CCOP2_PSEST
ID CCOP2_PSEST Reviewed; 305 AA.
AC Q8KS19;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Cbb3-type cytochrome c oxidase subunit CcoP2 {ECO:0000250|UniProtKB:D9IA45};
DE Short=Cbb3-Cox subunit CcoP2 {ECO:0000250|UniProtKB:D5ARP7};
DE AltName: Full=C-type cytochrome CcoP2 {ECO:0000250|UniProtKB:Q52689};
DE Short=Cyt c(P2) {ECO:0000250|UniProtKB:D5ARP7};
DE AltName: Full=Cytochrome c oxidase subunit III {ECO:0000312|EMBL:ADJ00006.1};
GN Name=ccoP2 {ECO:0000312|EMBL:ADJ00006.1};
OS Pseudomonas stutzeri (Pseudomonas perfectomarina).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=316;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAM76067.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY OF THE
RP CYTOCHROME C OXIDASE COMPLEX, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, MASS
RP SPECTROMETRY, MAGNETIC CIRCULAR DICHROISM, AND EPR SPECTROSCOPY.
RX PubMed=12070166; DOI=10.1074/jbc.m204103200;
RA Pitcher R.S., Cheesman M.R., Watmough N.J.;
RT "Molecular and spectroscopic analysis of the cytochrome cbb(3) oxidase from
RT Pseudomonas stutzeri.";
RL J. Biol. Chem. 277:31474-31483(2002).
RN [2] {ECO:0000312|EMBL:ADJ00006.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 14405 / JCM 20778 / CIP 107696 / IAM 12931 / LMG 2243 / NCIMB
RC 568 / 218 / ZoBell 632 {ECO:0000312|EMBL:ADJ00006.1};
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).
RN [3] {ECO:0000305}
RP FUNCTION, COFACTOR, AND SUBSTRATE ANALOG-PROTEIN INTERACTION AND KINETICS.
RX PubMed=14503876; DOI=10.1021/bi0343469;
RA Pitcher R.S., Brittain T., Watmough N.J.;
RT "Complex interactions of carbon monoxide with reduced cytochrome cbb3
RT oxidase from Pseudomonas stutzeri.";
RL Biochemistry 42:11263-11271(2003).
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. {ECO:0000250|UniProtKB:D9IA45, ECO:0000250|UniProtKB:Q3J015,
CC ECO:0000269|PubMed:12070166, ECO:0000269|PubMed:14503876}.
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000250|UniProtKB:D9IA45, ECO:0000269|PubMed:12070166,
CC ECO:0000269|PubMed:14503876};
CC Note=Binds 2 heme C groups per subunit. {ECO:0000250|UniProtKB:D9IA45,
CC ECO:0000269|PubMed:12070166, ECO:0000269|PubMed:14503876};
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:12070166}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:12070166}; Multi-pass membrane protein
CC {ECO:0000255, ECO:0000269|PubMed:12070166}.
CC -!- MASS SPECTROMETRY: Mass=34943; Method=SELDI;
CC Evidence={ECO:0000269|PubMed:12070166};
CC -!- SIMILARITY: Belongs to the CcoP / FixP family. {ECO:0000305}.
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DR EMBL; AF521004; AAM76067.1; -; Genomic_DNA.
DR EMBL; HM130676; ADJ00006.1; -; Genomic_DNA.
DR RefSeq; WP_003285367.1; NZ_POUM01000002.1.
DR AlphaFoldDB; Q8KS19; -.
DR SMR; Q8KS19; -.
DR STRING; 32042.PstZobell_19010; -.
DR eggNOG; COG2010; Bacteria.
DR UniPathway; UPA00705; -.
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:0005506; F:iron ion binding; IEA:InterPro.
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; IPR008168; Cyt_C_IC.
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 PRINTS; PR00605; CYTCHROMECIC.
DR SUPFAM; SSF46626; SSF46626; 2.
DR TIGRFAMs; TIGR00782; ccoP; 1.
DR PROSITE; PS51007; CYTC; 2.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; 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..305
FT /note="Cbb3-type cytochrome c oxidase subunit CcoP2"
FT /id="PRO_0000412289"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 130..209
FT /note="Cytochrome c 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT DOMAIN 219..300
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:0000250|UniProtKB:D9IA45"
FT BINDING 146
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:D9IA45"
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:0000250|UniProtKB:D9IA45"
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:0000250|UniProtKB:D9IA45"
FT BINDING 232
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:D9IA45"
FT BINDING 235
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:D9IA45"
FT BINDING 236
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:0000250|UniProtKB:D9IA45"
FT BINDING 277
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:0000250|UniProtKB:D9IA45"
SQ SEQUENCE 305 AA; 33780 MW; 63E7101681AD8E91 CRC64;
MTSFWSWYVT LLSLGTIAAL VWLLLATRKG QRPDSTEETV GHSYDGIEEY DNPLPRWWFM
LFVGTVIFAL GYLVLYPGLG NWKGILPGYE GGWTQVKEWQ REMDKANEQY GPLYAKYAAM
PVEEVAKDPQ ALKMGGRLFA SNCSVCHGSD AKGAYGFPNL TDDDWLWGGE PETIKTTILH
GRQAVMPGWK DVIGEEGIRN VAGYVRSLSG RDTPEGISVD IEQGQKIFAA NCVVCHGPEA
KGVTAMGAPN LTDNVWLYGS SFAQIQQTLR YGRNGRMPAQ EAILGNDKVH LLAAYVYSLS
QQPEQ
