Clusters of Characterized Proteins

Clustering the characterized proteins for opuBA (proline ABC transporter, ATPase component OpuBA/BusAA) in L-proline catabolism

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Definition of opuBA

• Curated sequence Q93A35: BilEA aka OpuBA protein, component of A proline/glycine betaine uptake system. Also reported to be a bile exclusion system that exports oxgall and other bile compounds, BilEA/EB or OpuBA/BB (required for normal virulence)
• Curated sequence Q9RQ06: BusAA, component of Uptake system for glycine-betaine (high affinity) and proline (low affinity) (OpuAA-OpuABC) or BusAA-ABC of Lactococcus lactis). BusAA, the ATPase subunit, has a C-terminal tandem cystathionine β-synthase (CBS) domain which is the cytoplasmic K+ sensor for osmotic stress (osmotic strength)while the BusABC subunit has the membrane and receptor domains fused to each other (Biemans-Oldehinkel et al., 2006; Mahmood et al., 2006; Gul et al. 2012). An N-terminal amphipathic α-helix of OpuA is necessary for high activity but is not critical for biogenesis or the ionic regulation of transport
• Comment: In Listeria monocytogenes and in Lactococcus lactis, the permease is fused to the substrate-binding component.

Fetched 2 sequences

Running BLASTp

Found similarities, at above 30% identity and 75% coverage, for 0 of these sequences

Found 0 clusters of similar sequences. Another 2 sequences are not clustered. Download as table or as draft rules or view by organism

Singletons (2/2 heteromeric)

TC 3.A.1.12.8 / Q93A35 BilEA aka OpuBA protein, component of A proline/glycine betaine uptake system. Also reported to be a bile exclusion system that exports oxgall and other bile compounds, BilEA/EB or OpuBA/BB (required for normal virulence) from Listeria monocytogenes
PFams: ABC_tran
Heteromeric, 328 amino acids: PaperBLAST, CDD

TC 3.A.1.12.5 / Q9RQ06 BusAA, component of Uptake system for glycine-betaine (high affinity) and proline (low affinity) (OpuAA-OpuABC) or BusAA-ABC of Lactococcus lactis). BusAA, the ATPase subunit, has a C-terminal tandem cystathionine β-synthase (CBS) domain which is the cytoplasmic K+ sensor for osmotic stress (osmotic strength)while the BusABC subunit has the membrane and receptor domains fused to each other (Biemans-Oldehinkel et al., 2006; Mahmood et al., 2006; Gul et al. 2012). An N-terminal amphipathic α-helix of OpuA is necessary for high activity but is not critical for biogenesis or the ionic regulation of transport from Lactococcus lactis
PFams: ABC_tran, CBS
Heteromeric, 407 amino acids: PaperBLAST, CDD