ID A0A378UI71_BERDE Unreviewed; 378 AA.
AC A0A378UI71;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Protein CcpR {ECO:0000313|EMBL:STZ77017.1};
DE EC=1.11.1.5 {ECO:0000313|EMBL:STZ77017.1};
GN Name=ccpA_1 {ECO:0000313|EMBL:STZ77017.1};
GN ORFNames=NCTC10295_01817 {ECO:0000313|EMBL:STZ77017.1};
OS Bergeriella denitrificans (Neisseria denitrificans).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Bergeriella.
OX NCBI_TaxID=494 {ECO:0000313|EMBL:STZ77017.1, ECO:0000313|Proteomes:UP000254651};
RN [1] {ECO:0000313|EMBL:STZ77017.1, ECO:0000313|Proteomes:UP000254651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10295 {ECO:0000313|EMBL:STZ77017.1,
RC ECO:0000313|Proteomes:UP000254651};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-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; UGQS01000002; STZ77017.1; -; Genomic_DNA.
DR RefSeq; WP_066080393.1; NZ_UGQS01000002.1.
DR AlphaFoldDB; A0A378UI71; -.
DR Proteomes; UP000254651; 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 PANTHER; PTHR30600:SF7; CYTOCHROME C PEROXIDASE-RELATED; 1.
DR Pfam; PF03150; CCP_MauG; 1.
DR Pfam; PF00034; Cytochrom_C; 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:STZ77017.1};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Peroxidase {ECO:0000313|EMBL:STZ77017.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000254651};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..378
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016772863"
FT DOMAIN 80..189
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 233..352
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT REGION 30..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 102
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 105
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 106
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 122
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 247
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 250
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 251
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 327
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 378 AA; 40914 MW; E4BF9AF6563FC537 CRC64;
MNTLPFGKLT FSLILAAALA ACGKQPAEAP QAPAEASAPA AAEQSQISAE DKDLLSRAQS
IFKPLPTAEE MQQLRPFTPE QAELGRQLWY EPRLSKGNTV SCNSCHNLAS AGVDNLPTSQ
GHKGAFGGRN SPTALNAATL GMQFWDGRAA DVEEQAGGPL LNPVEMANTS EAAVEAKIQN
IPEYQALFKT AFPEDGAVSF KNITTAIAAF ERTLLTPTKW DDYLKGNASA LNAQERKGLR
AFMDNGCISC HSGMNLGGNS FQKFGLVQGP YWKFIEDPNH DKGRADVTNK AEDEFFFRVP
GLRNVAKTYP YFHNGSVWEL EKAVQIMGQA QLGKELPQAE VDDIVAFLNT LSGSVPEQAR
TMPELPLSQP LEAKPDNK
//
