The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The E. coli K-12 gene manY (UniProt P69801) encodes IIC_Man (EIIC-Man), the integral inner-membrane permease subunit of the mannose-family phosphoenolpyruvate:sugar phosphotransferase system (PTS) transporter ManXYZ. In the canonical gene-to-subunit assignment, manX → IIAB_Man, manY → IIC_Man, and manZ → IID_Man. (seip1994mannosetransporterof pages 1-2)
ManY’s primary role is to form (with ManZ) the membrane translocation pathway that couples sugar transport to phosphorylation (group translocation). While mannose is the defining substrate, the E. coli ManXYZ system is also used for uptake/phosphorylation of glucose and multiple amino-sugars/sugar analogs (e.g., 2-deoxyglucose, N-acetylglucosamine, mannosamine/glucosamine) in a broad-specificity “mannose-family” PTS context. (jeckelmann2019carbohydratetransportby pages 27-30, aboulwafa2020proteinproteininteractionsin pages 2-4)
Recent work (2024) demonstrates that E. coli’s relatively slow growth on mannose is not an immutable biochemical limitation of the ManXYZ transporter; instead, it is largely a regulatory/resource-allocation outcome that can be reversed by chromosomal promoter rewiring increasing manXYZ and downstream mannose-metabolic expression, yielding growth on mannose comparable to wild-type growth on glucose. (mukherjee2024plasticityofgrowth pages 10-11, mukherjee2024plasticityofgrowth pages 9-10)
Primary biochemical literature directly assigns E. coli mannose-PTS genes to subunits: “manX, manY, and manZ, genes encoding IIAB_Man, IIC_Man, and IID_Man, respectively.” (Biochemistry, 1994-06; DOI URL: https://doi.org/10.1021/bi00189a021) (seip1994mannosetransporterof pages 1-2)
This mapping matches the user-specified UniProt identity: UniProt P69801 = PTS system mannose-specific EIIC component, gene manY (E. coli K-12). (seip1994mannosetransporterof pages 1-2)
In E. coli K-12, the mannose-specific PTS is encoded by manXYZ, which collectively supplies the mannose PTS Enzyme II components (EIIAB_Man–EIIC_Man–EIID_Man); deletion of manXYZ abolishes mannose utilization/transport. (Journal of Bacteriology, 2006-08; DOI URL: https://doi.org/10.1128/jb.00219-06) (becker2006yeeianovel pages 1-2, becker2006yeeianovel pages 3-4)
The bacterial PTS is a group translocation system: phosphate from phosphoenolpyruvate (PEP) is transferred through a protein phosphorylation cascade (EI → HPr → EIIA → EIIB) to the incoming sugar, so that transport and phosphorylation occur in a coupled process. The overall PEP→sugar phosphoryl transfer is energetically favorable (reported ΔG° ~ −48 kJ·mol−1 in a PTS context). (jeckelmann2019carbohydratetransportby pages 27-30)
The mannose-family PTS transporters are multi-subunit systems with soluble IIA/IIB (or IIAB) phosphotransfer components and membrane IIC + IID components; the IIC and IID subunits are both required for functional membrane transport and for certain receptor functions (e.g., phage/toxin entry). (jeckelmann2019carbohydratetransportby pages 27-30)
ManY (IIC_Man/EIIC-Man) is the integral inner-membrane permease subunit that—together with ManZ (IID_Man)—forms the membrane channel and substrate-binding/translocation machinery responsible for selectively transporting sugars across the inner membrane during PTS-mediated uptake. (seip1994mannosetransporterof pages 1-2, jeckelmann2019carbohydratetransportby pages 27-30)
The functional outcome of ManXYZ activity is import of specific hexoses/hexosamines with concomitant phosphorylation (cytosolic sugar-phosphate formation). Mechanistically, phosphate is relayed via soluble PTS components to the EIIB phosphocarrier and then to the sugar during translocation. (jeckelmann2019carbohydratetransportby pages 27-30, seip1994mannosetransporterof pages 1-2)
