ID   CYC2_CERSP              Reviewed;         124 AA.
AC   P0C0X8; P00095;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Cytochrome c2;
DE            Short=Cyt c2;
GN   Name=cycA;
OS   Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=1063;
RN   [1]
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
RX   PubMed=15299423; DOI=10.1107/s0907444994001319;
RA   Axelrod H.L., Feher G., Allen J.P., Chirino A.J., Day M.W., Hsu B.T.,
RA   Rees D.C.;
RT   "Crystallization and X-ray structure determination of cytochrome-c(2) from
RT   Rhodobacter-sphaeroides in 3 crystal forms.";
RL   Acta Crystallogr. D 50:596-602(1994).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX   PubMed=8611557; DOI=10.1021/bi9522054;
RA   Adir N., Axelrod H.L., Beroza P., Isaacson R.A., Rongey S.H., Okamura M.Y.,
RA   Feher G.;
RT   "Co-crystallization and characterization of the photosynthetic reaction
RT   center-cytochrome c2 complex from Rhodobacter sphaeroides.";
RL   Biochemistry 35:2535-2547(1996).
RN   [3]
RP   STRUCTURE BY NMR, PYROGLUTAMATE FORMATION AT GLN-1, AND MASS SPECTROMETRY.
RX   PubMed=8827449; DOI=10.1093/oxfordjournals.jbchem.a021359;
RA   Gans P., Simorre J.-P., Caffrey M., Marion D., Richaud P., Vermeglio A.;
RT   "Sequential 1H and 15N NMR resonance assignment and secondary structure of
RT   ferrocytochrome c2 from Rhodobacter sphaeroides.";
RL   J. Biochem. 119:1131-1142(1996).
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   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- PTM: Binds 1 heme c group covalently per subunit.
CC   -!- MASS SPECTROMETRY: Mass=14069; Mass_error=2.1; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:8827449};
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- CAUTION: The sequence shown here has been extracted from PDB entry
CC       1CXA. {ECO:0000305}.
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DR   PIR; A38896; CCRF2S.
DR   PDB; 1CXA; X-ray; 2.20 A; A=1-124.
DR   PDB; 1CXC; X-ray; 1.60 A; A=1-124.
DR   PDB; 1L9B; X-ray; 2.40 A; C=1-124.
DR   PDB; 1L9J; X-ray; 3.25 A; C/D=1-124.
DR   PDB; 2CXB; X-ray; 1.95 A; A/B=1-124.
DR   PDBsum; 1CXA; -.
DR   PDBsum; 1CXC; -.
DR   PDBsum; 1L9B; -.
DR   PDBsum; 1L9J; -.
DR   PDBsum; 2CXB; -.
DR   AlphaFoldDB; P0C0X8; -.
DR   SMR; P0C0X8; -.
DR   DrugBank; DB04147; Dodecyldimethylamine N-oxide.
DR   EvolutionaryTrace; P0C0X8; -.
DR   GO; GO:0042597; C:periplasmic space; 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; 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   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Electron transport; Heme; Iron; Metal-binding; Periplasm;
KW   Photosynthesis; Pyrrolidone carboxylic acid; Transport.
FT   CHAIN           1..124
FT                   /note="Cytochrome c2"
FT                   /id="PRO_0000108346"
FT   BINDING         15
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                   /note="covalent"
FT   BINDING         19
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         100
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   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:8827449"
FT   HELIX           5..11
FT                   /evidence="ECO:0007829|PDB:1CXC"
FT   HELIX           12..17
FT                   /evidence="ECO:0007829|PDB:1CXC"
FT   STRAND          20..22
FT                   /evidence="ECO:0007829|PDB:1L9B"
FT   STRAND          28..30
FT                   /evidence="ECO:0007829|PDB:1CXC"
FT   HELIX           59..66
FT                   /evidence="ECO:0007829|PDB:1CXC"
FT   HELIX           73..81
FT                   /evidence="ECO:0007829|PDB:1CXC"
FT   HELIX           83..91
FT                   /evidence="ECO:0007829|PDB:1CXC"
FT   HELIX           107..120
FT                   /evidence="ECO:0007829|PDB:1CXC"
SQ   SEQUENCE   124 AA;  13469 MW;  79560DEADA7A1758 CRC64;
     QEGDPEAGAK AFNQCQTCHV IVDDSGTTIA GRNAKTGPNL YGVVGRTAGT QADFKGYGEG
     MKEAGAKGLA WDEEHFVQYV QDPTKFLKEY TGDAKAKGKM TFKLKKEADA HNIWAYLQQV
     AVRP