CYC2_CERS4
ID CYC2_CERS4 Reviewed; 145 AA.
AC Q3J164; P00095; Q93V25;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Cytochrome c2;
DE Short=Cyt c2;
DE Flags: Precursor;
GN Name=cycA; OrderedLocusNames=RHOS4_19020; ORFNames=RSP_0296;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3023293; DOI=10.1128/jb.168.2.962-972.1986;
RA Donohue T.J., McEwan A.G., Kaplan S.;
RT "Cloning, DNA sequence, and expression of the Rhodobacter sphaeroides
RT cytochrome c2 gene.";
RL J. Bacteriol. 168:962-972(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1648072; DOI=10.1128/jb.173.13.3949-3957.1991;
RA McGregor B.J., Donohue T.J.;
RT "Evidence for two promoters for the cytochrome c2 gene (cycA) of
RT Rhodobacter sphaeroides.";
RL J. Bacteriol. 173:3949-3957(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10648776; DOI=10.1093/nar/28.4.862;
RA Choudhary M., Kaplan S.;
RT "DNA sequence analysis of the photosynthesis region of Rhodobacter
RT sphaeroides 2.4.1.";
RL Nucleic Acids Res. 28:862-867(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 22-124.
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 [6]
RP PROTEIN SEQUENCE OF 22-145.
RA Ambler R.P., Meyer T.E.;
RL Submitted (JUL-1974) 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 -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- PTM: Binds 1 heme c group covalently per subunit. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
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DR EMBL; M14501; AAA26101.1; -; Genomic_DNA.
DR EMBL; M64777; AAA26099.1; -; Genomic_DNA.
DR EMBL; AF195122; AAF24264.1; -; Genomic_DNA.
DR EMBL; CP000143; ABA79470.1; -; Genomic_DNA.
DR PIR; A38896; CCRF2S.
DR RefSeq; WP_002720461.1; NZ_CP030271.1.
DR RefSeq; YP_353371.1; NC_007493.2.
DR AlphaFoldDB; Q3J164; -.
DR SMR; Q3J164; -.
DR STRING; 272943.RSP_0296; -.
DR EnsemblBacteria; ABA79470; ABA79470; RSP_0296.
DR GeneID; 57470615; -.
DR KEGG; rsp:RSP_0296; -.
DR PATRIC; fig|272943.9.peg.2241; -.
DR eggNOG; COG3474; Bacteria.
DR OMA; YSDAMKN; -.
DR PhylomeDB; Q3J164; -.
DR Proteomes; UP000002703; Chromosome 1.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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 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 Periplasm; Photosynthesis; Pyrrolidone carboxylic acid; Reference proteome;
KW Signal; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:221822, ECO:0000269|Ref.6"
FT CHAIN 22..145
FT /note="Cytochrome c2"
FT /id="PRO_0000006499"
FT BINDING 36
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 39
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 40
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 121
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 MOD_RES 22
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250"
FT CONFLICT 45
FT /note="D -> E (in Ref. 1; AAA26101)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 145 AA; 15568 MW; 5F53F99F745A7AE8 CRC64;
MKFQVKALAA IAAFAALPAL AQEGDPEAGA KAFNQCQTCH VIVDDSGTTI AGRNAKTGPN
LYGVVGRTAG TQADFKGYGE GMKEAGAKGL AWDEEHFVQY VQDPTKFLKE YTGDAKAKGK
MTFKLKKEAD AHNIWAYLQQ VAVRP
