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CCOP_PSEU5
ID   CCOP_PSEU5              Reviewed;         311 AA.
AC   A4VKL4;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Cbb3-type cytochrome c oxidase subunit CcoP {ECO:0000250|UniProtKB:D5ARP7};
DE            Short=Cbb3-Cox subunit CcoP {ECO:0000250|UniProtKB:D5ARP7};
DE   AltName: Full=C-type cytochrome CcoP {ECO:0000250|UniProtKB:Q52689};
DE            Short=Cyt c(P) {ECO:0000250|UniProtKB:D5ARP7};
DE   AltName: Full=Cytochrome c oxidase subunit III {ECO:0000312|EMBL:ABP79515.1};
GN   Name=ccoP {ECO:0000250|UniProtKB:D9IA45}; OrderedLocusNames=PST_1841;
OS   Pseudomonas stutzeri (strain A1501).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=379731;
RN   [1] {ECO:0000312|EMBL:ABP79515.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A1501 {ECO:0000312|EMBL:ABP79515.1};
RX   PubMed=18495935; DOI=10.1073/pnas.0801093105;
RA   Yan Y., Yang J., Dou Y., Chen M., Ping S., Peng J., Lu W., Zhang W.,
RA   Yao Z., Li H., Liu W., He S., Geng L., Zhang X., Yang F., Yu H., Zhan Y.,
RA   Li D., Lin Z., Wang Y., Elmerich C., Lin M., Jin Q.;
RT   "Nitrogen fixation island and rhizosphere competence traits in the genome
RT   of root-associated Pseudomonas stutzeri A1501.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:7564-7569(2008).
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|UniProtKB:D5ARP7,
CC       ECO:0000250|UniProtKB:D9IA45, ECO:0000250|UniProtKB:Q3J015}.
CC   -!- COFACTOR:
CC       Name=heme c; Xref=ChEBI:CHEBI:61717;
CC         Evidence={ECO:0000250|UniProtKB:D9IA45};
CC       Note=Binds 2 heme C groups per subunit. {ECO:0000250|UniProtKB:D9IA45};
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:0000250|UniProtKB:D5ARP7}.
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; CP000304; ABP79515.1; -; Genomic_DNA.
DR   RefSeq; WP_011912992.1; NC_009434.1.
DR   AlphaFoldDB; A4VKL4; -.
DR   SMR; A4VKL4; -.
DR   STRING; 379731.PST_1841; -.
DR   EnsemblBacteria; ABP79515; ABP79515; PST_1841.
DR   KEGG; psa:PST_1841; -.
DR   eggNOG; COG2010; Bacteria.
DR   HOGENOM; CLU_047545_2_0_6; -.
DR   OMA; IDQMKSP; -.
DR   UniPathway; UPA00705; -.
DR   Proteomes; UP000000233; 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; 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   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; 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..311
FT                   /note="Cbb3-type cytochrome c oxidase subunit CcoP"
FT                   /id="PRO_0000412290"
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          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: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         233
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                   /note="covalent"
FT                   /evidence="ECO:0000250|UniProtKB:D9IA45"
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:0000250|UniProtKB:D9IA45"
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:0000250|UniProtKB:D9IA45"
SQ   SEQUENCE   311 AA;  33807 MW;  0E9E5855B83DE45B CRC64;
     MSTFWSGYIA LLTLGTIVAL FWLIFATRKG ESAGTTDQTM GHAFDGIEEY DNPLPRWWFL
     LFIGTLVFGI LYLVLYPGLG NWKGVLPGYE GGWTQEKQWE REVSQADEKY GPIFAKYAAM
     SVEQVAQDPQ AVKMGARLFA NYCAICHGSD AKGSLGFPNL ADQHWRWGGD ATSIKTSILN
     GRIAAMPAWG QAIGEEGVKN VAAFVRNELA GLPLPEGTDA DLGKGKEVYA QTCAVCHGQG
     GEGMAALGAP NLQHASGWIY GSSLGQLQQT IRHGRNGQMP AQQQYLGNDK VHLLAAYVYS
     LSKNPEQVAK Q
 
 
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