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Database: UniProt
Entry: A0A2R8AFE6_9RHOB
LinkDB: A0A2R8AFE6_9RHOB
Original site: A0A2R8AFE6_9RHOB 
ID   A0A2R8AFE6_9RHOB        Unreviewed;       429 AA.
AC   A0A2R8AFE6;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Cytochrome c551 peroxidase {ECO:0000313|EMBL:SPF30906.1};
DE            EC=1.11.1.5 {ECO:0000313|EMBL:SPF30906.1};
GN   Name=ccp_2 {ECO:0000313|EMBL:SPF30906.1};
GN   ORFNames=POI8812_03251 {ECO:0000313|EMBL:SPF30906.1};
OS   Pontivivens insulae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Pontivivens.
OX   NCBI_TaxID=1639689 {ECO:0000313|EMBL:SPF30906.1, ECO:0000313|Proteomes:UP000244932};
RN   [1] {ECO:0000313|EMBL:SPF30906.1, ECO:0000313|Proteomes:UP000244932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CeCT 8812 {ECO:0000313|EMBL:SPF30906.1,
RC   ECO:0000313|Proteomes:UP000244932};
RA   Keele B.F.;
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000294-1};
CC       Note=Binds 2 heme groups. {ECO:0000256|PIRSR:PIRSR000294-1};
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC   -!- PTM: Binds 2 heme groups per subunit. {ECO:0000256|PIRSR:PIRSR000294-
CC       1}.
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DR   EMBL; OMKW01000004; SPF30906.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2R8AFE6; -.
DR   OrthoDB; 9805202at2; -.
DR   Proteomes; UP000244932; Unassembled WGS sequence.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004130; F:cytochrome-c peroxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR004852; Di-haem_cyt_c_peroxidsae.
DR   InterPro; IPR026259; MauG/Cytc_peroxidase.
DR   PANTHER; PTHR30600; CYTOCHROME C PEROXIDASE-RELATED; 1.
DR   Pfam; PF03150; CCP_MauG; 1.
DR   PIRSF; PIRSF000294; Cytochrome-c_peroxidase; 3.
DR   SUPFAM; SSF46626; Cytochrome c; 2.
DR   PROSITE; PS51007; CYTC; 2.
PE   4: Predicted;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000294-1};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000294-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000294-2};
KW   Oxidoreductase {ECO:0000313|EMBL:SPF30906.1};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Peroxidase {ECO:0000313|EMBL:SPF30906.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000244932};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..429
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015331613"
FT   DOMAIN          33..203
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   DOMAIN          247..406
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   REGION          75..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         55
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000294-1"
FT   BINDING         58
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000294-1"
FT   BINDING         59
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:PIRSR000294-2"
FT   BINDING         262
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000294-1"
FT   BINDING         265
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000294-1"
FT   BINDING         266
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:PIRSR000294-2"
SQ   SEQUENCE   429 AA;  45752 MW;  ADBCE103E332DF7B CRC64;
     MKRILLCSLL AAPAGAQEFS APTDADYFPI NHALAEIGRD LFFDPILSGN RTISCATCHH
     PDHATADGVA LSLGEGGQGL GPERVASTDN PPEQRIPRNA PALFNLGARE FTVMFHDGRL
     EADETRPGGI RTPLGQDMVS GFSGVLSAQT MFPVLSDDEM AGHYSENDIS QAVRQGFITG
     EQGAWALISA RVAALPGYAD RFEAVLGTRD IGFTDISDAV AEFMALEWRS DQSPFDAYLR
     DGTPLPDAAE RGRILFYGEA GCAECHSGPF QTDHDFHALA MPQAGPGKAA SFESHARDEG
     RLRVTGDPAD AYAFRTPSLR NVALTGPYSH AGAYATLEGV IRHHLNPAES LISYDRTQFV
     VPAGFDDWQV LDGPDLEPLL ASAPAPGPQL DDAEIADIIA FLEALTDEAS VAGRLGIPDT
     VPSGLPIDR
//
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