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UniProtKB/Swiss-Prot entry P24010


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name COX1_BACSU
Primary accession number P24010
Secondary accession number O34467
Integrated into Swiss-Prot on March 1, 1992
Sequence was last modified on May 30, 2000 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 78)
Name and origin of the protein
Protein name Cytochrome c oxidase subunit 1
Synonyms EC 1.9.3.1
Cytochrome c oxidase polypeptide I
Cytochrome aa3 subunit 1
Caa-3605 subunit 1
Oxidase aa(3) subunit 1
Gene name
Name: ctaD
OrderedLocusNames: BSU14900
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=1847686 [NCBI, ExPASy, EBI, Israel, Japan]
Saraste M., Metso T., Nakari T., Jalli T., Lauraeus M., van der Oost J.;
"The Bacillus subtilis cytochrome-c oxidase. Variations on a conserved protein theme.";
Eur. J. Biochem. 195:517-525(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
Bertero M., Presecan E., Glaser P., Richou A., Danchin A.;
"Bacillus subtilis chromosomal region downstream nprE.";
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
DOI=10.1038/36786; PubMed=9384377 [NCBI, ExPASy, EBI, Israel, Japan]
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.";
Nature 390:249-256(1997).
Comments
  • FUNCTION: Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Co I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme a of subunit 1 to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer.
  • CATALYTIC ACTIVITY: 4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O.
  • COFACTOR: Binds 1 copper B ion per subunit.
  • COFACTOR: Binds 2 heme groups per subunit.
  • PATHWAY: Energy metabolism; oxidative phosphorylation.
  • SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
  • SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X54140; CAA38077.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z98682; CAB11343.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99111; CAB13363.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR E69609; E69609.
RefSeq NP_389373.1; -.
3D structure databases
HSSP P18401; 1FFT. [HSSP ENTRY / PDB]
ModBase P24010.
Enzyme and pathway databases
BioCyc BSUB224308:BSU1492-MON; -.
Organism-specific databases
SubtiList BG10216; ctaD. [Micado]
Ontologies
GO
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from InterPro).
GO:0005746; Cellular component: mitochondrial respiratory chain (inferred from electronic annotation from UniProtKB-KW).
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005507; Molecular function: copper ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004129; Molecular function: cytochrome-c oxidase activity (inferred from electronic annotation from InterPro).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0020037; Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0009060; Biological process: aerobic respiration (inferred from electronic annotation from InterPro).
GO:0022900; Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0015992; Biological process: proton transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000883; COX1.
IPR014241; COX1_bac-type.
Graphical view of domain structure.
Gene3D G3DSA:1.20.210.10; COX1; 1.
PANTHER PTHR10422; COX1; 1.
Pfam PF00115; COX1; 1.
Pfam graphical view of domain structure.
PRINTS PR01165; CYCOXIDASEI.
TIGRFAMs TIGR02891; CtaD_CoxA; 1.
PROSITE PS50855; COX1; 1.
PS00077; COX1_CUB; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet P24010.
Genome annotation databases
GeneID 936898; -.
GenomeReviews AL009126_GR; BSU14900.
KEGG bsu:BSU14900; -.
NMPDR fig|224308.1.peg.1492; -.
Phylogenomic databases
HOGENOM P24010; -.
Genome annotation databases
CMR P24010; BSU14900.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cell membrane; Complete proteome; Copper; Electron transport; Heme; Hydrogen ion transport; Ion transport; Iron; Membrane; Metal-binding; Oxidoreductase; Respiratory chain; Transmembrane; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   622  622     Cytochrome c oxidase subunit 1. PRO_0000183436
TOPO_DOM   1    27  27     Extracellular (Potential). 
TRANSMEM   28    46  19     Potential. 
TOPO_DOM   47    68  22     Cytoplasmic (Potential). 
TRANSMEM   69    88  20     Potential. 
TOPO_DOM   89   110  22     Extracellular (Potential). 
TRANSMEM   111   128  18     Potential. 
TOPO_DOM   129   159  31     Cytoplasmic (Potential). 
TRANSMEM   160   178  19     Potential. 
TOPO_DOM   179   196  18     Extracellular (Potential). 
TRANSMEM   197   215  19     Potential. 
TOPO_DOM   216   241  26     Cytoplasmic (Potential). 
TRANSMEM   242   261  20     Potential. 
TOPO_DOM   262   284  23     Extracellular (Potential). 
TRANSMEM   285   304  20     Potential. 
TOPO_DOM   305   312  8     Cytoplasmic (Potential). 
TRANSMEM   313   331  19     Potential. 
TOPO_DOM   332   346  15     Extracellular (Potential). 
TRANSMEM   347   366  20     Potential. 
TOPO_DOM   367   374  8     Cytoplasmic (Potential). 
TRANSMEM   375   394  20     Potential. 
TOPO_DOM   395   421  27     Extracellular (Potential). 
TRANSMEM   422   441  20     Potential. 
TOPO_DOM   442   459  18     Cytoplasmic (Potential). 
TRANSMEM   460   479  20     Potential. 
TOPO_DOM   480   552  73     Extracellular (Potential). 
TRANSMEM   553   572  20     Potential. 
TOPO_DOM   573   580  8     Cytoplasmic (Potential). 
TRANSMEM   581   604  24     Potential. 
TOPO_DOM   605   622  18     Cytoplasmic (Potential). 
METAL   73    73        Iron (heme A axial ligand) (Probable). 
METAL   249   249        Copper B (Probable). 
METAL   253   253        Copper B (Probable). 
METAL   298   298        Copper B (Probable). 
METAL   299   299        Copper B (Probable). 
METAL   384   384        Iron (heme A3 axial ligand) (Probable). 
METAL   386   386        Iron (heme A axial ligand) (Probable). 
CROSSLNK   249   253        1'-histidyl-3'-tyrosine (His-Tyr) (By similarity). 
CONFLICT   120   120        H -> G (in Ref. 1; CAA38077). 
CONFLICT   155   156        FV -> SI (in Ref. 1; CAA38077). 
CONFLICT   288   288        Missing (in Ref. 1; CAA38077). 
CONFLICT   474   474        A -> R (in Ref. 1; CAA38077). 
Sequence information
Length: 622 AA [This is the length of the unprocessed precursor] Molecular weight: 69108 Da [This is the MW of the unprocessed precursor] CRC64: 80159F21D1913068 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLNALTEKRT RGSMLWDYLT TVDHKKIAIL YLVAGGFFFL VGGIEAMFIR IQLAKPENAF 

