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P34957

- QOX2_BACSU

UniProt

P34957 - QOX2_BACSU

Protein

Quinol oxidase subunit 2

Gene

qoxA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 4 (16 Jun 2009)
      Previous versions | rss
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    Functioni

    Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. Major component for energy conversion during vegetative growth. Subunit II transfers the electrons from a quinol to the binuclear center of the catalytic subunit I By similarity.By similarity

    Catalytic activityi

    Ubiquinol-8 + O2 = Ubiquinone-8 + H2O.

    GO - Molecular functioni

    1. copper ion binding Source: InterPro
    2. cytochrome bo3 ubiquinol oxidase activity Source: InterPro
    3. cytochrome-c oxidase activity Source: InterPro
    4. cytochrome o ubiquinol oxidase activity Source: InterPro
    5. oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor Source: UniProtKB

    GO - Biological processi

    1. ATP synthesis coupled electron transport Source: UniProtKB
    2. mitochondrial electron transport, ubiquinol to cytochrome c Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Electron transport, Respiratory chain, Transport

    Enzyme and pathway databases

    BioCyciBSUB:BSU38170-MONOMER.
    MetaCyc:BSU38170-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Quinol oxidase subunit 2 (EC:1.10.3.-)
    Alternative name(s):
    Oxidase aa(3)-600 subunit 2
    Quinol oxidase aa3-600, subunit QoxA
    Quinol oxidase polypeptide II
    Gene namesi
    Name:qoxA
    Ordered Locus Names:BSU38170
    ORF Names:ipa-37d
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU38170. [Micado]

    Subcellular locationi

    Cell membrane PROSITE-ProRule annotation; Multi-pass membrane protein By similarity

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB-SubCell
    3. respiratory chain Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525PROSITE-ProRule annotationAdd
    BLAST
    Chaini26 – 321296Quinol oxidase subunit 2PRO_0000006069Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi26 – 261N-palmitoyl cysteinePROSITE-ProRule annotation
    Lipidationi26 – 261S-diacylglycerol cysteinePROSITE-ProRule annotation

    Keywords - PTMi

    Lipoprotein, Palmitate

    Proteomic databases

    PaxDbiP34957.

    Interactioni

    Protein-protein interaction databases

    STRINGi224308.BSU38170.

    Structurei

    3D structure databases

    ProteinModelPortaliP34957.
    SMRiP34957. Positions 30-271.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei49 – 6921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei90 – 11021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1622.
    HOGENOMiHOG000084157.
    KOiK02826.
    OrthoDBiEOG6PS5TJ.
    PhylomeDBiP34957.

    Family and domain databases

    Gene3Di1.10.287.90. 1 hit.
    2.60.40.420. 1 hit.
    InterProiIPR012141. Bo-type_Ubol_Oxase_su_II.
    IPR010514. COX_ARM.
    IPR008972. Cupredoxin.
    IPR002429. Cyt_c_oxidase_su2_C.
    IPR011759. Cyt_c_oxidase_su2_TM_dom.
    IPR006332. QoxA.
    [Graphical view]
    PfamiPF02790. COX2_TM. 1 hit.
    PF06481. COX_ARM. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000292. Ubi_od_II. 1 hit.
    SUPFAMiSSF49503. SSF49503. 1 hit.
    SSF81464. SSF81464. 1 hit.
    TIGRFAMsiTIGR01432. QOXA. 1 hit.
    PROSITEiPS50857. COX2_CUA. 1 hit.
    PS50999. COX2_TM. 1 hit.
    PS51257. PROKAR_LIPOPROTEIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P34957-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIFLFRALKP LLVLALLTVV FVLGGCSNAS VLDPKGPVAE QQSDLILLSI    50
    GFMLFIVGVV FVLFTIILVK YRDRKGKDNG SYNPEIHGNT FLEVVWTVIP 100
    ILIVIALSVP TVQTIYSLEK APEATKDKEP LVVYATSVDW KWVFSYPEQD 150
    IETVNYLNIP VDRPILFKIS SADSMASLWI PQLGGQKYAM AGMLMDQYLQ 200
    ADKVGTYEGR NANFTGEHFA DQEFDVNAVT EKDFNSWVKK TQNEAPKLTK 250
    EKYDELMLPE NVDELTFSST HLKYVDHGQD AEYAMEARKR LGYQAVSPHS 300
    KTDPFENVKK NEFKKSDDTE E 321
    Length:321
    Mass (Da):36,282
    Last modified:June 16, 2009 - v4
    Checksum:i6E4573332345DE7D
    GO

