Annotations: 4DK0

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	HlyD_D23_C	e4dk0A3	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: Alanine racemase-C	F: HlyD_D23_C	ECOD (1.6)
A	8a0102	e4dk0A4	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: Alanine racemase-C	F: 8a0102	ECOD (1.6)
A	HlyD_1st_2	e4dk0A2	A: alpha bundles	X: helical hairpin of HlyD-like secretion proteins (From Topology)	H: helical hairpin of HlyD-like secretion proteins (From Topology)	T: helical hairpin of HlyD-like secretion proteins	F: HlyD_1st_2	ECOD (1.6)
A	Biotin_lipoyl_1	e4dk0A1	A: a+b complex topology	X: alpha/beta-Hammerhead/Barrel-sandwich hybrid	H: alpha/beta-Hammerhead/Barrel-sandwich hybrid	T: Single hybrid motif	F: Biotin_lipoyl_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.40.420.20	Mainly Beta	Beta Barrel	conserved putative lor/sdh protein from methanococcus maripaludis s2 fold		CATH (4.3.0)
A	2.40.30.170	Mainly Beta	Beta Barrel	Elongation Factor Tu (Ef-tu)	domain 3	CATH (4.3.0)
A	2.40.50.100	Mainly Beta	Beta Barrel	OB fold (Dihydrolipoamide Acetyltransferase, E2P)	RNA polymerase II/Efflux pump adaptor protein, barrel-sandwich hybrid domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF16576	Barrel-sandwich domain of CusB or HlyD membrane-fusion (HlyD_D23)	Barrel-sandwich domain of CusB or HlyD membrane-fusion	HlyD_D23 is the combined domains 2 and 3 of the membrane-fusion proteins CusB and HlyD, which forms a barrel-sandwich. CusB and HlyD proteins are membrane fusion proteins of the CusCFBA copper efflux system in E.coli and related bacteria. The whole ...	HlyD_D23 is the combined domains 2 and 3 of the membrane-fusion proteins CusB and HlyD, which forms a barrel-sandwich. CusB and HlyD proteins are membrane fusion proteins of the CusCFBA copper efflux system in E.coli and related bacteria. The whole molecule hinges between D2 and D3. Efflux systems of this resistance-nodulation-division group - RND - have been developed to excrete poisonous metal ions, and in E.coli the only one that deals with silver and copper is the CusA transporter. The transporter CusA works in conjunction with a periplasmic component that is a membrane fusion protein, eg CusB, and an outer-membrane channel component CusC in a CusABC complex driven by import of protons.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Putative MacA	efflux transmembrane transporter activity transporter activity transmembrane transporter activity identical protein binding protein binding binding	xenobiotic export from cell xenobiotic transport response to stimulus xenobiotic detoxification by transmembrane export across the plasma membrane transport detoxification export from cell export across plasma membrane establishment of localization response to toxic substance transmembrane transport localization response to chemical cellular process	protein-containing complex cellular anatomical structure efflux pump complex transmembrane transporter complex membrane membrane protein complex transporter complex extrinsic component of membrane macrolide transmembrane transporter complex

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR030190	Macrolide export protein MacA, alpha-hairpin domain superfamily	Homologous Superfamily
A	IPR006143	RND efflux pump, membrane fusion protein	Family
A	IPR032317	RND efflux pump, membrane fusion protein, barrel-sandwich domain	Domain

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.