A key feature of the E. coli mannose-family transporter is broad specificity beyond mannose. In review-level synthesis of experimental data, 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). (jeckelmann2019carbohydratetransportby pages 27-30, aboulwafa2020proteinproteininteractionsin pages 2-4)
Reconstituted mannose-family IICIID complexes (membrane components corresponding to ManY/ManZ-type) have been reported with distinct kinetics for vectorial (physiological) vs non-vectorial phosphorylation:
- Vectorial phosphorylation: Km ≈ 30 μM, kcat ≈ 1.2 s−1
- Non-vectorial phosphorylation: Km ≈ 0.1 mM, kcat ≈ 3 s−1
These values are presented in an authoritative review of the PTS literature and are used to illustrate the mechanistic coupling of transport and phosphorylation. (jeckelmann2019carbohydratetransportby pages 27-30)
ManY is a cytoplasmic (inner) membrane protein. Together with ManZ it forms the membrane portion of the transporter (IIC/IID). (seip1994mannosetransporterof pages 1-2, jeckelmann2019carbohydratetransportby pages 27-30)
Experimental fusion-mapping and consensus models suggest that IIC_Man (ManY) contains approximately 6 transmembrane segments (with some models allowing 6–8), with N- and C-termini in the cytoplasm; topology predictions for mannose-family IIC/IID have historically been challenging and remain uncertain in older literature. (jeckelmann2019carbohydratetransportby pages 27-30)
A cryo-EM structure of the ManYZ inner-membrane components complexed with the bacteriocin microcin E492 (MccE492) provides detailed architecture. In this structure:
- ManY and ManZ each contain Core, Arm, and Vmotif domain types.
- The complex assembles with threefold symmetry and a 3:3 stoichiometry (3 MccE492 : 3 ManYZ), with mannose localized mid-membrane in the complex.
- Reported cryo-EM reconstruction achieved 2.28 Å overall resolution from 92,052 particles.
(huang2021structureofthe pages 1-3, huang2021structureofthe media feebbc59)
A conformational comparison between apo (inward-facing) and bacteriocin-bound occluded state supports a large “elevator-like” motion: a rigid-body rotation (~47°) and translation (~11 Å) of a Core domain during transition to an occluded state. (huang2021structureofthe pages 3-4)
The manXYZ operon supplies the core components of the D-mannose-specific PTS; deletion of manXYZ abolishes mannose transport/utilization in E. coli K-12, supporting its role as the principal mannose uptake route. (becker2006yeeianovel pages 1-2)
The ManY/ManZ (IIC/IID) membrane complex is exploited as an inner-membrane receptor/gateway in microbial antagonism and infection biology:
- Microcin E492 inserts into the cytoplasmic membrane and associates with ManYZ, using ManYZ as a receptor in a Trojan-horse entry mechanism (outer membrane entry via siderophore receptors followed by inner-membrane association). (huang2021structureofthe pages 1-3)
- The ManYZ complex is implicated as an inner-membrane receptor involved in bacteriophage λ entry; structural analysis suggests MccE492 binds away from the interface proposed to form the λ DNA tunnel and thus may not block λ infection. (huang2021structureofthe pages 3-4)
Mukherjee et al. (PLOS Computational Biology, 2024-01; DOI URL: https://doi.org/10.1371/journal.pcbi.1011735) engineered E. coli by rewiring chromosomal regulation of mannose uptake and catabolism:
- Replaced the native promoter of the manXYZ operon with a strong heterologous promoter (e.g., PptsG or Ptet), increased manA expression (Ptet-manA), and deleted mlc (a regulator affecting PTS expression).
- The resulting “swapped promoter” strain grew on mannose minimal medium at the same rate as wild-type on glucose minimal medium, with reported statistics: WT glucose vs WT mannose P < 0.0001; WT mannose vs engineered strain on mannose P < 0.0001; and WT glucose vs engineered strain on mannose: not significant.
