Annotations: 6YSL

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
D [auth F]	PF01618,PF20560	e6yslF1	A: alpha bundles	X: Bacterial hemolysins-like	H: Biopolymer transport protein ExbB (From Topology)	T: Biopolymer transport protein ExbB	F: PF01618,PF20560	ECOD (1.6)
E	PF01618,PF20560	e6yslE1	A: alpha bundles	X: Bacterial hemolysins-like	H: Biopolymer transport protein ExbB (From Topology)	T: Biopolymer transport protein ExbB	F: PF01618,PF20560	ECOD (1.6)
G [auth C]	PF01618,PF20560	e6yslC1	A: alpha bundles	X: Bacterial hemolysins-like	H: Biopolymer transport protein ExbB (From Topology)	T: Biopolymer transport protein ExbB	F: PF01618,PF20560	ECOD (1.6)
A [auth G]	PF01618,PF20560	e6yslG1	A: alpha bundles	X: Bacterial hemolysins-like	H: Biopolymer transport protein ExbB (From Topology)	T: Biopolymer transport protein ExbB	F: PF01618,PF20560	ECOD (1.6)
F [auth D]	PF01618,PF20560	e6yslD1	A: alpha bundles	X: Bacterial hemolysins-like	H: Biopolymer transport protein ExbB (From Topology)	T: Biopolymer transport protein ExbB	F: PF01618,PF20560	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth G], D [auth F], E, F [auth D], G [auth C]	PF20560	Motility protein A N-terminal (MotA_N)	Motility protein A N-terminal	This entry represents the N-terminal domain of Motility protein A (MotA). MotA is a membrane protein that forms the stator element of the flagellar motor complex together with MotB with 5:2 stoichiometry, which couples ion flow across the cytoplasmic ...	This entry represents the N-terminal domain of Motility protein A (MotA). MotA is a membrane protein that forms the stator element of the flagellar motor complex together with MotB with 5:2 stoichiometry, which couples ion flow across the cytoplasmic membrane to generate torque, and thus, it is required for rotation of the flagellar motor. This domain contains conserved torque-generating charged residues at the C-terminal [1] and is adjacent Pfam:PF01618, which represents MotA TMH3 and TMH4.	Domain
A [auth G], D [auth F], E, F [auth D], G [auth C]	PF01618	MotA/TolQ/ExbB proton channel family (MotA_ExbB)	MotA/TolQ/ExbB proton channel family	-	Family
B [auth A], C [auth B]	PF13677	Membrane MotB of proton-channel complex MotA/MotB (MotB_plug)	Membrane MotB of proton-channel complex MotA/MotB	This is the MotB member of the E.coli MotA/MotB proton-channel complex that forms the stator of the bacterial membrane flagellar motor. Key residues act as a plug to prevent premature proton flow. The plug is in the periplasm just C-terminal to the M ...	This is the MotB member of the E.coli MotA/MotB proton-channel complex that forms the stator of the bacterial membrane flagellar motor. Key residues act as a plug to prevent premature proton flow. The plug is in the periplasm just C-terminal to the MotB TM, consisting of an amphipathic alpha helix flanked by Pro-52 and Pro-65, eg in Swiss:D3V2T1. In addition to the Pro residues, Ile-58, Tyr-61, and Phe 62 are also essential for plug function [1][2].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth G], D [auth F], E, F [auth D], G [auth C]	Motility protein A	-	chemotaxis response to stimulus taxis response to chemical response to external stimulus locomotion transport proton transmembrane transport monoatomic ion transmembrane transport inorganic ion transmembrane transport establishment of localization inorganic cation transmembrane transport transmembrane transport monoatomic cation transmembrane transport chemotaxis response to stimulus taxis response to chemical response to external stimulus locomotion transport proton transmembrane transport monoatomic ion transmembrane transport inorganic ion transmembrane transport establishment of localization inorganic cation transmembrane transport transmembrane transport monoatomic cation transmembrane transport localization monoatomic ion transport cellular process monoatomic cation transport bacterial-type flagellum-dependent swarming motility bacterial-type flagellum-dependent cell motility cell motility archaeal or bacterial-type flagellum-dependent cell motility cilium or flagellum-dependent cell motility	cell periphery plasma membrane membrane cellular anatomical entity
B [auth A], C [auth B]	Motility protein B	-	chemotaxis response to stimulus taxis response to chemical response to external stimulus locomotion cellular process cell motility archaeal or bacterial-type flagellum-dependent cell motility cilium or flagellum-dependent cell motility	cell periphery plasma membrane membrane cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth G], D [auth F], E, F [auth D], G [auth C]	IPR047055	Motility protein A-like	Family
A [auth G], D [auth F], E, F [auth D], G [auth C]	IPR046786	Motility protein A, N-terminal	Domain
A [auth G], D [auth F], E, F [auth D], G [auth C]	IPR002898	MotA/TolQ/ExbB proton channel	Domain
A [auth G], D [auth F], E, F [auth D], G [auth C]	IPR000540	Flagellar motor protein MotA, conserved site	Conserved Site
B [auth A], C [auth B]	IPR006665	OmpA-like domain	Domain
B [auth A], C [auth B]	IPR025713	Motility protein B-like, N-terminal domain	Domain
B [auth A], C [auth B]	IPR036737	OmpA-like domain superfamily	Homologous Superfamily

Membrane Protein Annotation: OPM OPM Database Homepage

Chains	External Link	Type	Class	Superfamily	Family
A [auth G], B [auth A], C [auth B], D [auth F], E A [auth G], B [auth A], C [auth B], D [auth F], E, F [auth D], G [auth C]	OPM				MotA/TolQ/ExbB channel

Membrane Protein Annotation: PDBTM PDBTM Database Homepage

Chains	External Link	Comment
A [auth G], B [auth A], C [auth B], D [auth F], E A [auth G], B [auth A], C [auth B], D [auth F], E, F [auth D], G [auth C]	PDBTM	Annotated as membrane protein by PDBTM

Membrane Protein Annotation: MemProtMD MemProtMD Database Homepage

Chains	External Link	Comment
A [auth G], B [auth A], C [auth B], D [auth F], E A [auth G], B [auth A], C [auth B], D [auth F], E, F [auth D], G [auth C]	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 R01GM133198.