CCOP_RHOCB
ID CCOP_RHOCB Reviewed; 297 AA.
AC D5ARP7; O30730;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Cbb3-type cytochrome c oxidase subunit CcoP {ECO:0000303|PubMed:9473054};
DE Short=Cbb3-Cox subunit CcoP {ECO:0000303|PubMed:18556791};
DE AltName: Full=C-type cytochrome CcoP {ECO:0000250|UniProtKB:Q52689};
DE Short=Cyt c(P) {ECO:0000303|PubMed:9473054};
DE AltName: Full=Cytochrome c oxidase subunit III {ECO:0000303|PubMed:9473054};
GN Name=ccoP {ECO:0000312|EMBL:ADE84918.1}; OrderedLocusNames=RCAP_rcc01160;
OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=272942;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC46111.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY OF THE
RP CYTOCHROME C OXIDASE COMPLEX, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=MT1131 {ECO:0000312|EMBL:AAC46111.1};
RX PubMed=9473054; DOI=10.1128/jb.180.4.969-978.1998;
RA Koch H.G., Hwang O., Daldal F.;
RT "Isolation and characterization of Rhodobacter capsulatus mutants affected
RT in cytochrome cbb3 oxidase activity.";
RL J. Bacteriol. 180:969-978(1998).
RN [2] {ECO:0000312|EMBL:ADE84918.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003 {ECO:0000312|EMBL:ADE84918.1};
RX PubMed=20418398; DOI=10.1128/jb.00366-10;
RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA Haselkorn R.;
RT "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT Rhodobacter capsulatus SB 1003.";
RL J. Bacteriol. 192:3545-3546(2010).
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 86-107; 261-276 AND 285-297, FUNCTION, CATALYTIC
RP ACTIVITY OF THE CYTOCHROME C OXIDASE COMPLEX, COFACTOR, SUBUNIT, EPR
RP SPECTROSCOPY OF THE CYTOCHROME C OXIDASE COMPLEX, AND REDOX POTENTIOMETRY
RP OF HEMES.
RC STRAIN=MT1131 {ECO:0000269|PubMed:8130227};
RX PubMed=8130227; DOI=10.1021/bi00176a047;
RA Gray K.A., Grooms M., Myllykallio H., Moomaw C., Slaughter C., Daldal F.;
RT "Rhodobacter capsulatus contains a novel cb-type cytochrome c oxidase
RT without a CuA center.";
RL Biochemistry 33:3120-3127(1994).
RN [4] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY OF THE CYTOCHROME C OXIDASE COMPLEX, AND
RP SUBUNIT.
RC STRAIN=MT1131 {ECO:0000269|PubMed:17143652};
RX PubMed=17143652; DOI=10.1007/s11033-006-9031-9;
RA Ozturk M., Mandaci S.;
RT "Two conserved non-canonical histidines are essential for activity of the
RT cbb (3)-type oxidase in Rhodobacter capsulatus: non-canonical histidines
RT are essential for cbb (3)-type oxidase activity in R. capsulatus.";
RL Mol. Biol. Rep. 34:165-172(2007).
RN [5] {ECO:0000305}
RP FUNCTION, AND CATALYTIC ACTIVITY OF THE CYTOCHROME C OXIDASE COMPLEX.
RC STRAIN=MT1131 {ECO:0000269|PubMed:18556791};
RX PubMed=18556791; DOI=10.1128/jb.00534-08;
RA Peters A., Kulajta C., Pawlik G., Daldal F., Koch H.G.;
RT "Stability of the cbb3-type cytochrome oxidase requires specific CcoQ-CcoP
RT interactions.";
RL J. Bacteriol. 190:5576-5586(2008).
RN [6] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY OF THE CYTOCHROME C OXIDASE COMPLEX, SUBUNIT,
RP AND INTERACTION WITH CCOH.
RC STRAIN=MT1131 {ECO:0000269|PubMed:20952576};
RX PubMed=20952576; DOI=10.1128/jb.00988-10;
RA Pawlik G., Kulajta C., Sachelaru I., Schroder S., Waidner B., Hellwig P.,
RA Daldal F., Koch H.G.;
RT "The putative assembly factor CcoH is stably associated with the cbb3-type
RT cytochrome oxidase.";
RL J. Bacteriol. 192:6378-6389(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. {ECO:0000250|UniProtKB:Q3J015, ECO:0000269|PubMed:17143652,
CC ECO:0000269|PubMed:18556791, ECO:0000269|PubMed:20952576,
CC ECO:0000269|PubMed:8130227, ECO:0000269|PubMed:9473054,
CC ECO:0000303|PubMed:20952576}.
