Annotations: 9FUW

AMR Gene: CARD Annotation CARD Database Homepage

Chains	Accession	Short Name	Description	Provenance Source (Version)
A [auth B], B [auth A]	ARO:3003950	msbA	MsbA is a multidrug resistance transporter homolog from E. coli and belongs to a superfamily of transporters that contain an adenosine triphosphate (ATP) binding cassette (ABC) which is also called a nucleotide-binding domain (NBD). MsbA is a member of the MDR-ABC transporter group by sequence homology. MsbA transports lipid A, a major component of the bacterial outer cell membrane, and is the only bacterial ABC transporter that is essential for cell viability.	CARD (4.0.0)

AMR Gene Family: CARD Annotation CARD Database Homepage

Chains	Accession	Gene Family	Drug Class	Resistance Machanism	Provenance Source (Version)
A [auth B], B [auth A]	ARO:0010001	ATP-binding cassette (ABC) antibiotic efflux pump	nitroimidazole antibiotic	antibiotic efflux	CARD (4.0.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth B], B [auth A]	PF00664	ABC transporter transmembrane region (ABC_membrane)	ABC transporter transmembrane region	-	Family
A [auth B], B [auth A]	PF00005	ABC transporter (ABC_tran)	ABC transporter	ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are comp ...	ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain Pfam:PF00664. These four domains may belong to a single polypeptide as in Swiss:P13569, or belong in different polypeptide chains.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth B], B [auth A]	ATP-dependent lipid A-core flippase	xenobiotic transmembrane transporter activity ABC-type transporter activity active transmembrane transporter activity primary active transmembrane transporter activity ATPase-coupled transmembrane transporter activity ABC-type xenobiotic transporter activity transporter activity transmembrane transporter activity ATP-dependent activity binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding xenobiotic transmembrane transporter activity ABC-type transporter activity active transmembrane transporter activity primary active transmembrane transporter activity ATPase-coupled transmembrane transporter activity ABC-type xenobiotic transporter activity transporter activity transmembrane transporter activity ATP-dependent activity binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding lipid transporter activity lipid transmembrane transporter activity ATPase-coupled lipid transmembrane transporter activity lipid binding pyrophosphatase activity ATP hydrolysis activity ribonucleoside triphosphate phosphatase activity hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides hydrolase activity hydrolase activity, acting on acid anhydrides catalytic activity ATPase-coupled intramembrane lipid transporter activity intramembrane lipid transporter activity lipopolysaccharide floppase activity floppase activity identical protein binding protein binding	localization transport macromolecule localization lipid localization lipid transport establishment of localization lipopolysaccharide transport carbohydrate derivative transport membrane organization biological regulation lipid translocation regulation of membrane lipid distribution cellular component organization cellular process localization transport macromolecule localization lipid localization lipid transport establishment of localization lipopolysaccharide transport carbohydrate derivative transport membrane organization biological regulation lipid translocation regulation of membrane lipid distribution cellular component organization cellular process cellular component organization or biogenesis regulation of biological quality transmembrane transport	ATPase dependent transmembrane transport complex protein-containing complex plasma membrane protein complex membrane plasma membrane membrane protein complex transporter complex ATP-binding cassette (ABC) transporter complex cell periphery cellular anatomical structure transmembrane transporter complex MsbA transporter complex

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth B], B [auth A]	IPR017871	ABC transporter-like, conserved site	Conserved Site
A [auth B], B [auth A]	IPR003439	ABC transporter-like, ATP-binding domain	Domain
A [auth B], B [auth A]	IPR036640	ABC transporter type 1, transmembrane domain superfamily	Homologous Superfamily
A [auth B], B [auth A]	IPR011917	ABC transporter, lipid A-core flippase, MsbA	Family
A [auth B], B [auth A]	IPR003593	AAA+ ATPase domain	Domain
A [auth B], B [auth A]	IPR011527	ABC transporter type 1, transmembrane domain	Domain
A [auth B], B [auth A]	IPR039421	Type 1 protein exporter	Family
A [auth B], B [auth A]	IPR027417	P-loop containing nucleoside triphosphate hydrolase	Homologous Superfamily

Membrane Protein Annotation: PDBTM PDBTM Database Homepage

Chains	External Link	Comment
A [auth B], B [auth A]	PDBTM	Annotated as membrane protein by PDBTM

Membrane Protein Annotation: MemProtMD MemProtMD Database Homepage

Chains	External Link	Comment
A [auth B], B [auth A]	MemProtMD	Annotated as membrane protein by MemProtMD

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.