ID   P84153_CERSP            Unreviewed;       266 AA.
AC   P84153;
DT   13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2004, sequence version 1.
DT   27-MAR-2024, entry version 109.
DE   RecName: Full=cytochrome-c oxidase {ECO:0000256|ARBA:ARBA00012949};
DE            EC=7.1.1.9 {ECO:0000256|ARBA:ARBA00012949};
DE   AltName: Full=Cytochrome aa3 subunit 3 {ECO:0000256|ARBA:ARBA00031400};
DE   AltName: Full=Cytochrome c oxidase polypeptide III {ECO:0000256|ARBA:ARBA00031625};
GN   ORFNames=EBL86_02290 {ECO:0000313|EMBL:AZB67285.1};
OS   Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Cereibacter.
OX   NCBI_TaxID=1063 {ECO:0000313|PDB:1M56, ECO:0000313|PDB:1M57};
RN   [1] {ECO:0007829|PDB:1M56, ECO:0007829|PDB:1M57}
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS).
RX   PubMed=12144789; DOI=10.1016/S0022-2836(02)00619-8;
RA   Svensson-Ek M., Abramson J., Larsson G., Tornroth S., Brzezinski P.,
RA   Iwata S.;
RT   "The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome
RT   c oxidases from Rhodobacter sphaeroides.";
RL   J. Mol. Biol. 321:329-339(2002).
RN   [2] {ECO:0007829|PDB:5WEH}
RP   X-RAY CRYSTALLOGRAPHY (3.45 ANGSTROMS).
RX   PubMed=28842531; DOI=10.1042/BST20160138;
RA   Liu J., Hiser C., Ferguson-Miller S.;
RT   "Role of conformational change and K-path ligands in controlling cytochrome
RT   <i>c</i> oxidase activity.";
RL   Biochem. Soc. Trans. 45:1087-1095(2017).
RN   [3] {ECO:0000313|EMBL:AZB67285.1, ECO:0000313|Proteomes:UP000278666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AB24 {ECO:0000313|EMBL:AZB67285.1,
RC   ECO:0000313|Proteomes:UP000278666};
RA   Guzman M.S., Bose A.;
RT   "Draft genome sequences of four Rhodobacter sphaeroides strains.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU003376};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU003376}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 3 family.
CC       {ECO:0000256|ARBA:ARBA00010581, ECO:0000256|RuleBase:RU003376}.
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DR   EMBL; CP033434; AZB67285.1; -; Genomic_DNA.
DR   RefSeq; WP_002722701.1; NZ_WTFI01000005.1.
DR   PDB; 1M56; X-ray; 2.30 A; C/I=1-266.
DR   PDB; 1M57; X-ray; 3.00 A; C/I=1-266.
DR   PDB; 5WEH; X-ray; 3.45 A; C/I=1-266.
DR   PDBsum; 1M56; -.
DR   PDBsum; 1M57; -.
DR   PDBsum; 5WEH; -.
DR   AlphaFoldDB; P84153; -.
DR   SMR; P84153; -.
DR   IntAct; P84153; 1.
DR   GeneID; 67445618; -.
DR   OMA; SIYWWGS; -.
DR   EvolutionaryTrace; P84153; -.
DR   Proteomes; UP000278666; Chromosome 1.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019646; P:aerobic electron transport chain; IEA:InterPro.
DR   CDD; cd01665; Cyt_c_Oxidase_III; 1.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 1.20.120.80; Cytochrome c oxidase, subunit III, four-helix bundle; 1.
DR   InterPro; IPR024791; Cyt_c/ubiquinol_Oxase_su3.
DR   InterPro; IPR033945; Cyt_c_oxase_su3_dom.
DR   InterPro; IPR000298; Cyt_c_oxidase-like_su3.
DR   InterPro; IPR035973; Cyt_c_oxidase_su3-like_sf.
DR   InterPro; IPR013833; Cyt_c_oxidase_su3_a-hlx.
DR   PANTHER; PTHR11403:SF7; CYTOCHROME C OXIDASE SUBUNIT 3; 1.
DR   PANTHER; PTHR11403; CYTOCHROME C OXIDASE SUBUNIT III; 1.
DR   Pfam; PF00510; COX3; 1.
DR   SUPFAM; SSF81452; Cytochrome c oxidase subunit III-like; 1.
DR   PROSITE; PS50253; COX3; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:1M56, ECO:0007829|PDB:1M57};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU003376};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        16..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        42..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        79..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        204..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        245..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          5..266
FT                   /note="Heme-copper oxidase subunit III family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50253"
SQ   SEQUENCE   266 AA;  30172 MW;  793C65EBBE051B35 CRC64;
     MAHAKNHDYH ILPPSIWPFM ASVGAFVMLF GAVLWMHGSG PWMGLIGLVV VLYTMFGWWS
     DVVTESLEGD HTPVVRLGLR WGFILFIMSE VMFFSAWFWS FFKHALYPMG PESPIIDGIF
     PPEGIITFDP WHLPLINTLI LLCSGCAATW AHHALVHENN RRDVAWGLAL AIALGALFTV
     FQAYEYSHAA FGFAGNIYGA NFFMATGFHG FHVIVGTIFL LVCLIRVQRG HFTPEKHVGF
     EAAIWYWHFV DVVWLFLFAS IYIWGQ
//