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Database: UniProt
Entry: S6BQQ6_9GAMM
LinkDB: S6BQQ6_9GAMM
Original site: S6BQQ6_9GAMM 
ID   S6BQQ6_9GAMM            Unreviewed;       204 AA.
AC   S6BQQ6;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Cytochrome c, class I {ECO:0000313|EMBL:BAN68309.1};
GN   ORFNames=EBS_0331 {ECO:0000313|EMBL:BAN68309.1};
OS   endosymbiont of unidentified scaly snail isolate Monju.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria.
OX   NCBI_TaxID=1248727 {ECO:0000313|EMBL:BAN68309.1, ECO:0000313|Proteomes:UP000015562};
RN   [1] {ECO:0000313|EMBL:BAN68309.1, ECO:0000313|Proteomes:UP000015562}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Monju {ECO:0000313|EMBL:BAN68309.1};
RX   PubMed=23924784; DOI=10.1038/ismej.2013.131;
RA   Nakagawa S., Shimamura S., Takaki Y., Suzuki Y., Murakami S., Watanabe T.,
RA   Fujiyoshi S., Mino S., Sawabe T., Maeda T., Makita H., Nemoto S.,
RA   Nishimura S., Watanabe H., Watsuji T., Takai K.;
RT   "Allying with armored snails: the complete genome of gammaproteobacterial
RT   endosymbiont.";
RL   ISME J. 8:40-51(2014).
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC   -!- PTM: Binds 2 heme c groups covalently per subunit.
CC       {ECO:0000256|PIRSR:PIRSR000005-1}.
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DR   EMBL; AP012978; BAN68309.1; -; Genomic_DNA.
DR   RefSeq; WP_043107025.1; NZ_AP012978.1.
DR   AlphaFoldDB; S6BQQ6; -.
DR   STRING; 1248727.EBS_0331; -.
DR   KEGG; enm:EBS_0331; -.
DR   HOGENOM; CLU_076280_3_2_6; -.
DR   Proteomes; UP000015562; Chromosome.
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:0005506; F:iron ion binding; IEA:InterPro.
DR   Gene3D; 1.10.760.10; Cytochrome c-like domain; 2.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR024167; Cytochrome_c4-like.
DR   PANTHER; PTHR33751; CBB3-TYPE CYTOCHROME C OXIDASE SUBUNIT FIXP; 1.
DR   PANTHER; PTHR33751:SF9; CYTOCHROME C4; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   Pfam; PF13442; Cytochrome_CBB3; 1.
DR   PIRSF; PIRSF000005; Cytochrome_c4; 1.
DR   SUPFAM; SSF46626; Cytochrome c; 2.
DR   PROSITE; PS51007; CYTC; 2.
PE   4: Predicted;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000005-1};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000005-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000005-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015562};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..204
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004536515"
FT   DOMAIN          20..112
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   DOMAIN          125..204
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   BINDING         36
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000005-1"
FT   BINDING         39
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000005-1"
FT   BINDING         40
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000005-2"
FT   BINDING         89
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000005-2"
FT   BINDING         138
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000005-1"
FT   BINDING         141
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000005-1"
FT   BINDING         142
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000005-2"
FT   BINDING         182
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000005-2"
SQ   SEQUENCE   204 AA;  22774 MW;  BE4F7C129952AF10 CRC64;
     MLKTRTLAIA LLGAGLAFAI MPAIGTADVN SLAEKCGECH GKDGNSSDPK VPNIAGYSAK
     YIEDALEDYR DGERPGLKFK KEDGTETDMV EIAKKLSEDN IKAIAEYYSG QTFKSHAGEQ
     ETDPRLVARG EKIFKRKCKK CHTDFGTDPE DDAGILGGQW MEYLRHQFEM FASGEREMPK
     KMKKKFRKLK KEDYEAIIHA LGSK
//
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