ID   CYC2_RHOAD              Reviewed;         126 AA.
AC   P86320;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 27.
DE   RecName: Full=Cytochrome c2 {ECO:0000250|UniProtKB:P0C0X8};
OS   Rhodovulum adriaticum (Rhodopseudomonas adriatica).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodovulum.
OX   NCBI_TaxID=35804;
RN   [1]
RP   PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RX   PubMed=20697695; DOI=10.1007/s00203-010-0608-2;
RA   Meyer T., Van Driessche G., Ambler R., Kyndt J., Devreese B.,
RA   Van Beeumen J., Cusanovich M.;
RT   "Evidence from the structure and function of cytochromes c(2) that
RT   nonsulfur purple bacterial photosynthesis followed the evolution of oxygen
RT   respiration.";
RL   Arch. Microbiol. 192:855-865(2010).
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. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:20697695}.
CC   -!- PTM: Binds 1 heme c group covalently per subunit.
CC       {ECO:0000250|UniProtKB:P0C0X8}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000255}.
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DR   AlphaFoldDB; P86320; -.
DR   SMR; P86320; -.
DR   GO; GO:0042597; C:periplasmic space; IDA:UniProtKB.
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   Direct protein sequencing; Electron transport; Heme; Iron; Metal-binding;
KW   Periplasm; Photosynthesis; Transport.
FT   CHAIN           1..126
FT                   /note="Cytochrome c2"
FT                   /id="PRO_0000108353"
FT   BINDING         17
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250|UniProtKB:P0C0X8,
FT                   ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         20
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250|UniProtKB:P0C0X8,
FT                   ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         21
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:0000250|UniProtKB:P0C0X8,
FT                   ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         101
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:0000250|UniProtKB:P0C0X8,
FT                   ECO:0000255|PROSITE-ProRule:PRU00433"
SQ   SEQUENCE   126 AA;  13782 MW;  3410B2B347834292 CRC64;
     VDVSGDAAAG EKAFRQCITC HVVVDDSGET LAGRNAKVGP NLYKVPGRHA GQIEGFRYSD
     SMSQAGQNGL VWVEEEFVKY VQDPTGYLRE YLGDSKARGA MTHKVRKEDE AVDIYAYLAS
     LGVHEE