(mukherjee2024plasticityofgrowth pages 10-11, mukherjee2024plasticityofgrowth pages 9-10, mukherjee2024plasticityofgrowth pages 6-7)
Interpretation: this study supports an expert-level conclusion that the apparent “poorness” of mannose as a carbon source in E. coli is largely governed by regulatory architecture and proteome allocation, rather than inherent biochemical constraints of ManY/ManXYZ transport chemistry. (mukherjee2024plasticityofgrowth pages 10-11, mukherjee2024plasticityofgrowth pages 9-10)
Although not 2023–2024, Aboulwafa et al. provide experimental evidence that ManYZ/ManXYZ participates in a broader network of membrane protein–protein interactions affecting PTS activities; importantly, they show manYZ co-expression has much larger functional consequences than manY alone, consistent with ManY requiring ManZ for stable/functional membrane complex formation. (Microbial Physiology, 2020-09; DOI URL: https://doi.org/10.1159/000510257) (aboulwafa2020proteinproteininteractionsin pages 5-6, aboulwafa2020proteinproteininteractionsin pages 1-2)
The manXYZ system is a frequent engineering lever in E. coli strain design because it directly controls PTS-dependent sugar uptake and phosphorylation, shaping carbon flux and global regulation. The 2024 promoter-swap study demonstrates a concrete “implementation”: chromosomal promoter rewiring of manXYZ can markedly alter growth performance on mannose—an approach conceptually aligned with industrial strain optimization where transporter expression is tuned to match desired substrate and productivity profiles. (mukherjee2024plasticityofgrowth pages 10-11, mukherjee2024plasticityofgrowth pages 6-7)
The ManY/ManZ complex’s receptor role for microcin E492 is mechanistically important for designing or understanding bacteriocin-based antagonism strategies. High-resolution structural characterization provides a framework for rational engineering of toxin–receptor interactions. (huang2021structureofthe pages 1-3, huang2021structureofthe pages 3-4)
The following table consolidates gene-to-subunit mapping, localization/topology, substrate scope, quantitative values, and key references.
| Component / gene | Protein name / subunit | Cellular localization / topology notes | Molecular function & substrates | Key quantitative data | Key references (year, DOI URL) |
|---|---|---|---|---|---|
| manX | IIABMan (cytosolic Enzyme IIAB component of mannose-family PTS) | Peripheral/cytosolic phosphotransfer protein; IIA is a homodimeric soluble domain and IIB carries the phospho-accepting histidine/cysteine chemistry typical of the mannose-family pathway; associates with membrane ManY/ManZ complex in the full transporter (seip1994mannosetransporterof pages 1-2, jeckelmann2019carbohydratetransportby pages 27-30) | Receives phosphate from HPr and passes it toward the sugar during group translocation by ManXYZ; part of the transporter used for uptake/phosphorylation of mannose, and also contributes to transport of glucose, 2-deoxyglucose, glucosamine / N-acetylglucosamine in E. coli mannose-family PTS context (seip1994mannosetransporterof pages 1-2, jeckelmann2019carbohydratetransportby pages 27-30, aboulwafa2020proteinproteininteractionsin pages 2-4) | Stable transport complex described as IIABman2:(IICmanIIDman)2; overall PEP→sugar phosphotransfer is strongly favorable (ΔG° ≈ −48 kJ·mol−1) for the PTS pathway (jeckelmann2019carbohydratetransportby pages 27-30) | Seip et al. 1994, Biochemistry, DOI: https://doi.org/10.1021/bi00189a021 (seip1994mannosetransporterof pages 1-2); Jeckelmann & Erni 2019, DOI: https://doi.org/10.1007/978-3-030-18768-2_8 (jeckelmann2019carbohydratetransportby pages 27-30) |
