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P24012 (COX3_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytochrome c oxidase subunit 3
EC=1.9.3.1
Alternative name(s):
Caa-3605 subunit 3
Cytochrome aa3 subunit 3
Cytochrome c oxidase polypeptide III
Oxidase aa(3) subunit 3
Gene names
Name:ctaE
Ordered Locus Names:BSU14910
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length207 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O.

Subcellular location

Cell membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the cytochrome c oxidase subunit 3 family.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaerobic electron transport chain

Inferred from electronic annotation. Source: InterPro

   Cellular_componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncytochrome-c oxidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 207207Cytochrome c oxidase subunit 3
PRO_0000183877

Regions

Transmembrane30 – 5021Helical; Potential
Transmembrane67 – 8721Helical; Potential
Transmembrane101 – 12121Helical; Potential
Transmembrane144 – 16421Helical; Potential
Transmembrane186 – 20621Helical; Potential

Experimental info

Sequence conflict261K → N in CAA38078. Ref.1
Sequence conflict51 – 522LR → AS in CAA38078. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P24012 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 9357E3DDAB137F12

FASTA20723,266
        10         20         30         40         50         60 
MQVQEKFTAE TFPASPEKVT LEGKNKFLGF WLFLGGETVL FASLFATFLA LRNSNAGDPP 

        70         80         90        100        110        120 
TTEMFDVTLV FIATMLLLTS SLTSVYAMYH MKNFSFGKMQ LWLGITILLG AGFLGLEIYE 

       130        140        150        160        170        180 
FKHYTHEFGF TITSSALGSA FYTLVGTHGA HVAFGLMWIS TLMIRNAKRG LNLYTAPKFY 

       190        200 
VASLYWHFID VVWVFIFTVV YLMGMVG

« Hide

References

« Hide 'large scale' references
[1]"The Bacillus subtilis cytochrome-c oxidase. Variations on a conserved protein theme."
Saraste M., Metso T., Nakari T., Jalli T., Lauraeus M., van der Oost J.
Eur. J. Biochem. 195:517-525(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"Bacillus subtilis chromosomal region downstream nprE."
Bertero M., Presecan E., Glaser P., Richou A., Danchin A.
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[3]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
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. expand/collapse author list , 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.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X54140 Genomic DNA. Translation: CAA38078.1.
Z98682 Genomic DNA. Translation: CAB11344.1.
AL009126 Genomic DNA. Translation: CAB13364.1.
PIRF69609.
RefSeqNP_389374.1. NC_000964.3.

3D structure databases

ProteinModelPortalP24012.
SMRP24012. Positions 20-205.
ModBaseSearch...

Protein-protein interaction databases

STRING224308.BSU14910.

Protein family/group databases

TCDB3.D.4.4.1. proton-translocating cytochrome oxidase (COX) superfamily.

Proteomic databases

PaxDbP24012.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB13364; CAB13364; BSU14910.
GeneID935993.
KEGGbsu:BSU14910.
PATRIC18974783. VBIBacSub10457_1583.

Organism-specific databases

GenoListBSU14910. [Micado]

Phylogenomic databases

eggNOGCOG1845.
HOGENOMHOG000086398.
KOK02276.
OMATFPASPE.
ProtClustDBCLSK873365.

Enzyme and pathway databases

BioCycBSUB:BSU14910-MONOMER.

Family and domain databases

Gene3D1.20.120.80. 1 hit.
InterProIPR024791. Cyt_c/ubiquinol_Oxase_su3.
IPR000298. Cyt_c_oxidase_su3.
IPR013833. Cyt_c_oxidase_su3_a-hlx.
[Graphical view]
PANTHERPTHR11403. PTHR11403. 1 hit.
PfamPF00510. COX3. 1 hit.
[Graphical view]
SUPFAMSSF81452. CytC_oxdse_III. 1 hit.
PROSITEPS50253. COX3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOX3_BACSU
AccessionPrimary (citable) accession number: P24012
Secondary accession number(s): O34333
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: May 30, 2000
Last modified: May 1, 2013
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents