2KXX | pdb_00002kxx

NMR Structure of Escherichia coli BamE, a Lipoprotein Component of the beta-Barrel Assembly Machinery Complex

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	BLIP repeat-like	8092082	3000321	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	SmpA_OmlA	e2kxxA1	A: a+b two layers	X: BLIP-like	H: beta-lactamase-inhibitor protein, BLIP (From Topology)	T: beta-lactamase-inhibitor protein, BLIP	F: SmpA_OmlA	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.1450.10	Alpha Beta	2-Layer Sandwich	Beta-lactamase Inhibitory Protein	Chain:B, domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF04355	Outer membrane protein assembly factor BamE domain (BamE)	Outer membrane protein assembly factor BamE domain	This domain is found in bacterial outer membrane lipoproteins probably involved in maintaining the structural integrity of the cell envelope [1], including Outer membrane protein assembly factor BamE from Vibrio cholerae (also known as SmpA). The lip ...	This domain is found in bacterial outer membrane lipoproteins probably involved in maintaining the structural integrity of the cell envelope [1], including Outer membrane protein assembly factor BamE from Vibrio cholerae (also known as SmpA). The lipid attachment site is a conserved N terminal cysteine residue. Sometimes found adjacent to the OmpA domain (Pfam:PF00691).	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Small protein A	protein-macromolecule adaptor activity molecular adaptor activity identical protein binding protein binding binding	membrane organization membrane biogenesis membrane assembly cellular component organization cellular component biogenesis cellular component assembly cellular process cellular component organization or biogenesis cell envelope organization Gram-negative-bacterium-type cell outer membrane assembly external encapsulating structure organization protein localization cellular localization establishment of protein localization membrane organization membrane biogenesis membrane assembly cellular component organization cellular component biogenesis cellular component assembly cellular process cellular component organization or biogenesis cell envelope organization Gram-negative-bacterium-type cell outer membrane assembly external encapsulating structure organization protein localization cellular localization establishment of protein localization establishment of protein localization to membrane localization within membrane protein localization to membrane establishment of localization localization cellular macromolecule localization macromolecule localization protein insertion into membrane response to stimulus response to chemical response to antibiotic	cellular anatomical structure membrane protein-containing complex periplasmic side of cell outer membrane membrane protein complex side of membrane Bam protein complex cell periphery cell outer membrane external encapsulating structure cell envelope outer membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR037873	BamE-like	Homologous Superfamily
A	IPR007450	Outer membrane protein assembly factor BamE domain	Domain
A	IPR026592	Outer membrane protein assembly factor BamE	Family

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.