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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:P0A4G2
Protein Name:Manganese ABC transporter substrate-binding lipoprotein
Length:309
Molecular Weight:34594.00
Species:Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) [170187]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Cell membrane1 / Lipid-anchor2
Substrate Mn2+

Cross database links:

Structure:
1PSZ   3ZK7   3ZK8   3ZK9   3ZKA   3ZTT   4UTO   4UTP     

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MKKLGTLLVL FLSAIILVAC ASGKKDTTSG QKLKVVATNS IIADITKNIA GDKIDLHSIV 
61:	PIGQDPHEYE PLPEDVKKTS EADLIFYNGI NLETGGNAWF TKLVENAKKT ENKDYFAVSD 
121:	GVDVIYLEGQ NEKGKEDPHA WLNLENGIIF AKNIAKQLSA KDPNNKEFYE KNLKEYTDKL 
181:	DKLDKESKDK FNKIPAEKKL IVTSEGAFKY FSKAYGVPSA YIWEINTEEE GTPEQIKTLV 
241:	EKLRQTKVPS LFVESSVDDR PMKTVSQDTN IPIYAQIFTD SIAEQGKEGD SYYSMMKYNL 
301:	DKIAEGLAK