CCOP1_PSEST
ID CCOP1_PSEST Reviewed; 311 AA.
AC D9IA45;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Cbb3-type cytochrome c oxidase subunit CcoP1 {ECO:0000250|UniProtKB:D5ARP7, ECO:0000312|PDB:3MK7};
DE Short=Cbb3-Cox subunit CcoP1 {ECO:0000250|UniProtKB:D5ARP7};
DE AltName: Full=C-type cytochrome CcoP1 {ECO:0000250|UniProtKB:Q52689};
DE Short=Cyt c(P1) {ECO:0000250|UniProtKB:D5ARP7};
DE AltName: Full=Cytochrome c oxidase subunit III {ECO:0000250|UniProtKB:D5ARP7, ECO:0000312|EMBL:ADJ00002.1};
GN Name=ccoP1 {ECO:0000312|EMBL:ADJ00002.1};
OS Pseudomonas stutzeri (Pseudomonas perfectomarina).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=316;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ADJ00002.1, ECO:0000312|PDB:3MK7}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 30-58; 82-97;
RP 110-133; 183-199; 260-267 AND 300-311, COFACTOR, SUBUNIT, X-RAY
RP CRYSTALLOGRAPHY (3.20 ANGSTROMS) IN COMPLEX WITH HEME C, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=ATCC 14405 / JCM 20778 / CIP 107696 / IAM 12931 / LMG 2243 / NCIMB
RC 568 / 218 / ZoBell 632 {ECO:0000312|EMBL:ADJ00002.1};
RX PubMed=20576851; DOI=10.1126/science.1187303;
RA Buschmann S., Warkentin E., Xie H., Langer J.D., Ermler U., Michel H.;
RT "The structure of cbb3 cytochrome oxidase provides insights into proton
RT pumping.";
RL Science 329:327-330(2010).
CC -!- FUNCTION: C-type cytochrome. Part of the cbb3-type cytochrome c oxidase
CC complex. CcoP subunit is required for transferring electrons from donor
CC cytochrome c via its heme groups to CcoO subunit. From there, electrons
CC are shuttled to the catalytic binuclear center of CcoN subunit where
CC oxygen reduction takes place. The complex also functions as a proton
CC pump (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000269|PubMed:20576851};
CC Note=Binds 2 heme C groups per subunit. {ECO:0000269|PubMed:20576851};
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000250|UniProtKB:D5ARP7}.
CC -!- SUBUNIT: Component of the cbb3-type cytochrome c oxidase at least
CC composed of CcoN, CcoO, CcoQ and CcoP. {ECO:0000269|PubMed:20576851}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:Q8KS19, ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:Q8KS19, ECO:0000255}.
CC -!- SIMILARITY: Belongs to the CcoP / FixP family. {ECO:0000305}.
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DR EMBL; HM130676; ADJ00002.1; -; Genomic_DNA.
DR RefSeq; WP_003285277.1; NZ_POUM01000002.1.
DR PDB; 3MK7; X-ray; 3.20 A; C/F/I/M=1-311.
DR PDB; 5DJQ; X-ray; 3.20 A; C/F/I/M=1-311.
DR PDBsum; 3MK7; -.
DR PDBsum; 5DJQ; -.
DR AlphaFoldDB; D9IA45; -.
DR SMR; D9IA45; -.
DR STRING; 32042.PstZobell_18665; -.
DR TCDB; 3.D.4.3.3; the proton-translocating cytochrome oxidase (cox) superfamily.
DR UniPathway; UPA00705; -.
DR EvolutionaryTrace; D9IA45; -.
DR GO; GO:0070069; C:cytochrome complex; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
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 GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.760.10; -; 2.
DR Gene3D; 6.10.280.130; -; 1.
DR InterPro; IPR032858; CcoP_N.
DR InterPro; IPR038414; CcoP_N_sf.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR004678; Cyt_c_oxidase_cbb3_su3.
DR Pfam; PF13442; Cytochrome_CBB3; 2.
DR Pfam; PF14715; FixP_N; 1.
DR PIRSF; PIRSF000006; Cbb3-Cox_fixP; 1.
DR SUPFAM; SSF46626; SSF46626; 2.
DR TIGRFAMs; TIGR00782; ccoP; 1.
DR PROSITE; PS51007; CYTC; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane;
KW Direct protein sequencing; Electron transport; Heme;
KW Hydrogen ion transport; Ion transport; Iron; Membrane; Metal-binding;
KW Oxidoreductase; Repeat; Respiratory chain; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..311
FT /note="Cbb3-type cytochrome c oxidase subunit CcoP1"
FT /id="PRO_0000412288"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:20576851"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:20576851"
FT DOMAIN 130..209
FT /note="Cytochrome c 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT DOMAIN 220..302
FT /note="Cytochrome c 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 143
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:20576851"
FT BINDING 146
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:20576851"
FT BINDING 147
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:0000269|PubMed:20576851"
FT BINDING 186
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:0000269|PubMed:20576851"
FT BINDING 233
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:20576851"
FT BINDING 236
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:20576851"
FT BINDING 237
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:0000269|PubMed:20576851"
FT BINDING 279
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:0000269|PubMed:20576851"
FT HELIX 3..26
FT /evidence="ECO:0007829|PDB:3MK7"
FT TURN 27..30
FT /evidence="ECO:0007829|PDB:3MK7"
FT HELIX 56..75
FT /evidence="ECO:0007829|PDB:3MK7"
FT HELIX 95..118
FT /evidence="ECO:0007829|PDB:3MK7"
FT HELIX 122..126
FT /evidence="ECO:0007829|PDB:3MK7"
FT HELIX 129..142
FT /evidence="ECO:0007829|PDB:3MK7"
FT HELIX 144..147
FT /evidence="ECO:0007829|PDB:3MK7"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:3MK7"
FT HELIX 171..180
FT /evidence="ECO:0007829|PDB:3MK7"
FT HELIX 190..193
FT /evidence="ECO:0007829|PDB:3MK7"
FT HELIX 195..207
FT /evidence="ECO:0007829|PDB:3MK7"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:3MK7"
FT HELIX 222..231
FT /evidence="ECO:0007829|PDB:3MK7"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:3MK7"
FT TURN 245..248
FT /evidence="ECO:0007829|PDB:3MK7"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:3MK7"
FT HELIX 264..273
FT /evidence="ECO:0007829|PDB:3MK7"
FT TURN 283..286
FT /evidence="ECO:0007829|PDB:3MK7"
FT HELIX 287..301
FT /evidence="ECO:0007829|PDB:3MK7"
SQ SEQUENCE 311 AA; 33663 MW; 7ADEF88985C42E4F CRC64;
MSTFWSGYIA LLTLGTIVAL FWLIFATRKG ESAGTTDQTM GHAFDGIEEY DNPLPRWWFL
LFIGTLVFGI LYLVLYPGLG NWKGVLPGYE GGWTQEKQWE REVAQADEKY GPIFAKYAAM
SVEEVAQDPQ AVKMGARLFA NYCSICHGSD AKGSLGFPNL ADQDWRWGGD AASIKTSILN
GRIAAMPAWG QAIGEEGVKN VAAFVRKDLA GLPLPEGTDA DLSAGKNVYA QTCAVCHGQG
GEGMAALGAP KLNSAAGWIY GSSLGQLQQT IRHGRNGQMP AQQQYLGDDK VHLLAAYVYS
LSQKPEQLAN Q
