Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Combined Automated Annotation using Multiple IEA Methods
Falcon (Edison Scientific) deep research report: Functional annotation of manX (UniProt P69797) in Escherichia coli K-12
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Falcon corroborates ManX as the cytosolic EIIAB phosphotransfer subunit of the mannose-family PTS, distinct from the membrane permease subunits ManY/ManZ.
"ManX** is the **mannose-family PTS EIIAB subunit**. In curated annotations, it is associated with the inner-membrane system but is itself annotated as a **cytosolic component (IM, C)**, consistent with a cytosolic phosphotransfer function that operates in conjunction with inner-membrane permease components."
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Falcon corroborates the manXYZ operon organization, with manY and manZ encoding the membrane permease subunits of the complex.
"Multiple sources explicitly place **manX** with **manY** and **manZ** in the **manXYZ** locus, where manY and manZ encode the membrane permease subunits."
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Falcon corroborates the broad/promiscuous substrate range of the Man-PTS beyond mannose, consistent with the secondary glucose, fructose, and N-acetylglucosamine transport annotations marked non-core in this review.
"the mannose-family PTS can be **promiscuous** in substrate handling beyond mannose"
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Falcon corroborates a substrate set including mannose, glucose, 2-deoxyglucose, fructose, and amino sugars (GlcNAc/GlcN) for the ManXYZ PTS system.
"lists substrates associated with the ManXYZ PTS system including **mannose, glucose, 2-deoxyglucose, fructose**, and amino sugars (including **GlcNAc/GlcN**)"
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Falcon corroborates the dual localization of ManX as a cytosolic/peripheral phosphotransfer component associated with the inner membrane complex.
"ManX is annotated as **IM, C**, consistent with a **cytosolic/peripheral phosphotransfer component associated with the inner membrane complex**."
Large-scale identification of protein-protein interaction of Escherichia coli K-12.
A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis.
The mannose permease of Escherichia coli consists of three different proteins. Amino acid sequence and function in sugar transport, sugar phosphorylation, and penetration of phage lambda DNA.
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Demonstrated that the mannose permease consists of three subunits (IIIMan/ManX, II-PMan/ManY, II-MMan/ManZ) encoded in a single transcriptional unit. All three are required for sugar transport and phosphorylation. ManX (IIIMan, 35 kDa) is a hydrophilic protein that is transiently phosphorylated and contains the active site for sugar phosphorylation. The permease also functions as a receptor for bacterial chemotaxis and is required for bacteriophage lambda DNA penetration (II-PMan and II-MMan are sufficient for lambda DNA penetration).
The mannose-permease of the bacterial phosphotransferase system. Gene cloning and purification of the enzyme IIMan/IIIMan complex of Escherichia coli.
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Cloned ptsM and ptsL genes and purified IIMan/IIIMan complex. IIIMan (ManX, 35 kDa) exists as a dimer, found both membrane-associated and free in the cytoplasm. IIIMan can be phosphorylated in a PEP-dependent reaction. Both IIMan and IIIMan are required for phosphorylation of 2-deoxyglucose in vitro.
Mannose permease of Escherichia coli. Domain structure and function of the phosphorylating subunit.
The mannose transporter of Escherichia coli. Structure and function of the IIABMan subunit.
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Mutagenesis studies confirmed His-10 and His-175 as active site residues. H10C and H175C mutations abolish phosphotransferase activity. H10C also prevents dimerization. H86N mutation abolishes activity, indicating His-86 involvement in phosphoryl transfer between the two domains. EC 2.7.1.191 catalytic activity confirmed.
The role of phosphotransferase-mediated syntheses of fructose 1-phosphate and fructose 6-phosphate in the growth of Escherichia coli on fructose.
Genetical analysis of fructose utilization by Escherichia coli.
Sugar transport. II. Characterization of constitutive membrane-bound enzymes II of the Escherichia coli phosphotransferase system.
Amino-sugar transport systems of Escherichia coli K12.
Phosphotransferase-system enzymes as chemoreceptors for certain sugars in Escherichia coli chemotaxis.
E. coli K-12 pel mutants, which block phage lambda DNA injection, coincide with ptsM, which determines a component of a sugar transport system.