| manY (UniProt P69801; b1818/JW1807 in UniProt context) | IICMan / EIIC-Man; mannose permease IIC component | Integral inner-membrane subunit of ManXYZ. Seip 1994 explicitly maps manY → IICMan. Experimental/speculative topology literature supports ~6 TM segments (possibly 6–8 TM in consensus models) with cytoplasmic N- and C-termini; forms a tight membrane complex with ManZ and contributes Core/Arm/Vmotif architecture in cryo-EM ManYZ structures (seip1994mannosetransporterof pages 1-2, jeckelmann2019carbohydratetransportby pages 27-30, huang2021structureofthe pages 1-3, huang2021structureofthe media feebbc59) | Primary permease subunit for PTS-mediated uptake coupled to phosphorylation of mannose; broader specificity includes glucose, mannosamine, 2-deoxyglucose, glucosamine/N-acetylglucosamine, with poor tolerance for C-4/C-6 sugar substitutions. Physiologically part of the sole mannose uptake system in E. coli and involved in scavenging cell-wall-derived amino sugars (jeckelmann2019carbohydratetransportby pages 27-30, aboulwafa2020proteinproteininteractionsin pages 2-4) | Reconstituted mannose-family IICIID complexes: vectorial phosphorylation Km ≈ 30 μM, kcat ≈ 1.2 s−1; non-vectorial phosphorylation Km ≈ 0.1 mM, kcat ≈ 3 s−1. manY alone overexpression caused only modest uptake changes (e.g., ~1.6-fold for αMG, ~1.1-fold for GlcNAc), whereas manYZ co-overexpression strongly stimulated uptake (αMG ~14.0-fold, 2DG ~10.8-fold, mannitol ~2.1-fold) (jeckelmann2019carbohydratetransportby pages 27-30, aboulwafa2020proteinproteininteractionsin pages 2-4, aboulwafa2020proteinproteininteractionsin pages 5-6, aboulwafa2020proteinproteininteractionsin pages 4-5) | Seip et al. 1994, DOI: https://doi.org/10.1021/bi00189a021 (explicit manY→IICMan) (seip1994mannosetransporterof pages 1-2); Jeckelmann & Erni 2019, DOI: https://doi.org/10.1007/978-3-030-18768-2_8 (jeckelmann2019carbohydratetransportby pages 27-30); Aboulwafa et al. 2020, DOI: https://doi.org/10.1159/000510257 (aboulwafa2020proteinproteininteractionsin pages 4-5, aboulwafa2020proteinproteininteractionsin pages 2-4, aboulwafa2020proteinproteininteractionsin pages 5-6); Huang et al. 2021, DOI: https://doi.org/10.1038/s41421-021-00253-6 (huang2021structureofthe pages 1-3) |
| manZ | IIDMan / EIID-Man | Integral inner-membrane partner of ManY; tightly associated and apparently required for stable ManY function/expression. Topology models suggest a large N-terminal cytoplasmic domain plus multiple C-terminal TM segments; in cryo-EM ManYZ each protomer contributes Core/Arm/Vmotif elements, and ManY/ManZ assemble as a membrane complex (jeckelmann2019carbohydratetransportby pages 27-30, huang2021structureofthe pages 1-3, huang2021structureofthe pages 3-4) | Partner permease subunit that works with ManY to form the membrane translocation/phosphorylation apparatus for mannose-family substrates; required for full transport activity and receptor functions for certain toxins/phages (jeckelmann2019carbohydratetransportby pages 27-30, jeckelmann2019carbohydratetransportby pages 30-33) | manYZ, but not manY alone, strongly increased uptake of heterologous PTS substrates in overexpression assays; authors note ManY is thought to be unstable in the absence of ManZ (aboulwafa2020proteinproteininteractionsin pages 5-6, aboulwafa2020proteinproteininteractionsin pages 1-2) | Jeckelmann & Erni 2019, DOI: https://doi.org/10.1007/978-3-030-18768-2_8 (jeckelmann2019carbohydratetransportby pages 30-33, jeckelmann2019carbohydratetransportby pages 27-30); Huang et al. 2021, DOI: https://doi.org/10.1038/s41421-021-00253-6 (huang2021structureofthe pages 3-4, huang2021structureofthe pages 1-3); Aboulwafa et al. 2020, DOI: https://doi.org/10.1159/000510257 (aboulwafa2020proteinproteininteractionsin pages 5-6, aboulwafa2020proteinproteininteractionsin pages 1-2) |
