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P34957

- QOX2_BACSU

UniProt

P34957 - QOX2_BACSU

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Protein

Quinol oxidase subunit 2

Gene

qoxA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

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
Complete GO annotation...

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-KW
  3. respiratory chain Source: UniProtKB-KW
Complete GO annotation...

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.
InParanoidiP34957.
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

        10         20         30         40         50
MIFLFRALKP LLVLALLTVV FVLGGCSNAS VLDPKGPVAE QQSDLILLSI
60 70 80 90 100
GFMLFIVGVV FVLFTIILVK YRDRKGKDNG SYNPEIHGNT FLEVVWTVIP
110 120 130 140 150
ILIVIALSVP TVQTIYSLEK APEATKDKEP LVVYATSVDW KWVFSYPEQD
160 170 180 190 200
IETVNYLNIP VDRPILFKIS SADSMASLWI PQLGGQKYAM AGMLMDQYLQ
210 220 230 240 250
ADKVGTYEGR NANFTGEHFA DQEFDVNAVT EKDFNSWVKK TQNEAPKLTK
260 270 280 290 300
EKYDELMLPE NVDELTFSST HLKYVDHGQD AEYAMEARKR LGYQAVSPHS
310 320
KTDPFENVKK NEFKKSDDTE E
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.
InParanoidi P34957.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 125 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