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   02-SEP-2026, entry version 151.
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; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Nitrosomonadales; 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] + H2O2 + 2 H(+) = 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.
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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   AlphaFoldDB; P55929; -.
DR   SMR; P55929; -.
DR   STRING; 228410.NE1315; -.
DR   PeroxiBase; 5004; NeDiHCcP.
DR   GeneID; 309185225; -.
DR   KEGG; neu:NE1315; -.
DR   eggNOG; COG1858; Bacteria.
DR   HOGENOM; CLU_034652_1_0_4; -.
DR   OrthoDB; 9805202at2; -.
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   FunFam; 1.10.760.10:FF:000004; Cytochrome c peroxidase; 1.
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; IPR051395; Cytochrome_c_Peroxidase/MauG.
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.
DR   PDBsum; 1IQC; -.
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   COMPBIAS        322..334
FT                   /note="Polar residues"
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           93..96
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           256..258
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..284
FT                   /evidence="ECO:0007829|PDB:1IQC"
FT   HELIX           285..289
FT                   /evidence="ECO:0007829|PDB:1IQC"
FT   HELIX           295..306
FT                   /evidence="ECO:0007829|PDB:1IQC"
FT   HELIX           311..313
FT                   /evidence="ECO:0007829|PDB:1IQC"
FT   HELIX           320..323
FT                   /evidence="ECO:0007829|PDB:1IQC"
FT   HELIX           328..330
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
//