| ManXYZ system-level finding | Mannose-family PTS transporter (IIAB/IIC/IID) | Inner membrane transporter with cytosolic phosphotransfer components; historic biochemical models described a dimer of IICIID protomers, while cryo-EM of the MccE492–ManYZ complex resolved a 3:3 assembly with mannose located mid-membrane and domain organization into Core, Arm, Vmotif (jeckelmann2019carbohydratetransportby pages 27-30, huang2021structureofthe pages 1-3, huang2021structureofthe media feebbc59) | Main physiological role is group translocation: transport plus phosphorylation of mannose-family sugars. Also acts as an inner-membrane receptor exploited by bacteriophage λ and microcin E492; microcin binding occurs without blocking λ receptor interface (jeckelmann2019carbohydratetransportby pages 30-33, huang2021structureofthe pages 3-4) | Cryo-EM reconstruction of MccE492–ManYZ reached 2.28 Å from 92,052 particles; conformational change to occluded state involved ~47° Core rotation and ~11 Å translation (huang2021structureofthe pages 1-3, huang2021structureofthe pages 3-4) | Huang et al. 2021, DOI: https://doi.org/10.1038/s41421-021-00253-6 (huang2021structureofthe pages 3-4, huang2021structureofthe pages 1-3, huang2021structureofthe media feebbc59); Jeckelmann & Erni 2019, DOI: https://doi.org/10.1007/978-3-030-18768-2_8 (jeckelmann2019carbohydratetransportby pages 30-33, jeckelmann2019carbohydratetransportby pages 27-30) |
| Recent 2024 development relevant to manY/manXYZ | Promoter-engineered mannose PTS / mannose catabolism strain | Chromosomal promoter driving manXYZ replaced with strong heterologous promoter (PptsG or Ptet), combined with Δmlc and stronger manA expression to rewire mannose utilization (mukherjee2024plasticityofgrowth pages 6-7, mukherjee2024plasticityofgrowth pages 5-6) | Demonstrated that slow E. coli growth on mannose is not an intrinsic limitation of ManXYZ chemistry alone; instead, regulatory/proteome allocation limits mannose performance. Strengthening manXYZ and downstream mannose catabolic expression can make mannose behave like a high-quality substrate (mukherjee2024plasticityofgrowth pages 10-11, mukherjee2024plasticityofgrowth pages 9-10) | Engineered strain YCE119 grew on mannose minimal medium at the same rate as wild-type on glucose; statistics reported WT glucose vs WT mannose P < 0.0001, WT mannose vs YCE119 mannose P < 0.0001, while WT glucose vs YCE119 mannose was not significant (mukherjee2024plasticityofgrowth pages 10-11, mukherjee2024plasticityofgrowth pages 9-10) | Mukherjee et al. 2024, PLOS Comput Biol, DOI: https://doi.org/10.1371/journal.pcbi.1011735 (mukherjee2024plasticityofgrowth pages 10-11, mukherjee2024plasticityofgrowth pages 9-10, mukherjee2024plasticityofgrowth pages 6-7, mukherjee2024plasticityofgrowth pages 5-6) |
Table: This table summarizes the E. coli K-12 mannose-family PTS with emphasis on manY (UniProt P69801), including subunit assignments, membrane topology/function, quantitative transport data, and recent 2024 regulatory-engineering findings. It is useful for quickly verifying that manY is the EIIC permease subunit and for linking classic biochemical understanding to current physiological and structural studies.
Cropped Figure 1 panels from the ManYZ–microcin cryo-EM study show the domain architecture (Core/Arm/Vmotif) and the 3:3 assembly of MccE492 with ManYZ, supporting ManY’s role as a core inner-membrane structural component of the complex. (huang2021structureofthe media feebbc59, huang2021structureofthe media 7f7a09c3)
References
(seip1994mannosetransporterof pages 1-2): Stephan Seip, Jochen Balbach, Stefan Behrens, Horst Kessler, Karin Fluekiger, Rita de Meyer, and Bernhard Erni. Mannose transporter of escherichia coli. backbone assignments and secondary structure of the iia domain of the iiabman subunit. Biochemistry, 33 23:7174-83, Jun 1994. URL: https://doi.org/10.1021/bi00189a021, doi:10.1021/bi00189a021. This article has 25 citations and is from a peer-reviewed journal.
