ID A0A1P8W9H3_9PLAN Unreviewed; 369 AA.
AC A0A1P8W9H3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Cytochrome c551 peroxidase {ECO:0000313|EMBL:APZ90705.1};
DE EC=1.11.1.5 {ECO:0000313|EMBL:APZ90705.1};
DE Flags: Precursor;
GN Name=ccp_1 {ECO:0000313|EMBL:APZ90705.1};
GN ORFNames=Fuma_00286 {ECO:0000313|EMBL:APZ90705.1};
OS Fuerstiella marisgermanici.
OC Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC Planctomycetaceae; Fuerstiella.
OX NCBI_TaxID=1891926 {ECO:0000313|EMBL:APZ90705.1, ECO:0000313|Proteomes:UP000187735};
RN [1] {ECO:0000313|EMBL:APZ90705.1, ECO:0000313|Proteomes:UP000187735}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NH11 {ECO:0000313|EMBL:APZ90705.1,
RC ECO:0000313|Proteomes:UP000187735};
RX PubMed=28066393; DOI=10.3389/fmicb.2016.02079;
RA Kohn T., Heuer A., Jogler M., Vollmers J., Boedeker C., Bunk B., Rast P.,
RA Borchert D., Glockner I., Freese H.M., Klenk H.P., Overmann J.,
RA Kaster A.K., Rohde M., Wiegand S., Jogler C.;
RT "Fuerstia marisgermanicae gen. nov., sp. nov., an Unusual Member of the
RT Phylum Planctomycetes from the German Wadden Sea.";
RL Front. Microbiol. 7:2079-2079(2016).
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; CP017641; APZ90705.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1P8W9H3; -.
DR STRING; 1891926.Fuma_00286; -.
DR KEGG; fmr:Fuma_00286; -.
DR Proteomes; UP000187735; Chromosome.
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 PANTHER; PTHR30600:SF7; 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.
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:APZ90705.1};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Peroxidase {ECO:0000313|EMBL:APZ90705.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000187735};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..369
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013179322"
FT DOMAIN 60..188
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 214..340
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT BINDING 82
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 85
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 86
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 228
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 231
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 232
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"
FT BINDING 315
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; 40415 MW; 13DAA97655A7117D CRC64;
MQFAHTRHVV RAALPLVAVL VTAPMANSQP SEQEKHTVSD VWQTLPTRAE SPANNPTTAE
KVELGKQLFF DPRLSLTGTV SCNTCHNLME GGDDGRPSSM GIHGRIGPRN APTVWNSVFQ
TSQFWDGRAP DLEEQAKGPV IAGPEMGMPN HDKAIERVAA IPGYRSAFAT VFGDDDSVTI
DNAVKAIAAF ERTLITPNSA YDRYVDGDRS ALSASQVRGM QLFESAGCTE CHSGPAFNGW
TPGLTDASFE EFPRFSNRRF LDKYALAKDL GRYEVTKQPE DKHQFKVPVL RNITLTAPYF
HNGAVESLAE AVRVMADVQL DMELAEREVT DIVNFMGALE GEFPNITLPR IPSRSGHSIL
EDQDPAATN
//
