Clusters of Characterized Proteins

Clustering the characterized proteins for opuBB (proline ABC transporter, fused permease and substrate-binding components OpuBB/BusAB) in L-proline catabolism

Or see other characterized proteins similar to opuBB

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Definition of opuBB

• Curated sequence Q93A34: BilEB aka OpuBB 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 Q9RQ05: BusAB aka OPUABC, 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
• Ignore hits to Q7DAU8 when looking for 'other' hits (ABC-type quaternary amine transporter (EC 7.6.2.9))
• Comment: Ignore a nearly-identical protein from L. lactis, annotated as a quarternary amine transporter

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 cluster

Lactococcus lactis

TC 3.A.1.12.5 / Q9RQ05 BusAB aka OPUABC, 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: BPD_transp_1, OpuAC
Heteromeric, 573 amino acids: PaperBLAST, CDD (Singleton 2)

Listeria monocytogenes

TC 3.A.1.12.8 / Q93A34 BilEB aka OpuBB 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: BPD_transp_1, OpuAC
Heteromeric, 504 amino acids: PaperBLAST, CDD (Singleton 1)