General information | DisProt: | DP00089 | Name: | Ubiquinol oxidase subunit 2 | Synonym(s): | CYOA_ECOLI
Ubiquinol oxidase polypeptide II
Cytochrome o subunit 2
Oxidase BO(3) subunit 2
Cytochrome o ubiquinol oxidase subunit 2
Ubiquinol oxidase chain B
| First appeared in release: | Release 1.0 (08/01/2003) | UniProt: | P0ABJ1 | UniGene: | | SwissProt: | CYOA_ECOLI | TrEMBL: | | NCBI (GI): | 78099990 | Source organism: | Escherichia coli (strain K12) | Sequence length: | 315 | Percent disordered: | 19% | Homologues: | |
Native sequence |
10 20 30 40 50 60 | | | | | | MRLRKYNKSL GWLSLFAGTV LLSGCNSALL DPKGQIGLEQ RSLILTAFGL MLIVVIPAIL - 60 MAVGFAWKYR ASNKDAKYSP NWSHSNKVEA VVWTVPILII IFLAVLTWKT THALEPSKPL - 120 AHDEKPITIE VVSMDWKWFF IYPEQGIATV NEIAFPANTP VYFKVTSNSV MNSFFIPRLG - 180 SQIYAMAGMQ TRLHLIANEP GTYDGISASY SGPGFSGMKF KAIATPDRAA FDQWVAKAKQ - 240 SPNTMSDMAA FEKLAAPSEY NQVEYFSNVK PDLFADVINK FMAHGKSMDM TQPEGEHSAH - 300 EGMEGMDMSH AESAH
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Functional narrative |
Ubiquinol oxidase polypeptide II is a protein that is one of four subunits. The protein complex catalyzes oxygen reduction into water and uses available free energy to drive a proton gradient across the membrane in the aerobic respiratory chain of E. coli. It belongs to the heme-copper oxidase superfamily of enzymes and the cytochrome c oxidase subunit 2 family. It is a heteroctamer of two A chains, two B chains, two C chains and two D chains. The C-terminal extrinsic domain of subunit II has been proposed to contain a ubiquinone binding site at its interface with subunit I.
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Map of ordered and disordered regions |


Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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Region 1 | Type: | Disordered | Name: | | Location: | 1 - 26 | Length: | 26 | Region sequence: |
MRLRKYNKSLGWLSLFAGTVLLSGCN | Modification type: | Engineered
| PDB: | 1FFT:B, 1FFT:G | Structural/functional type: | Relationship to function unknown | Functional classes: | Unknown
| Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (PEG 1500 (approximate (w/v)) 9 %; sodium chloride 100 mM; magnesium chloride 100 mM; ethanol ((v/v)) 5 %)
| References:
- Abramson J, Riistama S, Larsson G, Jasaitis A, Svensson-Ek M, Laakkonen L, Puustinen A, Iwata S, Wikstrom M. "The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site." Nat Struct Biol. 2000; 7(10): 910-7. PubMed: 11017202
| Comments:This region is located in the periplasmic space.
Abramson et al. could not assign a sequence for residues 1-36 or 113-124. However the PDB file locates electron density for residues 27-283.
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Region 2 | Type: | Disordered | Name: | | Location: | 284 - 315 | Length: | 32 | Region sequence: |
HGKSMDMTQPEGEHSAHEGMEGMDMSHAESAH | Modification type: | Engineered
| PDB: | 1FFT:B, 1FFT:G | Structural/functional type: | Relationship to function unknown | Functional classes: | Unknown
| Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (ethanol ((v/v)) 5 %; magnesium chloride 100 mM; PEG 1500 (approximate (w/v)) 9 %; sodium chloride 100 mM)
| References:
- Abramson J, Riistama S, Larsson G, Jasaitis A, Svensson-Ek M, Laakkonen L, Puustinen A, Iwata S, Wikstrom M. "The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site." Nat Struct Biol. 2000; 7(10): 910-7. PubMed: 11017202
| Comments:This region is located in the periplasmic space.
