UniProt functional annotation for Q2EHL8



	UniProt functional annotation for Q2EHL8

UniProt code: Q2EHL8.

Organism: Aggregatibacter actinomycetemcomitans (Actinobacillus actinomycetemcomitans) (Haemophilus actinomycetemcomitans).

Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; Pasteurellaceae; Aggregatibacter.

Function: Part of the tripartite efflux system MacAB-TdeA. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides. {ECO:0000303|PubMed:19432486}.

Subunit: Homodimer. Part of the tripartite efflux system MacAB-TdeA, which is composed of an inner membrane transporter, MacB, a periplasmic membrane fusion protein, MacA, and an outer membrane component, TdeA. The complex forms a large protein conduit and can translocate molecules across both the inner and outer membranes. Interacts with MacA. {ECO:0000303|PubMed:19432486}.

Subcellular location: Cell inner membrane {ECO:0000255|HAMAP- Rule:MF_01720}; Multi-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_01720}.

Disruption phenotype: Mutation does not produce a noticeable phenotype or alter the drug resistance profile and the hemolytic activity of A.actinomycetemcomitans. {ECO:0000269|PubMed:17116373}.

Similarity: Belongs to the ABC transporter superfamily. Macrolide exporter (TC 3.A.1.122) family. {ECO:0000255|HAMAP-Rule:MF_01720}.

Sequence caution: Sequence=ABD38132.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.


Organism:		Aggregatibacter actinomycetemcomitans (Actinobacillus actinomycetemcomitans) (Haemophilus actinomycetemcomitans).
Taxonomy:		Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; Pasteurellaceae; Aggregatibacter.



Function:		Part of the tripartite efflux system MacAB-TdeA. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides. {ECO:0000303\|PubMed:19432486}.


Subunit:		Homodimer. Part of the tripartite efflux system MacAB-TdeA, which is composed of an inner membrane transporter, MacB, a periplasmic membrane fusion protein, MacA, and an outer membrane component, TdeA. The complex forms a large protein conduit and can translocate molecules across both the inner and outer membranes. Interacts with MacA. {ECO:0000303\|PubMed:19432486}.
Subcellular location:		Cell inner membrane {ECO:0000255\|HAMAP- Rule:MF_01720}; Multi-pass membrane protein {ECO:0000255\|HAMAP- Rule:MF_01720}.
Disruption phenotype:		Mutation does not produce a noticeable phenotype or alter the drug resistance profile and the hemolytic activity of A.actinomycetemcomitans. {ECO:0000269\|PubMed:17116373}.
Similarity:		Belongs to the ABC transporter superfamily. Macrolide exporter (TC 3.A.1.122) family. {ECO:0000255\|HAMAP-Rule:MF_01720}.
Sequence caution:		Sequence=ABD38132.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};