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Database: UniProt
Entry: A0A0J5QET3_9RHOB
LinkDB: A0A0J5QET3_9RHOB
Original site: A0A0J5QET3_9RHOB 
ID   A0A0J5QET3_9RHOB        Unreviewed;       201 AA.
AC   A0A0J5QET3;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Cytochrome c553 {ECO:0000313|EMBL:KMK66310.1};
GN   ORFNames=IMCC21224_111160 {ECO:0000313|EMBL:KMK66310.1};
OS   Puniceibacterium sp. IMCC21224.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Puniceibacterium.
OX   NCBI_TaxID=1618204 {ECO:0000313|EMBL:KMK66310.1, ECO:0000313|Proteomes:UP000036046};
RN   [1] {ECO:0000313|EMBL:KMK66310.1, ECO:0000313|Proteomes:UP000036046}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC21224 {ECO:0000313|EMBL:KMK66310.1,
RC   ECO:0000313|Proteomes:UP000036046};
RA   Cho J.-C., Yang S.-J., Kang I.;
RT   "Complete genome sequence of IMCC21224 belonging to the
RT   Alphaproteobacteria.";
RL   Submitted (MAY-2015) 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:KMK66310.1}.
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DR   EMBL; LDPY01000001; KMK66310.1; -; Genomic_DNA.
DR   RefSeq; WP_047994519.1; NZ_LDPY01000001.1.
DR   AlphaFoldDB; A0A0J5QET3; -.
DR   STRING; 1618204.IMCC21224_111160; -.
DR   OrthoDB; 9773456at2; -.
DR   Proteomes; UP000036046; Unassembled WGS sequence.
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; 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:UP000036046}.
FT   DOMAIN          16..103
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   DOMAIN          116..198
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         80
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         130
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         133
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                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000005-2"
FT   BINDING         175
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;  21778 MW;  BB7D895A37F2A744 CRC64;
     MPGRSLWVAF ALSLATVDPG GADMLSDETP AYERCALCHG LFGDSPRDKF PRLAGQRPAY
     IASQIRAFLD GQRRNDGGQM VAVVTELGPD DIALVVDWFS SQAQPDPILS DDTTAEAMET
     GYIAYLSAGC EECHDERGSG AINIPYLASQ HPAYLAKQMR DMRDGRRFGV SIDVMRAQLS
     SLSDADLDAI AAYLAAQDRT E
//
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