLFGVFENTA AHKDNYAYSE SYTEMKAKGL
     TWTEANLAAY VKNPKAFVLE KSGDPKAKSK MTFKLTKDDE IENVIAYLKT LK