ID   CYC2_FUSBL              Reviewed;         158 AA.
AC   P86319;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 29.
DE   RecName: Full=Cytochrome c2 {ECO:0000250|UniProtKB:P0C0X8};
OS   Fuscovulum blasticum (Rhodobacter blasticus) (Rhodopseudomonas blastica).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Fuscovulum.
OX   NCBI_TaxID=1075;
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; P86319; -.
DR   SMR; P86319; -.
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   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; Pyrrolidone carboxylic acid; Transport.
FT   CHAIN           1..158
FT                   /note="Cytochrome c2"
FT                   /id="PRO_0000379962"
FT   REGION          129..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         18
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                   /note="covalent"
FT                   /evidence="ECO:0000250|UniProtKB:P0C0X8,
FT                   ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         22
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         102
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   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250|UniProtKB:P0C0X8"
SQ   SEQUENCE   158 AA;  15904 MW;  FADB84B6E7A224BE CRC64;
     QDAPTGDAAA GAKVFNKCQT CHMVVAPDGT VLAGKAGKTG NPLYGLDGRA PASYPDFAYG
     DGIKELGAAG EVWNEADFLQ YVADPTKFLK TKTGDTKAKG KMTFKLPNEK EAHDVWAFLN
     SLAPAPAAAE AAPAADAAAP AAADAAAPAE PAAEGAAT