(jeckelmann2019carbohydratetransportby pages 27-30): Jean-Marc Jeckelmann and Bernhard Erni. Carbohydrate transport by group translocation: the bacterial phosphoenolpyruvate: sugar phosphotransferase system. Sub-cellular biochemistry, 92:223-274, Jan 2019. URL: https://doi.org/10.1007/978-3-030-18768-2_8, doi:10.1007/978-3-030-18768-2_8. This article has 63 citations.
(aboulwafa2020proteinproteininteractionsin pages 2-4): Mohammad M. Aboulwafa, Zhongge Zhang, and M. Saier. Protein-protein interactions in the cytoplasmic membrane of escherichia coli: influence of the overexpression of diverse transporter-encoding genes on the activities of pts sugar uptake systems. Microbial Physiology, 30:36-49, Sep 2020. URL: https://doi.org/10.1159/000510257, doi:10.1159/000510257. This article has 5 citations.
(mukherjee2024plasticityofgrowth pages 10-11): Avik Mukherjee, Yu-Fang Chang, Yanqing Huang, Nina Catherine Benites, Leander Ammar, Jade Ealy, Mark Polk, and Markus Basan. Plasticity of growth laws tunes resource allocation strategies in bacteria. PLOS Computational Biology, 20:e1011735, Jan 2024. URL: https://doi.org/10.1371/journal.pcbi.1011735, doi:10.1371/journal.pcbi.1011735. This article has 10 citations and is from a highest quality peer-reviewed journal.
(mukherjee2024plasticityofgrowth pages 9-10): Avik Mukherjee, Yu-Fang Chang, Yanqing Huang, Nina Catherine Benites, Leander Ammar, Jade Ealy, Mark Polk, and Markus Basan. Plasticity of growth laws tunes resource allocation strategies in bacteria. PLOS Computational Biology, 20:e1011735, Jan 2024. URL: https://doi.org/10.1371/journal.pcbi.1011735, doi:10.1371/journal.pcbi.1011735. This article has 10 citations and is from a highest quality peer-reviewed journal.
(becker2006yeeianovel pages 1-2): Ann-Katrin Becker, Tim Zeppenfeld, Ariane Staab, Sabine Seitz, Winfried Boos, Teppei Morita, Hiroji Aiba, Kerstin Mahr, Fritz Titgemeyer, and Knut Jahreis. Yeei, a novel protein involved in modulation of the activity of the glucose-phosphotransferase system in escherichia coli k-12. Journal of Bacteriology, 188:5439-5449, Aug 2006. URL: https://doi.org/10.1128/jb.00219-06, doi:10.1128/jb.00219-06. This article has 29 citations and is from a peer-reviewed journal.
(becker2006yeeianovel pages 3-4): Ann-Katrin Becker, Tim Zeppenfeld, Ariane Staab, Sabine Seitz, Winfried Boos, Teppei Morita, Hiroji Aiba, Kerstin Mahr, Fritz Titgemeyer, and Knut Jahreis. Yeei, a novel protein involved in modulation of the activity of the glucose-phosphotransferase system in escherichia coli k-12. Journal of Bacteriology, 188:5439-5449, Aug 2006. URL: https://doi.org/10.1128/jb.00219-06, doi:10.1128/jb.00219-06. This article has 29 citations and is from a peer-reviewed journal.
(huang2021structureofthe pages 1-3): Kai Huang, Jianwei Zeng, Xueli Liu, Tianyu Jiang, and Jiawei Wang. Structure of the mannose phosphotransferase system (man-pts) complexed with microcin e492, a pore-forming bacteriocin. Cell Discovery, Apr 2021. URL: https://doi.org/10.1038/s41421-021-00253-6, doi:10.1038/s41421-021-00253-6. This article has 33 citations and is from a peer-reviewed journal.
(huang2021structureofthe media feebbc59): Kai Huang, Jianwei Zeng, Xueli Liu, Tianyu Jiang, and Jiawei Wang. Structure of the mannose phosphotransferase system (man-pts) complexed with microcin e492, a pore-forming bacteriocin. Cell Discovery, Apr 2021. URL: https://doi.org/10.1038/s41421-021-00253-6, doi:10.1038/s41421-021-00253-6. This article has 33 citations and is from a peer-reviewed journal.
