ID   CYC22_RHOPA             Reviewed;         139 AA.
AC   P00091;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   16-FEB-2004, sequence version 2.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=Cytochrome c2;
DE   Flags: Precursor;
GN   Name=cycA; OrderedLocusNames=RPA1535;
OS   Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=258594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-98 / CGA009;
RX   PubMed=14704707; DOI=10.1038/nbt923;
RA   Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA   Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA   Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA   Harrison F.H., Gibson J., Harwood C.S.;
RT   "Complete genome sequence of the metabolically versatile photosynthetic
RT   bacterium Rhodopseudomonas palustris.";
RL   Nat. Biotechnol. 22:55-61(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 26-139.
RC   STRAIN=ATCC 17007 / ATH 2.1.37 / NCIB 11774;
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).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BX572597; CAE26977.1; -; Genomic_DNA.
DR   PIR; A00083; CCRF7P.
DR   RefSeq; WP_011157096.1; NC_005296.1.
DR   PDB; 1FJ0; X-ray; 1.70 A; A/B/C/D=26-139.
DR   PDB; 1HH7; X-ray; 1.40 A; A=27-139.
DR   PDB; 1I8O; X-ray; 1.15 A; A=26-139.
DR   PDB; 1I8P; X-ray; 1.95 A; A/B/C/D=26-139.
DR   PDBsum; 1FJ0; -.
DR   PDBsum; 1HH7; -.
DR   PDBsum; 1I8O; -.
DR   PDBsum; 1I8P; -.
DR   AlphaFoldDB; P00091; -.
DR   SMR; P00091; -.
DR   STRING; 258594.RPA1535; -.
DR   DrugBank; DB03317; Ferroheme C.
DR   DrugBank; DB03088; Pidolic acid.
DR   PRIDE; P00091; -.
DR   EnsemblBacteria; CAE26977; CAE26977; RPA1535.
DR   GeneID; 66892566; -.
DR   KEGG; rpa:RPA1535; -.
DR   eggNOG; COG3474; Bacteria.
DR   HOGENOM; CLU_060944_2_0_5; -.
DR   OMA; YSDAMKN; -.
DR   PhylomeDB; P00091; -.
DR   BioCyc; RPAL258594:TX73_RS07830-MON; -.
DR   EvolutionaryTrace; P00091; -.
DR   Proteomes; UP000001426; Chromosome.
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;
KW   Reference proteome; Signal; Transport.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000269|PubMed:221822"
FT   CHAIN           26..139
FT                   /note="Cytochrome c2"
FT                   /id="PRO_0000006501"
FT   BINDING         38
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         41
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         42
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         118
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         26
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250|UniProtKB:P00090"
FT   HELIX           28..38
FT                   /evidence="ECO:0007829|PDB:1I8O"
FT   TURN            39..41
FT                   /evidence="ECO:0007829|PDB:1I8O"
FT   STRAND          44..46
FT                   /evidence="ECO:0007829|PDB:1I8O"
FT   STRAND          48..50
FT                   /evidence="ECO:0007829|PDB:1I8O"
FT   HELIX           71..78
FT                   /evidence="ECO:0007829|PDB:1I8O"
FT   HELIX           85..93
FT                   /evidence="ECO:0007829|PDB:1I8O"
FT   HELIX           95..105
FT                   /evidence="ECO:0007829|PDB:1I8O"
FT   HELIX           109..111
FT                   /evidence="ECO:0007829|PDB:1I8O"
FT   HELIX           125..136
FT                   /evidence="ECO:0007829|PDB:1I8O"
SQ   SEQUENCE   139 AA;  14633 MW;  4DCF92466EE609A1 CRC64;
     MVKKLLTILS IAATAGSLSI GTASAQDAKA GEAVFKQCMT CHRADKNMVG PALGGVVGRK
     AGTAAGFTYS PLNHNSGEAG LVWTADNIIN YLNDPNAFLK KFLTDKGKAD QAVGVTKMTF
     KLANEQQRKD VVAYLATLK