CCPR_PSEAE
ID CCPR_PSEAE Reviewed; 346 AA.
AC P14532; Q51369;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Cytochrome c551 peroxidase;
DE Short=CCP {ECO:0000303|PubMed:8543038};
DE Short=Cytochrome c peroxidase {ECO:0000303|PubMed:7781769};
DE EC=1.11.1.5 {ECO:0000305|PubMed:1657179};
DE Flags: Precursor;
GN Name=ccpA; OrderedLocusNames=PA4587;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 19429 / NTCC 6750;
RX PubMed=7781769; DOI=10.1016/0014-5793(95)00461-h;
RA Ridout C.J., James R., Greenwood C.;
RT "Nucleotide sequence encoding the di-haem cytochrome c551 peroxidase from
RT Pseudomonas aeruginosa.";
RL FEBS Lett. 365:152-154(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP PROTEIN SEQUENCE OF 24-346, AND MASS SPECTROMETRY.
RC STRAIN=ATCC 10145 / DSM 50071 / JCM 5962 / LMG 1242 / NBRC 12689 / NCIMB
RC 8295 / NCTC 10332 / NRRL B-771;
RX PubMed=8543038; DOI=10.1016/0014-5793(95)01326-1;
RA Samyn B., van Craenenbroeck K., de Smet L., Vandenberghe I., Pettigrew G.,
RA van Beeumen J.;
RT "A reinvestigation of the covalent structure of Pseudomonas aeruginosa
RT cytochrome c peroxidase.";
RL FEBS Lett. 377:145-149(1995).
RN [4]
RP PROTEIN SEQUENCE OF 24-346, AND VARIANTS.
RX PubMed=2546794; DOI=10.1016/0014-5793(89)80714-8;
RA Roennberg M., Kalkkinen N., Ellfolk N.;
RT "The primary structure of Pseudomonas cytochrome c peroxidase.";
RL FEBS Lett. 250:175-178(1989).
RN [5]
RP PARTIAL PROTEIN SEQUENCE, AND COFACTOR.
RX PubMed=3030432; DOI=10.1016/0167-4838(87)90250-0;
RA Roennberg M.;
RT "Amino acid sequences of the two heme c-binding sites of Pseudomonas
RT cytochrome-c peroxidase.";
RL Biochim. Biophys. Acta 912:82-86(1987).
RN [6]
RP CHARACTERIZATION.
RX PubMed=1657179; DOI=10.1016/0167-4838(91)90113-e;
RA Ellfolk N., Roennberg M., Oesterlund K.;
RT "Structural and functional features of Pseudomonas cytochrome c
RT peroxidase.";
RL Biochim. Biophys. Acta 1080:68-77(1991).
RN [7] {ECO:0007744|PDB:1EB7}
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 24-346 IN COMPLEX WITH HEME, AND
RP DOMAIN.
RX PubMed=8591033; DOI=10.1016/s0969-2126(01)00258-1;
RA Fulop V., Ridout C.J., Greenwood C., Hajdu J.;
RT "Crystal structure of the di-haem cytochrome c peroxidase from Pseudomonas
RT aeruginosa.";
RL Structure 3:1225-1233(1995).
CC -!- FUNCTION: Catalyzes the peroxidative oxidation of azurin and cytochrome
CC c551. Likely to provide protection against toxic peroxides.
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 Evidence={ECO:0000305|PubMed:1657179};
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000269|PubMed:3030432};
CC Note=Binds 2 heme c groups covalently. Heme 1 is low-potential (-330
CC mV) with 2 His axial ligands and functions in the peroxidase reaction,
CC while heme 2 is high potential (+320 mV) with His and Met axial ligands
CC and functions to feed electrons from electron-shuttle proteins such as
CC cytochrome c and azurin. {ECO:0000305|PubMed:1657179};
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC -!- DOMAIN: Organized into two domains, each containing a covalent c-heme
CC in a structure reminiscent of class 1 cytochromes c. The domains are
CC related by a quasi-twofold axis. The domain interface contains a
CC calcium-binding site with an unusual set of ligands.
CC {ECO:0000269|PubMed:8591033}.
CC -!- PTM: Binds 2 heme groups per subunit (PubMed:8591033). Sequencing of
CC the whole protein indicates about 20% starts on Val-247
CC (PubMed:8543038). {ECO:0000269|PubMed:8543038,
CC ECO:0000269|PubMed:8591033}.
CC -!- MASS SPECTROMETRY: Mass=36251.4; Method=Electrospray; Note=Mature
CC protein with 2 bound heme groups.;
CC Evidence={ECO:0000269|PubMed:8543038};
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DR EMBL; U23766; AAC43378.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG07975.1; -; Genomic_DNA.
DR PIR; I53515; I53515.
DR RefSeq; NP_253277.1; NC_002516.2.
DR RefSeq; WP_003094815.1; NZ_QZGE01000004.1.
DR PDB; 1EB7; X-ray; 2.40 A; A=24-346.
DR PDB; 2VHD; X-ray; 2.30 A; A/B=24-346.
DR PDBsum; 1EB7; -.
DR PDBsum; 2VHD; -.
DR AlphaFoldDB; P14532; -.
