SBP_bac_3 |
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PFAM accession number: | PF00497 |
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Interpro abstract (IPR001638): | Bacterial high affinity transport systems are involved in active transport of solutes across the cytoplasmic membrane. Most of the bacterial ABC (ATP-binding cassette) importers are composed of one or two transmembrane permease proteins, one or two nucleotide-binding proteins and a highly specific periplasmic solute-binding protein. In Gram-negative bacteria the solute-binding proteins are dissolved in the periplasm, while in archaea and Gram-positive bacteria, their solute-binding proteins are membrane-anchored lipoproteins [ (PUBMED:8003968) (PUBMED:18310026) ]. On the basis of sequence similarities, the vast majority of these solute-binding proteins can be grouped [ (PUBMED:8336670) ] into eight families or clusters, which generally correlate with the nature of the solute bound. This entry represents a domain found in the solute-binding protein family 3 members from Gram-positive bacteria, Gram-negative bacteria and archaea. This domain can also be found in the N-terminal of the membrane-bound lytic murein transglycosylase F (MltF) protein. MltF is a murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product [ (PUBMED:18234673) ]. Familiy 3 members include:
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This is a PFAM domain. For full annotation and more information, please see the PFAM entry SBP_bac_3