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Database: UniProt
Entry: A0A0A7EBU1_9GAMM
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ID   A0A0A7EBU1_9GAMM        Unreviewed;       369 AA.
AC   A0A0A7EBU1;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Cytochrome C peroxidase {ECO:0000313|EMBL:AIY64085.1};
GN   ORFNames=OM33_02135 {ECO:0000313|EMBL:AIY64085.1};
OS   Pseudoalteromonas piratica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=1348114 {ECO:0000313|EMBL:AIY64085.1, ECO:0000313|Proteomes:UP000030341};
RN   [1] {ECO:0000313|EMBL:AIY64085.1, ECO:0000313|Proteomes:UP000030341}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OCN003 {ECO:0000313|EMBL:AIY64085.1,
RC   ECO:0000313|Proteomes:UP000030341};
RA   Beurmann S., Videau P., Ushijima B., Smith A.M., Aeby G.S., Callahan S.M.,
RA   Belcaid M.;
RT   "Complete Genome Sequence of Pseudoalteromonas sp. Strain OCN003 Isolated
RT   from Kaneohe Bay, Oahu, Hawaii.";
RL   Submitted (NOV-2014) 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; CP009888; AIY64085.1; -; Genomic_DNA.
DR   RefSeq; WP_038638147.1; NZ_CP009888.1.
DR   AlphaFoldDB; A0A0A7EBU1; -.
DR   STRING; 1348114.OM33_02135; -.
DR   KEGG; pseo:OM33_02135; -.
DR   eggNOG; COG1858; Bacteria.
DR   HOGENOM; CLU_034652_3_1_6; -.
DR   OrthoDB; 9805202at2; -.
DR   Proteomes; UP000030341; Chromosome 1.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004601; F:peroxidase activity; 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; IPR023929; Di-heme_enz_MXAN0977.
DR   InterPro; IPR026259; MauG/Cytc_peroxidase.
DR   NCBIfam; TIGR04039; MXAN_0977_Heme2; 1.
DR   PANTHER; PTHR30600:SF12; BLL6722 PROTEIN; 1.
DR   PANTHER; PTHR30600; CYTOCHROME C PEROXIDASE-RELATED; 1.
DR   Pfam; PF03150; CCP_MauG; 1.
DR   PIRSF; PIRSF000294; Cytochrome-c_peroxidase; 1.
DR   SUPFAM; SSF46626; Cytochrome c; 2.
DR   PROSITE; PS51007; CYTC; 2.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
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:AIY64085.1};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Peroxidase {ECO:0000313|EMBL:AIY64085.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030341};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          44..130
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   DOMAIN          201..353
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   BINDING         66
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         69
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         70
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         217
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         220
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         221
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   369 AA;  41708 MW;  DA7ABDD77016AD9A CRC64;
     MRRSLLLFAL LLVGCSEPSK PYKWQLPDGF PEPQVPSTNP MSDAKVELGR HLFYDKNLSA
     NGLQSCASCH QQDRAFAEMI PTSIGSTGEV HHRNAQALVN VAYNKTLTWA HSEMTELEQQ
     ILLPLFGETP LEMGVTGHEE EVLARFNTPE YNALFEHAFD TEDASFDHIV KALASFTRSL
     ISFQSRFDQY AYAMQDDALT ASEIRGMDLF FSERLECHHC HGGFNFTQST THQKQQLDRH
     PFHNTGLYNV DGKGAFPLSD QGLFTITETP QDMGKFRAPT LRNIALTAPY MHDGSLQTLE
     QVIDFYADAG RNITTGKHRG DGRENPYKSA FIKGFQLTEQ EKQDLVAFLH TLTDEKFIKN
     KAFSNPFKQ
//
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