DR SMR; P14532; -.
DR STRING; 287.DR97_1892; -.
DR DrugBank; DB03317; Ferroheme C.
DR PeroxiBase; 3543; PaerDiHCcP.
DR PaxDb; P14532; -.
DR PRIDE; P14532; -.
DR EnsemblBacteria; AAG07975; AAG07975; PA4587.
DR GeneID; 881021; -.
DR KEGG; pae:PA4587; -.
DR PATRIC; fig|208964.12.peg.4801; -.
DR PseudoCAP; PA4587; -.
DR HOGENOM; CLU_034652_1_1_6; -.
DR InParanoid; P14532; -.
DR OMA; KGPINAP; -.
DR PhylomeDB; P14532; -.
DR BioCyc; MetaCyc:MON-17891; -.
DR BioCyc; PAER208964:G1FZ6-4681-MON; -.
DR BRENDA; 1.11.1.5; 5087.
DR EvolutionaryTrace; P14532; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004130; F:cytochrome-c peroxidase activity; IDA:PseudoCAP.
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 Signal; Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:2546794,
FT ECO:0000269|PubMed:8543038"
FT CHAIN 24..346
FT /note="Cytochrome c551 peroxidase"
FT /evidence="ECO:0000269|PubMed:7781769"
FT /id="PRO_0000006598"
FT BINDING 74
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:1EB7"
FT BINDING 77
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:1EB7"
FT BINDING 78
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:0007744|PDB:1EB7"
FT BINDING 220
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:1EB7"
FT BINDING 223
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:1EB7"
FT BINDING 224
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:0007744|PDB:1EB7"
FT BINDING 284
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 BINDING 298
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:0007744|PDB:1EB7"
FT VARIANT 81
FT /note="G -> D"
FT /evidence="ECO:0000305|PubMed:2546794"
FT VARIANT 83
FT /note="G -> D"
FT /evidence="ECO:0000305|PubMed:2546794"
FT VARIANT 152
FT /note="I -> V"
FT /evidence="ECO:0000305|PubMed:2546794"
FT VARIANT 164
FT /note="P -> A"
FT /evidence="ECO:0000305|PubMed:2546794"
FT VARIANT 198
FT /note="K -> I"
FT /evidence="ECO:0000305|PubMed:2546794"
FT VARIANT 334
FT /note="L -> W"
FT /evidence="ECO:0000305|PubMed:2546794"
FT CONFLICT 86
FT /note="D -> G (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="Missing (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="W -> G (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 102..120
FT /note="Missing (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="E -> Q (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="M -> V (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="C -> K (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="Missing (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 286..287
FT /note="GQ -> QG (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="E -> Q (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 25..33
FT /evidence="ECO:0007829|PDB:2VHD"
FT HELIX 51..61
FT /evidence="ECO:0007829|PDB:2VHD"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:2VHD"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:2VHD"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:2VHD"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:2VHD"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:2VHD"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:2VHD"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:2VHD"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:2VHD"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:2VHD"
FT HELIX 124..127
FT /evidence="ECO:0007829|PDB:2VHD"
FT HELIX 129..133
FT /evidence="ECO:0007829|PDB:2VHD"
FT TURN 135..138
FT /evidence="ECO:0007829|PDB:2VHD"
FT HELIX 142..150
FT /evidence="ECO:0007829|PDB:2VHD"
FT HELIX 153..162
FT /evidence="ECO:0007829|PDB:2VHD"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:1EB7"
FT HELIX 172..183
FT /evidence="ECO:0007829|PDB:2VHD"
FT HELIX 192..197
FT /evidence="ECO:0007829|PDB:2VHD"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:2VHD"
FT HELIX 206..217
FT /evidence="ECO:0007829|PDB:2VHD"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:2VHD"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:2VHD"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:2VHD"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:2VHD"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:2VHD"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:2VHD"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:1EB7"
FT HELIX 256..259
FT /evidence="ECO:0007829|PDB:2VHD"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:2VHD"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:2VHD"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:2VHD"
FT TURN 283..286
FT /evidence="ECO:0007829|PDB:2VHD"
FT HELIX 291..303
FT /evidence="ECO:0007829|PDB:2VHD"
FT HELIX 309..320
FT /evidence="ECO:0007829|PDB:2VHD"
SQ SEQUENCE 346 AA; 37403 MW; 8B402E5BA149EA44 CRC64;
MQSSQLLPLG SLLLSFATPL AQADALHDQA SALFKPIPEQ VTELRGQPIS EQQRELGKKL
FFDPRLSRSH VLSCNTCHNV GTGGADNVPT SVGHGWQKGP RNSPTVFNAV FNAAQFWDGR
AKDLGEQAKG PIQNSVEMHS TPQLVEQTLG SIPEYVDAFR KAFPKAGKPV SFDNMALAIE
AYEATLVTPD SPFDLYLKGD DKALDAQQKK GLKAFMDSGC SACHNGINLG GQAYFPFGLV
KKPDASVLPS GDKGRFAVTK TQSDEYVFRA APLRNVALTA PYFHSGQVWE LKDAVAIMGN
AQLGKQLAPD DVENIVAFLH SLSGKQPRVE YPLLPASTET TPRPAE
