ID   CYC2_RHOVT              Reviewed;         125 AA.
AC   P00082; E3I2Y7;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 2.
DT   27-MAR-2024, entry version 120.
DE   RecName: Full=Cytochrome c2;
DE   Flags: Precursor;
GN   OrderedLocusNames=Rvan_1007;
OS   Rhodomicrobium vannielii (strain ATCC 17100 / ATH 3.1.1 / DSM 162 / LMG
OS   4299).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Hyphomicrobiaceae; Rhodomicrobium.
OX   NCBI_TaxID=648757;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17100 / ATH 3.1.1 / DSM 162 / LMG 4299;
RX   PubMed=21705585; DOI=10.1128/jb.05453-11;
RG   US DOE Joint Genome Institute;
RA   Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT   "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL   J. Bacteriol. 193:4567-4568(2011).
RN   [2]
RP   PROTEIN SEQUENCE OF 22-125.
RC   STRAIN=ATCC 17100 / ATH 3.1.1 / DSM 162 / LMG 4299;
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).
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; CP002292; ADP70281.1; -; Genomic_DNA.
DR   PIR; A00074; CCRD2.
DR   RefSeq; WP_013418685.1; NC_014664.1.
DR   AlphaFoldDB; P00082; -.
DR   SMR; P00082; -.
DR   STRING; 648757.Rvan_1007; -.
DR   KEGG; rva:Rvan_1007; -.
DR   eggNOG; COG3474; Bacteria.
DR   HOGENOM; CLU_060944_2_1_5; -.
DR   OrthoDB; 9805828at2; -.
DR   Proteomes; UP000001399; Chromosome.
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; Cytochrome c-like domain; 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; CYTOCHROME C; 1.
DR   PANTHER; PTHR11961:SF12; CYTOCHROME C; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Electron transport; Heme; Iron; Metal-binding;
KW   Photosynthesis; Reference proteome; Signal; Transport.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:174109"
FT   CHAIN           22..125
FT                   /note="Cytochrome c2"
FT                   /id="PRO_0000108348"
FT   DOMAIN          23..123
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         35
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         38
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         39
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         101
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   CONFLICT        47
FT                   /note="P -> N (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        52
FT                   /note="V -> E (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        55..59
FT                   /note="NVVGS -> DVFGQ (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        63
FT                   /note="S -> A (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        118..125
FT                   /note="FLATQHGQ -> YLKQLSGK (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   125 AA;  13187 MW;  9E8949E84DE2423D CRC64;
     MKAIKIAMVG AALVWSASAY AAGDPVKGEQ VFKQCKICHQ VGPTAKPGVG PVQNNVVGSK
     AGSRPGFNYS DAMKNSGLTW DEATLDKYLE NPKAVVPGTK MVFVGLKNPQ DRADVIAFLA
     TQHGQ
//