4CU4

FhuA from E. coli in complex with the lasso peptide microcin J25 (MccJ25)

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Membrane Protein Annotation: OPM
Membrane Protein Annotation: PDBTM
Membrane Protein Annotation: MemProtMD
Membrane Protein Annotation: mpstruc

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d4cu4b_	Peptides	Macrocyclic bacteriocins	Macrocyclic bacteriocins	Microcin J25	Microcin J25	(Escherichia coli str. K-12 substr. MC4100 ) [TaxId: 1403831 ],	SCOPe (2.08)
A	d4cu4a_	Membrane and cell surface proteins and peptides	Transmembrane beta-barrels	Porins	Ligand-gated protein channel	automated matches	(Escherichia coli str. K-12 substr. MG1655 ) [TaxId: 511145 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Porins	8037920	3000224	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	TonB_dep_Rec_1	e4cu4A2	A: beta barrels	X: Outer membrane meander beta-barrels	H: Porins	T: Ligand-gated protein channel	F: TonB_dep_Rec_1	ECOD (1.6)
A	Plug	e4cu4A1	A: a+b complex topology	X: N0 domain in phage tail proteins and secretins-like	H: TonB-dependent receptor plug domain (From Topology)	T: TonB-dependent receptor plug domain	F: Plug	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.170.130.10	Mainly Beta	Beta Complex	Ferric Hydroxamate Uptake Protein	Chain A, domain 1	CATH (4.3.0)
A	2.40.170.20	Mainly Beta	Beta Barrel	Maltoporin	Chain A	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00593	TonB dependent receptor-like, beta-barrel (TonB_dep_Rec_b-barrel)	TonB dependent receptor-like, beta-barrel	This entry represents the beta-barrel domain of TonB-dependent receptors, such as BtuB, CirA, FatA, FcuT, FecA, FepA, among others [1].	Domain
A	PF07715	TonB-dependent Receptor Plug Domain (Plug)	TonB-dependent Receptor Plug Domain	The Plug domain has been shown to be an independently folding subunit of the TonB-dependent receptors ([1]). It acts as the channel gate, blocking the pore until the channel is bound by ligand. At this point it under goes conformational changes opens ...	The Plug domain has been shown to be an independently folding subunit of the TonB-dependent receptors ([1]). It acts as the channel gate, blocking the pore until the channel is bound by ligand. At this point it under goes conformational changes opens the channel.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
B	MICROCIN J25	-	biological process involved in interspecies interaction between organisms response to stimulus response to other organism defense response response to external stimulus response to biotic stimulus defense response to bacterium defense response to other organism response to stress response to bacterium response to external biotic stimulus cellular process disruption of cell in another organism disruption of anatomical structure in another organism biological process involved in interspecies interaction between organisms response to stimulus response to other organism defense response response to external stimulus response to biotic stimulus defense response to bacterium defense response to other organism response to stress response to bacterium response to external biotic stimulus cellular process disruption of cell in another organism disruption of anatomical structure in another organism killing of cells of another organism cell killing	cellular anatomical structure extracellular region
A	FERRICHROME-IRON RECEPTOR	protein binding binding protein domain specific binding molecular transducer activity signaling receptor activity cation binding transition metal ion binding iron ion binding ion binding metal ion binding small molecule binding toxic substance binding siderophore-iron transmembrane transporter activity siderophore uptake transmembrane transporter activity protein binding binding protein domain specific binding molecular transducer activity signaling receptor activity cation binding transition metal ion binding iron ion binding ion binding metal ion binding small molecule binding toxic substance binding siderophore-iron transmembrane transporter activity siderophore uptake transmembrane transporter activity transporter activity transmembrane transporter activity virion binding	intracellular iron ion homeostasis inorganic ion homeostasis cellular homeostasis chemical homeostasis homeostatic process intracellular monoatomic cation homeostasis monoatomic ion homeostasis intracellular chemical homeostasis monoatomic cation homeostasis intracellular monoatomic ion homeostasis siderophore transport transport monoatomic ion transmembrane transport iron ion transport intracellular iron ion homeostasis inorganic ion homeostasis cellular homeostasis chemical homeostasis homeostatic process intracellular monoatomic cation homeostasis monoatomic ion homeostasis intracellular chemical homeostasis monoatomic cation homeostasis intracellular monoatomic ion homeostasis siderophore transport transport monoatomic ion transmembrane transport iron ion transport iron ion transmembrane transport inorganic ion transmembrane transport establishment of localization metal ion transport inorganic cation transmembrane transport siderophore transmembrane transport transmembrane transport monoatomic cation transmembrane transport localization transition metal ion transport monoatomic ion transport cellular process monoatomic cation transport iron coordination entity transport	cellular anatomical structure membrane protein-containing complex transmembrane transporter complex membrane protein complex transporter 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	IPR039426	TonB-dependent receptor-like	Family
A	IPR037066	TonB-dependent receptor, plug domain superfamily	Homologous Superfamily
A	IPR010917	TonB-dependent receptor, conserved site	Conserved Site
A	IPR010105	TonB-dependent siderophore receptor	Family
A	IPR036942	TonB-dependent receptor-like, beta-barrel domain superfamily	Homologous Superfamily
A	IPR012910	TonB-dependent receptor, plug domain	Domain
A	IPR010916	TonB box, conserved site	Conserved Site
A	IPR000531	TonB-dependent receptor-like, beta-barrel	Domain

Membrane Protein Annotation: OPM OPM Database Homepage

Chains	External Link	Type	Class	Superfamily	Family
A	OPM	Transmembrane	Beta-barrel transmembrane	Ligand-gated protein channels (n=22,S=24)	Outer Membrane Receptor (OMR)

Membrane Protein Annotation: PDBTM PDBTM Database Homepage

Chains	External Link	Comment
A	PDBTM	Annotated as membrane protein by PDBTM

Membrane Protein Annotation: MemProtMD MemProtMD Database Homepage

Chains	External Link	Comment
A	MemProtMD	Annotated as membrane protein by MemProtMD

Membrane Protein Annotation: mpstruc mpstruc Database Homepage

Chains	Resource Link	Group	Subgroup	Protein
A	mpstruc	TRANSMEMBRANE PROTEINS: BETA-BARREL	Beta-Barrel Membrane Proteins: Monomeric/Dimeric	FhuA in complex with lasso peptide microcin J25 (MccJ25)

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.