QOX2_BACSU
ID QOX2_BACSU Reviewed; 321 AA.
AC P34957; O32281;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 4.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Quinol oxidase subunit 2;
DE EC=1.10.3.-;
DE AltName: Full=Oxidase aa(3)-600 subunit 2;
DE AltName: Full=Quinol oxidase aa3-600, subunit QoxA;
DE AltName: Full=Quinol oxidase polypeptide II;
DE Flags: Precursor;
GN Name=qoxA; OrderedLocusNames=BSU38170; ORFNames=ipa-37d;
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=1316894; DOI=10.1016/s0021-9258(19)50007-2;
RA Santana M., Kunst F., Hullo M.-F., Rapoport G., Danchin A., Glaser P.;
RT "Molecular cloning, sequencing, and physiological characterization of the
RT qox operon from Bacillus subtilis encoding the aa3-600 quinol oxidase.";
RL J. Biol. Chem. 267:10225-10231(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7934828; DOI=10.1111/j.1365-2958.1993.tb01963.x;
RA Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F.,
RA Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E.,
RA Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.;
RT "Bacillus subtilis genome project: cloning and sequencing of the 97 kb
RT region from 325 degrees to 333 degrees.";
RL Mol. Microbiol. 10:371-384(1993).
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 38; 167 AND 300.
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).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=22882210; DOI=10.1111/j.1365-2958.2012.08205.x;
RA Yepes A., Schneider J., Mielich B., Koch G., Garcia-Betancur J.C.,
RA Ramamurthi K.S., Vlamakis H., Lopez D.;
RT "The biofilm formation defect of a Bacillus subtilis flotillin-defective
RT mutant involves the protease FtsH.";
RL Mol. Microbiol. 86:457-471(2012).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH FLOT, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=168;
RX PubMed=23651456; DOI=10.1111/mmi.12252;
RA Bach J.N., Bramkamp M.;
RT "Flotillins functionally organize the bacterial membrane.";
RL Mol. Microbiol. 88:1205-1217(2013).
CC -!- FUNCTION: Catalyzes quinol oxidation with the concomitant reduction of
CC oxygen to water. Major component for energy conversion during
CC vegetative growth. Subunit II transfers the electrons from a quinol to
CC the binuclear center of the catalytic subunit I (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a quinol + O2 = 2 a quinone + 2 H2O; Xref=Rhea:RHEA:55376,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:132124;
CC -!- SUBUNIT: Interacts with FloT. {ECO:0000269|PubMed:23651456}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303, ECO:0000269|PubMed:22882210,
CC ECO:0000269|PubMed:23651456}; Multi-pass membrane protein
CC {ECO:0000255}. Membrane raft {ECO:0000269|PubMed:22882210,
CC ECO:0000269|PubMed:23651456}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Present in detergent-resistant membrane (DRM)
CC fractions that may be equivalent to eukaryotic membrane rafts; these
CC rafts include proteins involved in signaling, molecule trafficking and
CC protein secretion. {ECO:0000269|PubMed:22882210,
CC ECO:0000269|PubMed:23651456}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA22686.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M86548; AAA22686.1; ALT_INIT; Genomic_DNA.
DR EMBL; X73124; CAA51593.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15843.2; -; Genomic_DNA.
DR PIR; E69687; E69687.
DR RefSeq; NP_391696.2; NC_000964.3.
DR RefSeq; WP_010886637.1; NZ_JNCM01000034.1.
DR PDB; 6KOB; X-ray; 3.60 A; B/F=26-321.
DR PDB; 6KOC; X-ray; 3.80 A; B/F=26-321.
DR PDB; 6KOE; X-ray; 3.75 A; B/F=26-321.
DR PDBsum; 6KOB; -.
DR PDBsum; 6KOC; -.
DR PDBsum; 6KOE; -.
DR AlphaFoldDB; P34957; -.
DR SMR; P34957; -.
DR STRING; 224308.BSU38170; -.
DR jPOST; P34957; -.
DR PaxDb; P34957; -.
DR PRIDE; P34957; -.
DR EnsemblBacteria; CAB15843; CAB15843; BSU_38170.
DR GeneID; 937295; -.
DR KEGG; bsu:BSU38170; -.
DR PATRIC; fig|224308.43.peg.4001; -.
DR eggNOG; COG1622; Bacteria.
DR InParanoid; P34957; -.
DR OMA; TAMNSFF; -.
DR PhylomeDB; P34957; -.
DR BioCyc; BSUB:BSU38170-MON; -.
DR BioCyc; MetaCyc:BSU38170-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0009486; F:cytochrome bo3 ubiquinol oxidase activity; IEA:InterPro.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR GO; GO:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; ISS:UniProtKB.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; ISS:UniProtKB.
DR CDD; cd04212; CuRO_UO_II; 1.
DR Gene3D; 1.10.287.90; -; 1.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR045187; CcO_II.
DR InterPro; IPR002429; CcO_II-like_C.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR034227; CuRO_UO_II.
DR InterPro; IPR011759; Cyt_c_oxidase_su2_TM_dom.
DR InterPro; IPR036257; Cyt_c_oxidase_su2_TM_sf.
DR InterPro; IPR006333; Cyt_o_ubiquinol_oxidase_su2.
DR InterPro; IPR006332; QoxA.
DR PANTHER; PTHR22888; PTHR22888; 1.
DR Pfam; PF00116; COX2; 1.
DR Pfam; PF02790; COX2_TM; 1.
DR PIRSF; PIRSF000292; Ubi_od_II; 1.
DR SUPFAM; SSF49503; SSF49503; 1.
DR SUPFAM; SSF81464; SSF81464; 1.
DR TIGRFAMs; TIGR01432; QOXA; 1.
DR PROSITE; PS50857; COX2_CUA; 1.
DR PROSITE; PS50999; COX2_TM; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Electron transport; Lipoprotein; Membrane;
KW Oxidoreductase; Palmitate; Reference proteome; Respiratory chain; Signal;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 26..321
FT /note="Quinol oxidase subunit 2"
FT /id="PRO_0000006069"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 294..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 26
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 26
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CONFLICT 38
FT /note="V -> VD (in Ref. 1; AAA22686 and 2; CAA51593)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="F -> C (in Ref. 1; AAA22686 and 2; CAA51593)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="S -> C (in Ref. 1; AAA22686 and 2; CAA51593)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 321 AA; 36282 MW; 6E4573332345DE7D CRC64;
MIFLFRALKP LLVLALLTVV FVLGGCSNAS VLDPKGPVAE QQSDLILLSI GFMLFIVGVV
FVLFTIILVK YRDRKGKDNG SYNPEIHGNT FLEVVWTVIP ILIVIALSVP TVQTIYSLEK
APEATKDKEP LVVYATSVDW KWVFSYPEQD IETVNYLNIP VDRPILFKIS SADSMASLWI
PQLGGQKYAM AGMLMDQYLQ ADKVGTYEGR NANFTGEHFA DQEFDVNAVT EKDFNSWVKK
TQNEAPKLTK EKYDELMLPE NVDELTFSST HLKYVDHGQD AEYAMEARKR LGYQAVSPHS
KTDPFENVKK NEFKKSDDTE E
