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Database: UniProt
Entry: S6HP09_9GAMM
LinkDB: S6HP09_9GAMM
Original site: S6HP09_9GAMM 
ID   S6HP09_9GAMM            Unreviewed;       201 AA.
AC   S6HP09;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=Cytochrome c4 {ECO:0000313|EMBL:EPJ52849.1};
GN   ORFNames=OFPI_12580 {ECO:0000313|EMBL:EPJ52849.1};
OS   Osedax symbiont Rs2.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae.
OX   NCBI_TaxID=1330035 {ECO:0000313|EMBL:EPJ52849.1, ECO:0000313|Proteomes:UP000014830};
RN   [1] {ECO:0000313|EMBL:EPJ52849.1, ECO:0000313|Proteomes:UP000014830}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rs2 {ECO:0000313|Proteomes:UP000014830};
RA   Yi H., Goffredi S.;
RT   "Comparative genomics of two novel heterotrophic symbionts of deep-sea
RT   Osedax worms: functional variation and environmental selection.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC   -!- PTM: Binds 2 heme c groups covalently per subunit.
CC       {ECO:0000256|PIRSR:PIRSR000005-1}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EPJ52849.1}.
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DR   EMBL; ASZI01000087; EPJ52849.1; -; Genomic_DNA.
DR   AlphaFoldDB; S6HP09; -.
DR   PATRIC; fig|1330035.3.peg.1209; -.
DR   Proteomes; UP000014830; Unassembled WGS sequence.
DR   GO; GO:0042597; C:periplasmic space; IEA:InterPro.
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; IPR008168; Cyt_C_IC.
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   PIRSF; PIRSF000005; Cytochrome_c4; 1.
DR   PRINTS; PR00605; CYTCHROMECIC.
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:UP000014830};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..201
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004539218"
FT   DOMAIN          23..101
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   DOMAIN          110..201
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   BINDING         35
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         38
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                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000005-2"
FT   BINDING         78
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         131
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         134
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         135
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         178
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   201 AA;  21057 MW;  C969066B185C78E7 CRC64;
     MMNKILIGLV LSLSASTYVY AAGDAAAGKE KSVACGACHA ADGNSEIGNF PKLAGQNAKY
     LIKQMVDIQS GVRSVPEMAG QLDAKNEQDL EDLAAYFSSK KILGGKTAAD QLELGQSIYR
     SGISSKQVAA CTACHGAKGQ GLSTAGFPAL GGQHAAYTQK QLQGFRTSVR SNDPNNMMRD
     IAARLSDAEI KAVSSYIQGL Y
//
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