ID Q31RP8_SYNE7 Unreviewed; 112 AA.
AC Q31RP8;
DT 06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 06-DEC-2005, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=Cytochrome c6 {ECO:0000256|HAMAP-Rule:MF_00594};
DE AltName: Full=Cytochrome c-553 {ECO:0000256|HAMAP-Rule:MF_00594};
DE AltName: Full=Cytochrome c553 {ECO:0000256|HAMAP-Rule:MF_00594};
DE AltName: Full=Soluble cytochrome f {ECO:0000256|HAMAP-Rule:MF_00594};
GN Name=petJ {ECO:0000256|HAMAP-Rule:MF_00594};
GN OrderedLocusNames=Synpcc7942_0239 {ECO:0000313|EMBL:ABB56271.1};
OS Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805)
OS (Anacystis nidulans R2).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1140 {ECO:0000313|EMBL:ABB56271.1, ECO:0000313|Proteomes:UP000889800};
RN [1] {ECO:0000313|Proteomes:UP000889800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33912 / PCC 7942 / FACHB-805
RC {ECO:0000313|Proteomes:UP000889800};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Functions as an electron carrier between membrane-bound
CC cytochrome b6-f and photosystem I in oxygenic photosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_00594}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00594}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid lumen
CC {ECO:0000256|ARBA:ARBA00004518, ECO:0000256|HAMAP-Rule:MF_00594}.
CC -!- PTM: Binds 1 heme c group per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_00594}.
CC -!- SIMILARITY: Belongs to the cytochrome c family. PetJ subfamily.
CC {ECO:0000256|ARBA:ARBA00009650, ECO:0000256|HAMAP-Rule:MF_00594}.
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; CP000100; ABB56271.1; -; Genomic_DNA.
DR AlphaFoldDB; Q31RP8; -.
DR STRING; 1140.Synpcc7942_0239; -.
DR PaxDb; 1140-Synpcc7942_0239; -.
DR KEGG; syf:Synpcc7942_0239; -.
DR eggNOG; COG2010; Bacteria.
DR HOGENOM; CLU_101159_1_0_3; -.
DR OrthoDB; 5570429at2; -.
DR BioCyc; SYNEL:SYNPCC7942_0239-MONOMER; -.
DR Proteomes; UP000889800; Chromosome.
DR GO; GO:0031979; C:plasma membrane-derived thylakoid lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR HAMAP; MF_00594; Cytc_PetJ; 1.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR023655; Cyt_C6.
DR InterPro; IPR008168; Cyt_C_IC.
DR PANTHER; PTHR34688:SF4; CYTOCHROME C-553; 1.
DR PANTHER; PTHR34688; CYTOCHROME C6, CHLOROPLASTIC; 1.
DR Pfam; PF13442; Cytochrome_CBB3; 1.
DR PRINTS; PR00605; CYTCHROMECIC.
DR SUPFAM; SSF46626; Cytochrome c; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|HAMAP-Rule:MF_00594};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|HAMAP-Rule:MF_00594};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00594};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00594}; Photosynthesis {ECO:0000256|HAMAP-Rule:MF_00594};
KW Reference proteome {ECO:0000313|Proteomes:UP000889800};
KW Signal {ECO:0000256|HAMAP-Rule:MF_00594};
KW Thylakoid {ECO:0000256|ARBA:ARBA00023078, ECO:0000256|HAMAP-Rule:MF_00594};
KW Transport {ECO:0000256|HAMAP-Rule:MF_00594}.
FT DOMAIN 25..105
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT BINDING 38
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00594"
FT BINDING 41
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00594"
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 /evidence="ECO:0000256|HAMAP-Rule:MF_00594"
FT BINDING 82
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:0000256|HAMAP-Rule:MF_00594"
SQ SEQUENCE 112 AA; 12204 MW; A18E196CFD6F1A71 CRC64;
MGRWLVLGLL VIGLSVVNPA RAIAADLQVG ARLFQSNCTT CHLNGGNVIN GQKTLRQEAL
RRYGMDSVAA IQKQVTYGKN AMPAFGQRLS PEQIEAVATY VFDRAERGWT AL
//