ID   CYC2_BLAVI              Reviewed;         127 AA.
AC   P00083;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 2.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Cytochrome c2;
DE   Flags: Precursor;
GN   Name=cycA;
OS   Blastochloris viridis (Rhodopseudomonas viridis).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Blastochloridaceae; Blastochloris.
OX   NCBI_TaxID=1079;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 19567 / DSM 133 / F;
RX   PubMed=1697576; DOI=10.1128/jb.172.9.5071-5078.1990;
RA   Grisshammer R., Wiessner C., Michel H.;
RT   "Sequence analysis and transcriptional organization of the Rhodopseudomonas
RT   viridis cytochrome c2 gene.";
RL   J. Bacteriol. 172:5071-5078(1990).
RN   [2]
RP   PROTEIN SEQUENCE OF 21-127, AND PYROGLUTAMATE FORMATION AT GLN-21.
RX   PubMed=174109; DOI=10.1073/pnas.73.2.472;
RA   Ambler R.P., Meyer T.E., Kamen M.D.;
RT   "Primary structure determination of two cytochromes c2: close similarity to
RT   functionally unrelated mitochondrial cytochrome C.";
RL   Proc. Natl. Acad. Sci. U.S.A. 73:472-475(1976).
RN   [3]
RP   SEQUENCE REVISION TO 34.
RA   Ambler R.P.;
RL   Submitted (JUN-1977) to the PIR data bank.
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RX   PubMed=7674304; DOI=10.1006/jmbi.1995.0491;
RA   Sogabe S., Miki M.;
RT   "Refined crystal structure of ferrocytochrome c2 from Rhodopseudomonas
RT   viridis at 1.6-A resolution.";
RL   J. Mol. Biol. 252:235-247(1995).
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.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
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DR   EMBL; M59302; AAA26092.1; -; Genomic_DNA.
DR   PIR; A36720; CCRF2V.
DR   RefSeq; WP_055036459.1; NZ_LN907867.1.
DR   PDB; 1CO6; X-ray; 1.60 A; A=21-127.
DR   PDB; 1CRY; X-ray; 3.00 A; A=21-127.
DR   PDB; 1IO3; X-ray; 1.90 A; A=21-127.
DR   PDBsum; 1CO6; -.
DR   PDBsum; 1CRY; -.
DR   PDBsum; 1IO3; -.
DR   AlphaFoldDB; P00083; -.
DR   SMR; P00083; -.
DR   STRING; 1079.BVIR_718; -.
DR   OMA; YSDAMKN; -.
DR   OrthoDB; 1853490at2; -.
DR   EvolutionaryTrace; P00083; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProt.
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   3D-structure; Direct protein sequencing; Electron transport; Heme; Iron;
KW   Metal-binding; Photosynthesis; Pyrrolidone carboxylic acid; Signal;
KW   Transport.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:174109"
FT   CHAIN           21..127
FT                   /note="Cytochrome c2"
FT                   /evidence="ECO:0000269|PubMed:174109"
FT                   /id="PRO_0000006500"
FT   BINDING         33
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         36
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         37
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         99
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         21
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:174109"
FT   CONFLICT        66
FT                   /note="A -> S (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        104
FT                   /note="V -> I (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        117
FT                   /note="I -> L (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   HELIX           23..34
FT                   /evidence="ECO:0007829|PDB:1CO6"
FT   STRAND          62..64
FT                   /evidence="ECO:0007829|PDB:1CRY"
FT   HELIX           69..72
FT                   /evidence="ECO:0007829|PDB:1CO6"
FT   HELIX           80..88
FT                   /evidence="ECO:0007829|PDB:1CO6"
FT   HELIX           90..93
FT                   /evidence="ECO:0007829|PDB:1CO6"
FT   HELIX           107..118
FT                   /evidence="ECO:0007829|PDB:1CO6"
SQ   SEQUENCE   127 AA;  13665 MW;  398ABCFF6A7D0DF4 CRC64;
     MRKLVFGLFV LAASVAPAAA QDAASGEQVF KQCLVCHSIG PGAKNKVGPV LNGLFGRHSG
     TIEGFAYSDA NKNSGITWTE EVFREYIRDP KAKIPGTKMI FAGVKDEQKV SDLIAYIKQF
     NADGSKK