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000250|UniProtKB:D9IA45, ECO:0000269|PubMed:8130227};
CC Note=Binds 2 heme C groups per subunit. {ECO:0000250|UniProtKB:D9IA45,
CC ECO:0000269|PubMed:8130227};
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000305|PubMed:17143652, ECO:0000305|PubMed:18556791,
CC ECO:0000305|PubMed:20952576, ECO:0000305|PubMed:8130227,
CC ECO:0000305|PubMed:9473054}.
CC -!- SUBUNIT: Component of the cbb3-type cytochrome c oxidase at least
CC composed of CcoN, CcoO, CcoQ and CcoP. Interacts with CcoH (via
CC transmembrane domain). {ECO:0000269|PubMed:17143652,
CC ECO:0000269|PubMed:20952576, ECO:0000269|PubMed:8130227,
CC ECO:0000269|PubMed:9473054}.
CC -!- INTERACTION:
CC D5ARP7; O30729: ccoQ; Xeno; NbExp=2; IntAct=EBI-6440217, EBI-6403447;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:Q8KS19, ECO:0000255}; Single-pass membrane
CC protein {ECO:0000250|UniProtKB:Q8KS19, ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: No oxygen uptake activity by the cbb3-type
CC cytochrome c oxidase complex can be detected.
CC {ECO:0000269|PubMed:9473054}.
CC -!- SIMILARITY: Belongs to the CcoP / FixP family. {ECO:0000305}.
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DR EMBL; AF016223; AAC46111.1; -; Genomic_DNA.
DR EMBL; CP001312; ADE84918.1; -; Genomic_DNA.
DR RefSeq; WP_013066897.1; NC_014034.1.
DR PDB; 6XKW; EM; 5.20 A; p=1-297.
DR PDB; 6XKX; EM; 6.10 A; p=1-297.
DR PDB; 6XKZ; EM; 7.20 A; p=1-297.
DR PDBsum; 6XKW; -.
DR PDBsum; 6XKX; -.
DR PDBsum; 6XKZ; -.
DR AlphaFoldDB; D5ARP7; -.
DR SMR; D5ARP7; -.
DR IntAct; D5ARP7; 1.
DR STRING; 272942.RCAP_rcc01160; -.
DR EnsemblBacteria; ADE84918; ADE84918; RCAP_rcc01160.
DR GeneID; 31490073; -.
DR KEGG; rcp:RCAP_rcc01160; -.
DR eggNOG; COG2010; Bacteria.
DR HOGENOM; CLU_047545_2_0_5; -.
DR OMA; DWLYGGE; -.
DR OrthoDB; 1315115at2; -.
DR BioCyc; MetaCyc:MON-20999; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000002361; Chromosome.
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; PF00034; Cytochrom_C; 1.
DR Pfam; PF13442; Cytochrome_CBB3; 1.
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; Reference proteome; Repeat; Respiratory chain;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..297
FT /note="Cbb3-type cytochrome c oxidase subunit CcoP"
FT /id="PRO_0000412292"
FT TOPO_DOM 1..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q3J015, ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..297
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q3J015, ECO:0000255"
FT DOMAIN 108..199
FT /note="Cytochrome c 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT DOMAIN 206..294
FT /note="Cytochrome c 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 121
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 124
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 125
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 174
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 219
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 222
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 223
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 264
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 VARIANT 57
FT /note="A -> P (in strain: MT1131)"
FT /evidence="ECO:0000269|PubMed:9473054"
FT VARIANT 66
FT /note="G -> R (in strain: MT1131)"
FT /evidence="ECO:0000269|PubMed:9473054"
FT VARIANT 96
FT /note="L -> V (in strain: MT1131)"
FT /evidence="ECO:0000269|PubMed:9473054"
FT VARIANT 250
FT /note="N -> K (in strain: MT1131)"
FT /evidence="ECO:0000269|PubMed:9473054"
FT CONFLICT 261..262
FT /note="GG -> AT (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 297 AA; 31712 MW; 2D21069DC82D99C2 CRC64;
MSKKPTTKKE VQTTGHSWDG IEELNTPLPR WWLWTFYATI VWGVAYSIAM PAWPIFASGA
TPGILGSSTR ADVEKDIAKF AEMNKAVEDK LVATDLTAIA ADPELVTYTR NAGAAVFRTW
CAQCHGAGAG GNTGFPSLLD GDWLHGGSIE TIYTNIKHGI RDPLDPDTLP VANMPAHLTD
ELLEPAQIDD VVQYVLKISG QPADEARATA GQQVFADNCV SCHGEDAKGM VEMGAPNLTD
GIWLYGGDAN TITTTIQLGR GGVMPSWSWA ADGAKPRLSE AQIRAVASYV HSLGGGQ
