btuD vitamin B12 ABC transporter ATP binding subunit [Escherichia coli str. K-12 substr. MG1655] - Gene

Summary

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Official Symbol: btuD
Official Full Name: vitamin B12 ABC transporter ATP binding subunit
Primary source: ECOCYC:EG10128
Locus tag: b1709
See related: ASAP:ABE-0005707
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage: Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as: ECK1707
Summary: BtuD is the ATP-binding component of the BtuCD, an ABC-type vitamin B12 uptake system. [More information is available at EcoCyc: EG10128].
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Genomic context

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Sequence:: NC_000913.3 (1792809..1793558, complement)

NC_000913.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

The periplasmic soluble binding protein BtuF binds the vitamin B12 and the transmembrane and ATPase domains BtuCD mediate the translocation.
Title: Single-molecule visualization of conformational changes and substrate transport in the vitamin B(12) ABC importer BtuCD-F.
study used molecular dynamics simulations to investigate the atomic-level mechanism of conformational coupling in the ABC transporter BtuCD-F
Title: Release of Entropic Spring Reveals Conformational Coupling Mechanism in the ABC Transporter BtuCD-F.
ATP Hydrolysis Induced Conformational Changes in the Vitamin B12 Transporter BtuCD Revealed by MD Simulations
Title: ATP Hydrolysis Induced Conformational Changes in the Vitamin B12 Transporter BtuCD Revealed by MD Simulations.
Data suggest that the asymmetric crystal structure of BtuCD-F is an intermediate state in the process of reverse inward-facing to outward-facing (I-->O) transition.
Title: The conformational transition pathways of ATP-binding cassette transporter BtuCD revealed by targeted molecular dynamics simulation.
Data suggest that BtuF does not discriminate between, or impose, asymmetric conformations of BtuC/BtuD complex. Data confirm conformational disorder observed in BtuC/BtuD/BtuF crystals.
Title: Asymmetric states of vitamin B₁₂ transporter BtuCD are not discriminated by its cognate substrate binding protein BtuF.
Data provide insights into the subunit interactions of an ABC transporter and lays the foundation for studies of the reassembly of BtuCD.
Title: Unravelling the folding and stability of an ABC (ATP-binding cassette) transporter.
ATP-binding cassette transporter BtuCD mediating vitamin B(12) uptake in Escherichia coli couples the energy of ATP hydrolysis to the translocation of vitamin B(12) across the membrane into the cell.
Title: The conformational coupling and translocation mechanism of vitamin B12 ATP-binding cassette transporter BtuCD.
The 2.6 angstrom crystal structure of a complex BtuCD-F reveals substantial conformational changes as compared with the previously reported structures of BtuCD and BtuF
Title: Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF.

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Pathways from PubChem

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

Gene Ontology Provided by EcoCyc

Function	Evidence Code	Pubs
enables ABC-type vitamin B12 transporter activity	IDA Inferred from Direct Assay more info	PubMed
enables ABC-type vitamin B12 transporter activity	IEA Inferred from Electronic Annotation more info
enables ATP binding	IEA Inferred from Electronic Annotation more info
enables ATP binding	ISM Inferred from Sequence Model more info	PubMed
enables ATP binding	RCA inferred from Reviewed Computational Analysis more info	PubMed
enables ATP hydrolysis activity	IEA Inferred from Electronic Annotation more info
enables ATPase-coupled transmembrane transporter activity	IBA Inferred from Biological aspect of Ancestor more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
acts_upstream_of_or_within cobalamin transport	IDA Inferred from Direct Assay more info	PubMed
involved_in cobalamin transport	IDA Inferred from Direct Assay more info	PubMed
involved_in cobalamin transport	IEA Inferred from Electronic Annotation more info
involved_in transmembrane transport	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
part_of ATP-binding cassette (ABC) transporter complex	IBA Inferred from Biological aspect of Ancestor more info
part_of ATP-binding cassette (ABC) transporter complex	IDA Inferred from Direct Assay more info	PubMed
part_of BtuCD complex	IPI Inferred from Physical Interaction more info	PubMed
part_of cobalamin transport complex	IPI Inferred from Physical Interaction more info	PubMed
located_in extrinsic component of membrane	IDA Inferred from Direct Assay more info	PubMed
located_in membrane	IDA Inferred from Direct Assay more info	PubMed
located_in plasma membrane	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: vitamin B12 ABC transporter ATP binding subunit

NP_416224.1

EC 7.6.2.8

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_000913.3 Reference assembly

Range

1792809..1793558 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NP_416224.1 vitamin B12 ABC transporter ATP binding subunit [Escherichia coli str. K-12 substr. MG1655]

See identical proteins and their annotated locations for NP_416224.1

Status: PROVISIONAL

UniProtKB/TrEMBL

A0A2X1KZC0, A0A376KWZ5, A0A403CSX7

Conserved Domains (1) summary

COG4138
Location:2 → 249

BtuD; ABC-type cobalamin transport system, ATPase component [Coenzyme transport and metabolism]