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3.A.1.15.14
High affinity Mn2+ uptake complex, PsaABC (Lisher et al. 2013). The crystal structure of the manganese transporter PsaBC from Streptococcus pneumoniae has been solved in an open-inward conformation (Neville et al. 2021). The type II transporter has a tightly closed transmembrane channel due to "extracellular gating" residues that prevent water permeation and ion reflux. Below these residues, the channel contains a metal coordination site, which is essential for manganese translocation. Mutagenesis of the extracellular gate perturbs manganese uptake, while coordination site mutagenesis abolishes import. These structural features are well conserved in metal-specific ABC transporters and are represented throughout the kingdoms of life. Collectively, these results define the structure of PsaBC and reveal the features required for divalent cation transport (Neville et al. 2021).

Accession Number:Q2MGF9
Protein Name:Putative manganese ABC transporter, permease protein
Length:282
Molecular Weight:30186.00
Species:Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) [170187]
Number of TMSs:9
Location1 / Topology2 / Orientation3: Membrane1 / Multi-pass membrane protein2
Substrate Mn2+

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FASTA formatted sequence
1:	MIAEFIDGLQ KFHFLQNALI TAIVVGIVAG AVGCFIILRG MSLMGDAISH AVLPGVALSF 
61:	ILGLDFFIGA IVFGLLAAII ITYIKGNSII KSDTAIGITF SSFLALGIIL IGVAKSSTDL 
121:	FHILFGNILA VQDTDMFITM GVGAAILLLI WIFFKQLLIT SFDELLAKAM GMPVNFYHYL 
181:	LMVLLTLVSV TAMQSVGTIL IVAMLITPAA TAYLYANSLK SMIFLSSTFG ATASVLGLFI 
241:	GYSFNVAAGS SIVLTAASFF LISFFIAPKQ RYLKLKNKHL LK