        70         80         90        100        110        120 
LSAQAYNEVM TMHGTTMIFL AAMPLLFALM NAVVPLQIGA RDVSFPFLNA LGFWLFFFGH 

       130        140        150        160        170        180 
IFLNLSWFLG GAPDAGWTSY ASLSLHSKGH GIDFFVLGLQ ISGLGTLIAG INFLATIINM 

       190        200        210        220        230        240 
RAPGMTYMRL PLFTWTTFVA SALILFAFPP LTVGLALMML DRLFGTNFFN PELGGNTVIW 

       250        260        270        280        290        300 
EHLFWIFGHP EVYILILPAF GIFSEVIPVF ARKRLFGYSS MVFAIVLIGF LGFMVWVHHM 

       310        320        330        340        350        360 
FTTGLGPIAN AIFAVATMAI AIPTGIKIFN WLLTIWGGNV KYTTAMLYAV SFIPSFVLGG 

       370        380        390        400        410        420 
VTGVMLAAAA ADYQFHDTYF VVAHFHYVII GGVVFGLLAG VHFWWPKMFG KILHETMGKI 

       430        440        450        460        470        480 
SFVLFFIGFH LTFFIQHFVG LMGMPRRVYT FLPGQGLETG NLISTIGAFF MAAAVILLLV 

       490        500        510        520        530        540 
NVIWTSVKGE YVGADPWHDG RTLEWTVSSP PPEYNFKQLP FVRGLDPLWI EKQAGHKSMT 

       550        560        570        580        590        600 
PAEPVDDIHM PNGSILPLII SFGLFVAAFG LLYRSDYAWG LPVIFIGLGI TFITMLLRSV 

       610        620 
IDDHGYHIHK EELPNDDKGV KA 

P24010 in FASTA format

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