TCDB is operated by the Saier Lab Bioinformatics Group
« See all members of the family


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:Q97PG9
Protein Name:Manganese ABC transporter, ATP-binding protein
Length:240
Molecular Weight:26844.00
Species:Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) [170187]
Substrate Mn2+

Cross database links:

External Searches:

Analyze:

Predict TMSs (Predict number of transmembrane segments)
Window Size: Angle:  
FASTA formatted sequence
1:	MIRIENLSVS YKETLALKDI SLVLHGPTIT GIIGPNGAGK STLLKGMLGI IPHQGQAFLD 
61:	DKEVKKSLHR IAYVEQKINI DYNFPIKVKE CVSLGLFPSI PLFRSLKAKH WKKVQEALEI 
121:	VGLADYAERQ ISQLSGGQFQ RVLIARCLVQ EADYILLDEP FAGIDSVSEE IIMNTLRDLK 
181:	KAGKTVLIVH HDLSKIPHYF DQVLLVNREV IAFGPTKETF TETNLKEAYG NQLFFNGGDL