(huang2021structureofthe pages 3-4): Kai Huang, Jianwei Zeng, Xueli Liu, Tianyu Jiang, and Jiawei Wang. Structure of the mannose phosphotransferase system (man-pts) complexed with microcin e492, a pore-forming bacteriocin. Cell Discovery, Apr 2021. URL: https://doi.org/10.1038/s41421-021-00253-6, doi:10.1038/s41421-021-00253-6. This article has 33 citations and is from a peer-reviewed journal.
(mukherjee2024plasticityofgrowth pages 6-7): Avik Mukherjee, Yu-Fang Chang, Yanqing Huang, Nina Catherine Benites, Leander Ammar, Jade Ealy, Mark Polk, and Markus Basan. Plasticity of growth laws tunes resource allocation strategies in bacteria. PLOS Computational Biology, 20:e1011735, Jan 2024. URL: https://doi.org/10.1371/journal.pcbi.1011735, doi:10.1371/journal.pcbi.1011735. This article has 10 citations and is from a highest quality peer-reviewed journal.
(aboulwafa2020proteinproteininteractionsin pages 5-6): Mohammad M. Aboulwafa, Zhongge Zhang, and M. Saier. Protein-protein interactions in the cytoplasmic membrane of escherichia coli: influence of the overexpression of diverse transporter-encoding genes on the activities of pts sugar uptake systems. Microbial Physiology, 30:36-49, Sep 2020. URL: https://doi.org/10.1159/000510257, doi:10.1159/000510257. This article has 5 citations.
(aboulwafa2020proteinproteininteractionsin pages 1-2): Mohammad M. Aboulwafa, Zhongge Zhang, and M. Saier. Protein-protein interactions in the cytoplasmic membrane of escherichia coli: influence of the overexpression of diverse transporter-encoding genes on the activities of pts sugar uptake systems. Microbial Physiology, 30:36-49, Sep 2020. URL: https://doi.org/10.1159/000510257, doi:10.1159/000510257. This article has 5 citations.
(aboulwafa2020proteinproteininteractionsin pages 4-5): Mohammad M. Aboulwafa, Zhongge Zhang, and M. Saier. Protein-protein interactions in the cytoplasmic membrane of escherichia coli: influence of the overexpression of diverse transporter-encoding genes on the activities of pts sugar uptake systems. Microbial Physiology, 30:36-49, Sep 2020. URL: https://doi.org/10.1159/000510257, doi:10.1159/000510257. This article has 5 citations.
(jeckelmann2019carbohydratetransportby pages 30-33): Jean-Marc Jeckelmann and Bernhard Erni. Carbohydrate transport by group translocation: the bacterial phosphoenolpyruvate: sugar phosphotransferase system. Sub-cellular biochemistry, 92:223-274, Jan 2019. URL: https://doi.org/10.1007/978-3-030-18768-2_8, doi:10.1007/978-3-030-18768-2_8. This article has 63 citations.
(mukherjee2024plasticityofgrowth pages 5-6): Avik Mukherjee, Yu-Fang Chang, Yanqing Huang, Nina Catherine Benites, Leander Ammar, Jade Ealy, Mark Polk, and Markus Basan. Plasticity of growth laws tunes resource allocation strategies in bacteria. PLOS Computational Biology, 20:e1011735, Jan 2024. URL: https://doi.org/10.1371/journal.pcbi.1011735, doi:10.1371/journal.pcbi.1011735. This article has 10 citations and is from a highest quality peer-reviewed journal.
(huang2021structureofthe media 7f7a09c3): Kai Huang, Jianwei Zeng, Xueli Liu, Tianyu Jiang, and Jiawei Wang. Structure of the mannose phosphotransferase system (man-pts) complexed with microcin e492, a pore-forming bacteriocin. Cell Discovery, Apr 2021. URL: https://doi.org/10.1038/s41421-021-00253-6, doi:10.1038/s41421-021-00253-6. This article has 33 citations and is from a peer-reviewed journal.