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3.A.1.26.10 ATP-dependent folic acid uptake porter, FolT/EcfT/EcfA1/EcfA2. The crystal structure of FolT has been solved to 3.2 Å resolution in substrate-bound and free conformations, revealing a potential gating mechanism (Zhao et al. 2015).
Accession Number:	I7BV49
Protein Name:	Energy-coupling factor transporter transmembrane protein EcfT
Length:	264
Molecular Weight:	30073.00
Species:	Enterococcus faecalis D32 [1206105]
Number of TMSs:	6
Location¹ / Topology² / Orientation³:	Cell membrane¹ / Multi-pass membrane protein²
Substrate	folic acid

UniProt (Universal Protein Resource)
CDD Search (Conserved Domain Database)

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FASTA formatted sequence

1:	MNKLIFGRYI PGDSFIHRLD PRAKLLASFY FIGIIFLANN WQSYVLIAAF TAFAISLSKI 
61:	SARFFIRGVR PLLWLILFTV ALQTLFTQGG EVYFQWGIIS ITQFGVTNGL FIFCRFVLII 
121:	FMSTLLTLTT APLELSDAIE YLLRPLRVVK FPVHEVSLML SIALRFVPTL MDETEKIMNA 
181:	QRARGVDFGE GNLLQKMKAI VPLLIPLFVS SFNRAEDLAT AMEARGYQGG EGRTKYRILH 
241:	WHLRDTIVMF GFVLLTIGLF VLRT

3.A.1.26.10
ATP-dependent folic acid uptake porter, FolT/EcfT/EcfA1/EcfA2. The crystal structure of FolT has been solved to 3.2 Å resolution in substrate-bound and free conformations, revealing a potential gating mechanism (Zhao et al. 2015).

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3.A.1.26.10ATP-dependent folic acid uptake porter, FolT/EcfT/EcfA1/EcfA2. The crystal structure of FolT has been solved to 3.2 Å resolution in substrate-bound and free conformations, revealing a potential gating mechanism (Zhao et al. 2015).

Cross database links:

External Searches:

Analyze:

3.A.1.26.10
ATP-dependent folic acid uptake porter, FolT/EcfT/EcfA1/EcfA2. The crystal structure of FolT has been solved to 3.2 Å resolution in substrate-bound and free conformations, revealing a potential gating mechanism (Zhao et al. 2015).