    Sequence cautioni

    The sequence AAA22686.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti38 – 381V → VD in AAA22686. (PubMed:1316894)Curated
    Sequence conflicti38 – 381V → VD in CAA51593. (PubMed:7934828)Curated
    Sequence conflicti167 – 1671F → C in AAA22686. (PubMed:1316894)Curated
    Sequence conflicti167 – 1671F → C in CAA51593. (PubMed:7934828)Curated
    Sequence conflicti300 – 3001S → C in AAA22686. (PubMed:1316894)Curated
    Sequence conflicti300 – 3001S → C in CAA51593. (PubMed:7934828)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M86548 Genomic DNA. Translation: AAA22686.1. Different initiation.
    X73124 Genomic DNA. Translation: CAA51593.1.
    AL009126 Genomic DNA. Translation: CAB15843.2.
    PIRiE69687.
    RefSeqiNP_391696.2. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB15843; CAB15843; BSU38170.
    GeneIDi937295.
    KEGGibsu:BSU38170.
    PATRICi18979678. VBIBacSub10457_4001.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M86548 Genomic DNA. Translation: AAA22686.1 . Different initiation.
    X73124 Genomic DNA. Translation: CAA51593.1 .
    AL009126 Genomic DNA. Translation: CAB15843.2 .
    PIRi E69687.
    RefSeqi NP_391696.2. NC_000964.3.

    3D structure databases

    ProteinModelPortali P34957.
    SMRi P34957. Positions 30-271.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU38170.

    Proteomic databases

    PaxDbi P34957.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB15843 ; CAB15843 ; BSU38170 .
    GeneIDi 937295.
    KEGGi bsu:BSU38170.
    PATRICi 18979678. VBIBacSub10457_4001.

    Organism-specific databases

    GenoListi BSU38170. [Micado ]

    Phylogenomic databases

    eggNOGi COG1622.
    HOGENOMi HOG000084157.
    KOi K02826.
    OrthoDBi EOG6PS5TJ.
    PhylomeDBi P34957.

    Enzyme and pathway databases

    BioCyci BSUB:BSU38170-MONOMER.
    MetaCyc:BSU38170-MONOMER.

    Family and domain databases

    Gene3Di 1.10.287.90. 1 hit.
    2.60.40.420. 1 hit.
    InterProi IPR012141. Bo-type_Ubol_Oxase_su_II.
    IPR010514. COX_ARM.
    IPR008972. Cupredoxin.
    IPR002429. Cyt_c_oxidase_su2_C.
    IPR011759. Cyt_c_oxidase_su2_TM_dom.
    IPR006332. QoxA.
    [Graphical view ]
    Pfami PF02790. COX2_TM. 1 hit.
    PF06481. COX_ARM. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000292. Ubi_od_II. 1 hit.
    SUPFAMi SSF49503. SSF49503. 1 hit.
    SSF81464. SSF81464. 1 hit.
    TIGRFAMsi TIGR01432. QOXA. 1 hit.
    PROSITEi PS50857. COX2_CUA. 1 hit.
    PS50999. COX2_TM. 1 hit.
    PS51257. PROKAR_LIPOPROTEIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning, sequencing, and physiological characterization of the qox operon from Bacillus subtilis encoding the aa3-600 quinol oxidase."
      Santana M., Kunst F., Hullo M.-F., Rapoport G., Danchin A., Glaser P.
      J. Biol. Chem. 267:10225-10231(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    2. 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.
      , 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.
    4. "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
      Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
      Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION TO 38; 167 AND 300.

    Entry informationi

    Entry nameiQOX2_BACSU
    AccessioniPrimary (citable) accession number: P34957
    Secondary accession number(s): O32281
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: June 16, 2009
    Last modified: October 1, 2014
    This is version 124 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3