CYC2_RHOCB
ID CYC2_RHOCB Reviewed; 137 AA.
AC P00094; D5ASA6;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Cytochrome c2;
DE Flags: Precursor;
GN Name=cycA; OrderedLocusNames=RCAP_rcc01240;
OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=272942;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=16593675; DOI=10.1073/pnas.83.7.2012;
RA Daldal F., Cheng S., Applebaum J., Davidson E., Prince R.C.;
RT "Cytochrome c2 is not essential for photosynthetic growth of
RT Rhodopseudomonas capsulata.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:2012-2016(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=20418398; DOI=10.1128/jb.00366-10;
RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA Haselkorn R.;
RT "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT Rhodobacter capsulatus SB 1003.";
RL J. Bacteriol. 192:3545-3546(2010).
RN [3]
RP PROTEIN SEQUENCE OF 22-137.
RC STRAIN=ATCC 11166 / 2.3.1, and ATCC 23782 / St Louis;
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 [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=1651396; DOI=10.1016/0022-2836(91)90109-j;
RA Benning M.M., Wesenberg G., Caffrey M.S., Bartsch R.G., Meyer T.E.,
RA Cusanovich M.A., Rayment I., Holden H.M.;
RT "Molecular structure of cytochrome c2 isolated from Rhodobacter capsulatus
RT determined at 2.5-A resolution.";
RL J. Mol. Biol. 220:673-685(1991).
RN [5]
RP STRUCTURE BY NMR.
RX PubMed=2159796; DOI=10.1021/bi00461a011;
RA Gooley P.R., Caffrey M.S., Cusanovich M.A., McKenzie N.E.;
RT "Assignment of the 1H and 15N NMR spectra of Rhodobacter capsulatus
RT ferrocytochrome c2.";
RL Biochemistry 29:2278-2290(1990).
RN [6]
RP STRUCTURE BY NMR.
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=9698552; DOI=10.1006/jmbi.1998.1950;
RA Cordier F., Caffrey M., Brutscher B., Cusanovich M.A., Marion D.,
RA Blackledge M.;
RT "Solution structure, rotational diffusion anisotropy and local backbone
RT dynamics of Rhodobacter capsulatus cytochrome c2.";
RL J. Mol. Biol. 281:341-361(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 -!- 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; M12776; AAA26102.1; -; Genomic_DNA.
DR EMBL; CP001312; ADE84997.1; -; Genomic_DNA.
DR PIR; A25452; CCRF2C.
DR PDB; 1C2N; NMR; -; A=1-137.
DR PDB; 1C2R; X-ray; 2.50 A; A/B=22-137.
DR PDB; 1VYD; X-ray; 2.30 A; A/B=22-137.
DR PDBsum; 1C2N; -.
DR PDBsum; 1C2R; -.
DR PDBsum; 1VYD; -.
DR AlphaFoldDB; P00094; -.
DR BMRB; P00094; -.
DR SMR; P00094; -.
DR IntAct; P00094; 1.
DR STRING; 272942.RCAP_rcc01240; -.
DR EnsemblBacteria; ADE84997; ADE84997; RCAP_rcc01240.
DR KEGG; rcp:RCAP_rcc01240; -.
DR eggNOG; COG3474; Bacteria.
DR HOGENOM; CLU_060944_1_0_5; -.
DR OMA; AQCHTIN; -.
DR EvolutionaryTrace; P00094; -.
DR Proteomes; UP000002361; 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; -; 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 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; Reference proteome; Signal; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:221822"
FT CHAIN 22..137
FT /note="Cytochrome c2"
FT /evidence="ECO:0000269|PubMed:221822"
FT /id="PRO_0000006497"
FT BINDING 34
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 /note="covalent"
FT BINDING 38
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 117
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 VARIANT 108
FT /note="L -> T (in strain: 2.3.1)"
FT VARIANT 115
FT /note="T -> S (in strain: 2.3.1)"
FT HELIX 24..30
FT /evidence="ECO:0007829|PDB:1VYD"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:1VYD"
FT TURN 34..37
FT /evidence="ECO:0007829|PDB:1VYD"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:1VYD"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:1VYD"
FT HELIX 76..83
FT /evidence="ECO:0007829|PDB:1VYD"
FT HELIX 90..98
FT /evidence="ECO:0007829|PDB:1VYD"
FT HELIX 100..108
FT /evidence="ECO:0007829|PDB:1VYD"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:1C2N"
FT HELIX 125..134
FT /evidence="ECO:0007829|PDB:1VYD"
SQ SEQUENCE 137 AA; 14279 MW; 394E29348E4537CD CRC64;
MKISLTAATV AALVLAAPAF AGDAAKGEKE FNKCKTCHSI IAPDGTEIVK GAKTGPNLYG
VVGRTAGTYP EFKYKDSIVA LGASGFAWTE EDIATYVKDP GAFLKEKLDD KKAKTGMAFK
LAKGGEDVAA YLASVVK