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Region 3 | Type: | Disordered | Name: | | Location: | 1 - 14 | Length: | 14 | Region sequence: |
MRLRKYNKSLGWLS | Modification type: | Fragment
| PDB: | 1FFT:B, 1FFT:G | Structural/functional type: | Relationship to function unknown | Functional classes: | Unknown
| Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (277 K; ammonium sulfate (precipitant) 35 %; citrate/bis-Tris-propane ((pH 9.0-9.5)) 100 mM; dimethylsulphoxide ((to obtain sharp edges) v/v) 2 %; DTT (buffer) 1 mM; EDTA (buffer) 1 mM; NaN3 (buffer) 1 mM)
| References:
- van der Oost J, Lappalainen P, Musacchio A, Warne A, Lemieux L, Rumbley J, Gennis RB, Aasa R, Pascher T, Malmstrom BG, et al. "Restoration of a lost metal-binding site: construction of two different copper sites into a subunit of the E. coli cytochrome o quinol oxidase complex." Embo J. 1992; 11(9): 3209-17. PubMed: 1324168
- van der Oost J, Musacchio A, Pauptit RA, Ceska TA, Wierenga RK, Saraste M. "Crystallization and preliminary X-ray analysis of the periplasmic fragment of CyoA-a subunit of the Escherichia coli cytochrome o complex." J Mol Biol. 1993; 229(3): 794-6. PubMed: 8433374
- Wilmanns M, Lappalainen P, Kelly M, Sauer-Eriksson E, Saraste M. "Crystal structure of the membrane-exposed domain from a respiratory quinol oxidase complex with an engineered dinuclear copper center." Proc Natl Acad Sci U S A. 1995; 92(26): 11955-9. PubMed: 8618822
| Comments:This region is located in the periplasmic space.
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Region 4 | Type: | Disordered | Name: | | Location: | 283 - 315 | Length: | 33 | Region sequence: |
AHGKSMDMTQPEGEHSAHEGMEGMDMSHAESAH | Modification type: | Fragment
| PDB: | 1FFT:B, 1FFT:G | Structural/functional type: | Relationship to function unknown | Functional classes: | Unknown
| Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (277 K; ammonium sulfphate (precipitant) 35 %; citrate/bis-Tris-propane ((pH 9.0-9.5)) 100 mM; dimethylsuphoxide ((to obtain sharp edges) v/v) 2 %; DTT (buffer) 1 mM; EDTA (buffer) 1 mM; NaN3 (buffer) 1 mM)
| References:
- van der Oost J, Lappalainen P, Musacchio A, Warne A, Lemieux L, Rumbley J, Gennis RB, Aasa R, Pascher T, Malmstrom BG, et al. "Restoration of a lost metal-binding site: construction of two different copper sites into a subunit of the E. coli cytochrome o quinol oxidase complex." Embo J. 1992; 11(9): 3209-17. PubMed: 1324168
- van der Oost J, Musacchio A, Pauptit RA, Ceska TA, Wierenga RK, Saraste M. "Crystallization and preliminary X-ray analysis of the periplasmic fragment of CyoA-a subunit of the Escherichia coli cytochrome o complex." J Mol Biol. 1993; 229(3): 794-6. PubMed: 8433374
- Wilmanns M, Lappalainen P, Kelly M, Sauer-Eriksson E, Saraste M. "Crystal structure of the membrane-exposed domain from a respiratory quinol oxidase complex with an engineered dinuclear copper center." Proc Natl Acad Sci U S A. 1995; 92(26): 11955-9. PubMed: 8618822
| Comments:This region is located in the periplasmic space.
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References |
- Chepuri V, Lemieux L, Au DC, Gennis RB. "The sequence of the cyo operon indicates substantial structural similarities between the cytochrome o ubiquinol oxidase of Escherichia coli and the aa3-type family of cytochrome c oxidases." J Biol Chem. 1990; 265(19): 11185-92. PubMed: 2162835
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Comments |
A periplasmic fragment of subunit II is located under the PDB identification of 1CYW. It is residues 125-283 of subunit II as described by Abramson et. al.
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