ID   CYC22_MAGML             Reviewed;          97 AA.
AC   P00088;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Cytochrome c2 iso-2;
OS   Magnetospirillum molischianum (Rhodospirillum molischianum).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Magnetospirillum.
OX   NCBI_TaxID=1083;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=ATCC 14031 / DSM 120 / KCTC 15609 / LMG 4354 / NCIMB 9957 / NTHC
RC   131;
RX   PubMed=221822; DOI=10.1038/278659a0;
RA   Ambler R.P., Daniel M., Hermoso J., Meyer T.E., Bartsch R.G., Kamen M.D.;
RT   "Cytochrome c2 sequence variation among the recognised species of purple
RT   nonsulphur photosynthetic bacteria.";
RL   Nature 278:659-660(1979).
RN   [2]
RP   PROTEIN SEQUENCE.
RA   Ambler R.P.;
RL   Submitted (JUN-1977) to the PIR data bank.
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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC   -!- CAUTION: Approximately 30% of the residue corresponding to Tyr-62 is
CC       present as Phe, suggesting there may be more than 1 gene for this
CC       protein in this organism. {ECO:0000305}.
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DR   PIR; A00080; CCQFM2.
DR   AlphaFoldDB; P00088; -.
DR   SMR; P00088; -.
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; Transport.
FT   CHAIN           1..97
FT                   /note="Cytochrome c2 iso-2"
FT                   /id="PRO_0000108352"
FT   BINDING         10
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         13
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         14
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:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         75
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:0000255|PROSITE-ProRule:PRU00433"
SQ   SEQUENCE   97 AA;  10222 MW;  5A1CBC489B0DBFB6 CRC64;
     ADAPAGFTLC KACHSVEAGK NGVGPSLAGV YGRKAGTISG FKFSDPHIKS GLTWDEPTLT
     KYLADPKTVI PGNKMVFAGL KNPDDVKAVI EYLKTLK