CCPR_NITEU
ID CCPR_NITEU Reviewed; 334 AA.
AC P55929;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Cytochrome c551 peroxidase;
DE Short=Cytochrome c peroxidase;
DE EC=1.11.1.5;
DE Flags: Precursor;
GN Name=ccp; OrderedLocusNames=NE1315;
OS Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC
OS 14298).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=228410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298;
RX PubMed=12700255; DOI=10.1128/jb.185.9.2759-2773.2003;
RA Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L.,
RA Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A.,
RA Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.;
RT "Complete genome sequence of the ammonia-oxidizing bacterium and obligate
RT chemolithoautotroph Nitrosomonas europaea.";
RL J. Bacteriol. 185:2759-2773(2003).
RN [2]
RP PROTEIN SEQUENCE OF 27-55; 60-86 AND 206-225.
RC STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298;
RX PubMed=8163487; DOI=10.1016/s0021-9258(17)32655-8;
RA Arciero D.M., Hooper A.B.;
RT "A di-heme cytochrome c peroxidase from Nitrosomonas europaea catalytically
RT active in both the oxidized and half-reduced states.";
RL J. Biol. Chem. 269:11878-11886(1994).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(II)-[cytochrome c] + 2 H(+) + H2O2 = 2 Fe(III)-
CC [cytochrome c] + 2 H2O; Xref=Rhea:RHEA:16581, Rhea:RHEA-COMP:10350,
CC Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.11.1.5;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) are +450 mV (low spin) and -260 mV (high spin).;
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC -!- PTM: Binds 2 heme c groups covalently per subunit.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL954747; CAD85226.1; -; Genomic_DNA.
DR PIR; A53573; A53573.
DR RefSeq; WP_011111893.1; NC_004757.1.
DR PDB; 1IQC; X-ray; 1.80 A; A/B/C/D=27-334.
DR PDBsum; 1IQC; -.
DR AlphaFoldDB; P55929; -.
DR SMR; P55929; -.
DR STRING; 228410.NE1315; -.
DR PeroxiBase; 5004; NeDiHCcP.
DR EnsemblBacteria; CAD85226; CAD85226; NE1315.
DR KEGG; neu:NE1315; -.
DR eggNOG; COG1858; Bacteria.
DR HOGENOM; CLU_034652_1_0_4; -.
DR OMA; KGPINAP; -.
DR OrthoDB; 52724at2; -.
DR PhylomeDB; P55929; -.
DR BRENDA; 1.11.1.5; 3654.
DR EvolutionaryTrace; P55929; -.
DR Proteomes; UP000001416; 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; -; 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 Pfam; PF03150; CCP_MauG; 1.
DR Pfam; PF00034; Cytochrom_C; 1.
DR PIRSF; PIRSF000294; Cytochrome-c_peroxidase; 1.
DR SUPFAM; SSF46626; SSF46626; 2.
DR PROSITE; PS51007; CYTC; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Electron transport; Heme; Iron;
KW Metal-binding; Oxidoreductase; Periplasm; Peroxidase; Reference proteome;
KW Repeat; Signal; Transport.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:8163487"
FT CHAIN 27..334
FT /note="Cytochrome c551 peroxidase"
FT /id="PRO_0000006599"
FT REGION 315..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 65
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 68
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 69
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:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 209
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 212
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 213
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:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 270
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:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 284
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:0000255|PROSITE-ProRule:PRU00433"
FT CONFLICT 77
FT /note="D -> C (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 42..52
FT /evidence="ECO:0007829|PDB:1IQC"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:1IQC"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:1IQC"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:1IQC"
FT TURN 71..74
FT /evidence="ECO:0007829|PDB:1IQC"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:1IQC"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:1IQC"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:1IQC"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:1IQC"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:1IQC"
FT HELIX 115..124
FT /evidence="ECO:0007829|PDB:1IQC"
FT TURN 126..129
FT /evidence="ECO:0007829|PDB:1IQC"
FT HELIX 133..141
FT /evidence="ECO:0007829|PDB:1IQC"
FT HELIX 144..154
FT /evidence="ECO:0007829|PDB:1IQC"
FT HELIX 161..173
FT /evidence="ECO:0007829|PDB:1IQC"
FT HELIX 181..186
FT /evidence="ECO:0007829|PDB:1IQC"
FT HELIX 195..207
FT /evidence="ECO:0007829|PDB:1IQC"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:1IQC"
FT TURN 215..218
FT /evidence="ECO:0007829|PDB:1IQC"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:1IQC"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:1IQC"
FT HELIX 242..245
FT /evidence="ECO:0007829|PDB:1IQC"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:1IQC"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:1IQC"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:1IQC"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:1IQC"
FT HELIX 277..289
FT /evidence="ECO:0007829|PDB:1IQC"
FT HELIX 295..306
FT /evidence="ECO:0007829|PDB:1IQC"
SQ SEQUENCE 334 AA; 36633 MW; 44E67A23550A862C CRC64;
MIKRTLTVSL LSLSLGAMFA SAGVMAANEP IQPIKAVTPE NADMAELGKM LFFDPRLSKS
GFISCNSCHN LSMGGTDNIT TSIGHKWQQG PINAPTVLNS SMNLAQFWDG RAKDLKEQAA
GPIANPKEMA STHEIAEKVV ASMPQYRERF KKVFGSDEVT IDRITTAIAQ FEETLVTPGS
KFDKWLEGDK NALNQDELEG YNLFKGSGCV QCHNGPAVGG SSYQKMGVFK PYETKNPAAG
RMDVTGNEAD RNVFKVPTLR NIELTYPYFH DGGAATLEQA VETMGRIQLN REFNKDEVSK
IVAFLKTLTG DQPDFKLPIL PPSNNDTPRS QPYE
