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Database: UniProt
Entry: Q31RP8_SYNE7
LinkDB: Q31RP8_SYNE7
Original site: Q31RP8_SYNE7 
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}.
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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
//
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