PMID:2951378

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.

The mannose permease consists of three subunits (IIIMan/ManX, II-PMan/ManY, II-MMan/ManZ) that are all required for sugar transport and phosphorylation.

"The permease consists of three different subunits, IIIMan, II-PMan, and II-MMan, which are encoded in a single transcriptional unit ptsLPM"
ManY (II-PMan) is very hydrophobic and is an integral membrane protein that forms the transmembrane channel together with ManZ (II-MMan).

"II-PMan (28 kDa) is very hydrophobic...Both are integral membrane proteins and most likely form the transmembrane channel"
ManY and ManZ alone are sufficient for lambda DNA penetration.

"II-PMan and II-MMan alone are sufficient for penetration of lambda DNA"
The Man-PTS mediates sugar transport concomitant with phosphorylation and also functions as a chemoreceptor and phage lambda pore.

"The mannose permease of the bacterial phosphotransferase system mediates sugar transport across the cytoplasmic membrane concomitant with sugar phosphorylation. It also functions as a receptor for bacterial chemotaxis and is required for infection of the cell by bacteriophage lambda where it most likely functions as a pore for penetration of lambda DNA"

PMID:5545083

Sugar transport. II. Characterization of constitutive membrane-bound enzymes II of the Escherichia coli phosphotransferase system.

Characterization of PTS enzyme II activities for mannose and glucose transport in E. coli membranes.

PMID:6252281

Amino-sugar transport systems of Escherichia coli K12.

N-acetylglucosamine enters E. coli by two distinct PTS systems; one of these is the PtsM (Man-PTS) system.

"N-Acetylglucosamine enters E. coli by two distinct phosphotransferase systems...One of these is the PtsM system"

PMID:4153999

The role of phosphotransferase-mediated syntheses of fructose 1-phosphate and fructose 6-phosphate in the growth of Escherichia coli on fructose.

Fructose can be transported via the mannose PTS (ptsM) producing fructose 6-phosphate.

PMID:4154035

Genetical analysis of fructose utilization by Escherichia coli.

Genetic analysis of fructose utilization pathways in E. coli, including the role of ptsM.

PMID:15919996

Global topology analysis of the Escherichia coli inner membrane proteome.

Global topology analysis confirmed ManY as an inner membrane protein with cytoplasmic C-terminus using C-terminal GFP/PhoA fusions.

"Using C-terminal tagging with the alkaline phosphatase and green fluorescent protein, we established the periplasmic or cytoplasmic locations of the C termini for 601 inner membrane proteins"

PMID:16858726

A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis.

ManY was identified in membrane protein complexes by 2D BN/SDS-PAGE and LC-MS/MS, confirming its membrane localization.

"the cytosolic and membrane protein complexes of Escherichia coli were separated...the different partners of each protein complex were identified by LC-MS/MS"

PMID:353494

E. coli K-12 pel mutants, which block phage lambda DNA injection, coincide with ptsM, which determines a component of a sugar transport system.

pel mutations that block phage lambda DNA injection map to ptsM (manY), establishing the mannose permease as the receptor for phage lambda DNA injection.

PMID:4604906

Phosphotransferase-system enzymes as chemoreceptors for certain sugars in Escherichia coli chemotaxis.

PTS enzymes serve as chemoreceptors for sugars in E. coli chemotaxis, with the mannose PTS functioning as a chemoreceptor.

PMID:31209249

Structure of the mannose transporter of the bacterial phosphotransferase system.

Cryo-EM structure of ManYZ shows the complex forms a homotrimer of ManY-ManZ heterodimers.

PMID:8774730

Membrane topology of the mannose transporter of Escherichia coli K12.

Membrane topology study establishing ManY as a multi-pass inner membrane protein.

GO_REF:0000033

Annotation inferences using phylogenetic trees

GO_REF:0000044

Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt

GO_REF:0000002

Gene Ontology annotation through association of InterPro records with GO terms

file:ECOLI/manY/manY-deep-research-falcon.md

Falcon (Edison Scientific) deep research report: manY (UniProt P69801), PTS system mannose-specific EIIC component in E. coli K-12

Seip et al. (1994) explicitly map the E. coli mannose-PTS genes to subunits, confirming manY encodes the IIC_Man membrane permease subunit.

"manX, manY, and manZ, genes encoding IIAB\_Man, IIC\_Man, and IID\_Man, respectively."
ManY (IIC_Man) together with ManZ (IID_Man) forms the membrane channel and substrate-binding/translocation machinery; both IIC and IID subunits are required for functional membrane transport and certain receptor functions.

"forms the **membrane channel and substrate-binding/translocation machinery** responsible for selectively transporting sugars across the inner membrane during PTS-mediated uptake"
The mannose-family PTS couples transport to phosphorylation in a single group-translocation step, with phosphate relayed from PEP through EI->HPr->EIIA->EIIB to the incoming sugar.

"so that **transport and phosphorylation occur in a coupled process**"
The ManXYZ/ManY transporter has broad substrate specificity beyond mannose, including glucose, mannosamine, N-acetylglucosamine and 2-deoxyglucose, with poor tolerance for substitutions at C-4 and C-6.

"ManXYZ/ManY is described as mediating PTS uptake/phosphorylation of **mannose** and several other sugars/analogs including **glucose**, **mannosamine**, and **N-acetylglucosamine**, and it can accommodate certain substitutions (e.g., transport/phosphorylation of **2-deoxyglucose**; poor tolerance of substitutions at C-4 and C-6)."
ManY requires ManZ for stable, functional membrane complex formation; ManY is thought to be unstable in the absence of ManZ, and manY-alone overexpression gives only modest uptake effects.

"authors note **ManY is thought to be unstable in the absence of ManZ**"
The cryo-EM ManYZ-microcin E492 structure shows a threefold-symmetric 3:3 assembly with mannose localized mid-membrane, supporting ManY as a core inner-membrane structural component of the transporter complex.

"The complex assembles with **threefold symmetry** and a **3:3 stoichiometry** (3 MccE492 : 3 ManYZ), with **mannose localized mid-membrane** in the complex."
The ManYZ (IIC/IID) membrane complex serves as an inner-membrane receptor/gateway, being used by the pore-forming bacteriocin microcin E492 in a Trojan-horse entry mechanism.

"Microcin E492** inserts into the cytoplasmic membrane and associates with ManYZ, using ManYZ as a receptor in a Trojan-horse entry mechanism"
The ManYZ complex is implicated as the inner-membrane receptor for bacteriophage lambda entry.

"The ManYZ complex is implicated as an inner-membrane receptor involved in **bacteriophage λ** entry"