COX1_BACSU
ID COX1_BACSU Reviewed; 622 AA.
AC P24010; O34467;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 3.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Cytochrome c oxidase subunit 1;
DE EC=7.1.1.9;
DE AltName: Full=Caa-3605 subunit 1;
DE AltName: Full=Cytochrome aa3 subunit 1;
DE AltName: Full=Cytochrome c oxidase polypeptide I;
DE AltName: Full=Oxidase aa(3) subunit 1;
GN Name=ctaD; OrderedLocusNames=BSU14900;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=1847686; DOI=10.1111/j.1432-1033.1991.tb15732.x;
RA Saraste M., Metso T., Nakari T., Jalli T., Lauraeus M., van der Oost J.;
RT "The Bacillus subtilis cytochrome-c oxidase. Variations on a conserved
RT protein theme.";
RL Eur. J. Biochem. 195:517-525(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Bertero M., Presecan E., Glaser P., Richou A., Danchin A.;
RT "Bacillus subtilis chromosomal region downstream nprE.";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP SEQUENCE REVISION TO 120.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
CC -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory
CC chain that catalyzes the reduction of oxygen to water. Subunits 1-3
CC form the functional core of the enzyme complex. Co I is the catalytic
CC subunit of the enzyme. Electrons originating in cytochrome c are
CC transferred via the copper A center of subunit 2 and heme a of subunit
CC 1 to the bimetallic center formed by heme a3 and copper B. This
CC cytochrome c oxidase shows proton pump activity across the membrane in
CC addition to the electron transfer.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-
CC [cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436,
CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034; EC=7.1.1.9;
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Note=Binds 1 copper B ion per subunit.;
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Note=Binds 2 heme groups per subunit.;
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC {ECO:0000305}.
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DR EMBL; X54140; CAA38077.1; -; Genomic_DNA.
DR EMBL; Z98682; CAB11343.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13363.2; -; Genomic_DNA.
DR PIR; E69609; E69609.
DR RefSeq; NP_389373.2; NC_000964.3.
DR RefSeq; WP_003232245.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P24010; -.
DR SMR; P24010; -.
DR STRING; 224308.BSU14900; -.
DR TCDB; 3.D.4.4.1; the proton-translocating cytochrome oxidase (cox) superfamily.
DR PaxDb; P24010; -.
DR PRIDE; P24010; -.
DR EnsemblBacteria; CAB13363; CAB13363; BSU_14900.
DR GeneID; 936898; -.
DR KEGG; bsu:BSU14900; -.
DR PATRIC; fig|224308.179.peg.1625; -.
DR eggNOG; COG0843; Bacteria.
DR InParanoid; P24010; -.
DR OMA; PVDFQYH; -.
DR PhylomeDB; P24010; -.
DR BioCyc; BSUB:BSU14900-MON; -.
DR BioCyc; MetaCyc:BSU14900-MON; -.
DR SABIO-RK; P24010; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000001570; 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:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR GO; GO:0015990; P:electron transport coupled proton transport; IBA:GO_Central.
DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0022904; P:respiratory electron transport chain; IBA:GO_Central.
DR Gene3D; 1.20.210.10; -; 1.
DR InterPro; IPR023616; Cyt_c_oxase-like_su1_dom.
DR InterPro; IPR036927; Cyt_c_oxase-like_su1_sf.
DR InterPro; IPR000883; Cyt_C_Oxase_1.
DR InterPro; IPR023615; Cyt_c_Oxase_su1_BS.
DR InterPro; IPR014241; Cyt_c_oxidase_su1_bac.
DR PANTHER; PTHR10422; PTHR10422; 1.
DR Pfam; PF00115; COX1; 1.
DR PRINTS; PR01165; CYCOXIDASEI.
DR SUPFAM; SSF81442; SSF81442; 1.
DR TIGRFAMs; TIGR02891; CtaD_CoxA; 1.
DR PROSITE; PS50855; COX1; 1.
DR PROSITE; PS00077; COX1_CUB; 1.
PE 3: Inferred from homology;
KW Cell membrane; Copper; Electron transport; Heme; Hydrogen ion transport;
KW Ion transport; Iron; Membrane; Metal-binding; Reference proteome;
KW Respiratory chain; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..622
FT /note="Cytochrome c oxidase subunit 1"
FT /id="PRO_0000183436"
FT TOPO_DOM 1..27
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 28..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 47..68
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..110
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..159
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..196
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..241
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..284
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 305..312
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 332..346
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 367..374
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 395..421
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 422..441
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 442..459
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 460..479
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 480..552
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 553..572
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 573..580
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 581..604
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 605..622
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 73
FT /ligand="Fe(II)-heme a"
FT /ligand_id="ChEBI:CHEBI:61715"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305"
FT BINDING 249
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 253
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 298
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 299
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 384
FT /ligand="heme a3"
FT /ligand_id="ChEBI:CHEBI:83282"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305"
FT BINDING 386
FT /ligand="Fe(II)-heme a"
FT /ligand_id="ChEBI:CHEBI:61715"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305"
FT CROSSLNK 249..253
FT /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT /evidence="ECO:0000250"
FT CONFLICT 120
FT /note="G -> H (in Ref. 2; CAB11343)"
FT /evidence="ECO:0000305"
FT CONFLICT 155..156
FT /note="FV -> SI (in Ref. 1; CAA38077)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="Missing (in Ref. 1; CAA38077)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="A -> R (in Ref. 1; CAA38077)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 622 AA; 69028 MW; DF159F21D191332D CRC64;
MLNALTEKRT RGSMLWDYLT TVDHKKIAIL YLVAGGFFFL VGGIEAMFIR IQLAKPENAF
LSAQAYNEVM TMHGTTMIFL AAMPLLFALM NAVVPLQIGA RDVSFPFLNA LGFWLFFFGG
IFLNLSWFLG GAPDAGWTSY ASLSLHSKGH GIDFFVLGLQ ISGLGTLIAG INFLATIINM
RAPGMTYMRL PLFTWTTFVA SALILFAFPP LTVGLALMML DRLFGTNFFN PELGGNTVIW
EHLFWIFGHP EVYILILPAF GIFSEVIPVF ARKRLFGYSS MVFAIVLIGF LGFMVWVHHM
FTTGLGPIAN AIFAVATMAI AIPTGIKIFN WLLTIWGGNV KYTTAMLYAV SFIPSFVLGG
VTGVMLAAAA ADYQFHDTYF VVAHFHYVII GGVVFGLLAG VHFWWPKMFG KILHETMGKI
SFVLFFIGFH LTFFIQHFVG LMGMPRRVYT FLPGQGLETG NLISTIGAFF MAAAVILLLV
NVIWTSVKGE YVGADPWHDG RTLEWTVSSP PPEYNFKQLP FVRGLDPLWI EKQAGHKSMT
PAEPVDDIHM PNGSILPLII SFGLFVAAFG LLYRSDYAWG LPVIFIGLGI TFITMLLRSV
IDDHGYHIHK EELPNDDKGV KA
