ID   CYC21_RHOCE             Reviewed;         120 AA.
AC   P81153;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Cytochrome c2 iso-1;
DE   AltName: Full=Cytochrome c552;
OS   Rhodospirillum centenum (Rhodocista centenaria).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=34018;
RN   [1]
RP   PROTEIN SEQUENCE, AND PYROGLUTAMATE FORMATION AT GLN-1.
RC   STRAIN=ATCC 43720 / DSM 9894 / IAM 14193 / JCM 21060 / NBRC 16667;
RX   PubMed=9659396; DOI=10.1016/s0167-4838(98)00030-2;
RA   Samyn B., Fitch J., Meyer T.E., Cusanovich M.A., van Beeumen J.J.;
RT   "Purification and primary structure analysis of two cytochrome c2 isozymes
RT   from the purple phototrophic bacterium Rhodospirillum centenum.";
RL   Biochim. Biophys. Acta 1384:345-355(1998).
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Redox potential:
CC         E(0) is +316 mV.;
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   AlphaFoldDB; P81153; -.
DR   SMR; P81153; -.
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   Direct protein sequencing; Electron transport; Heme; Iron; Metal-binding;
KW   Photosynthesis; Pyrrolidone carboxylic acid; Transport.
FT   CHAIN           1..120
FT                   /note="Cytochrome c2 iso-1"
FT                   /id="PRO_0000108341"
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         98
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:9659396"
SQ   SEQUENCE   120 AA;  12818 MW;  BBE05414A003E6BF CRC64;
     QDGDPVKGEA VFKKCMACHR IGPDAKNLVG PVLTGVVGRQ AGVAPGFSYS ALNHAAGEAG
     LHWTAENIMA YLPDPNAFLR KFVTDAGNPE AAKGSTKMVF KLPNEQERKD VVAYLKTFSN