mraY

UniProt ID: Q88N79
Organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
Review Status: COMPLETE
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Gene Description

mraY encodes phospho-N-acetylmuramoyl-pentapeptide-transferase (translocase I; EC 2.7.8.13), a polytopic integral inner-membrane enzyme that catalyzes the first committed, lipid-linked step of peptidoglycan biosynthesis. It transfers the phospho-MurNAc-pentapeptide moiety from the soluble precursor UDP-MurNAc-pentapeptide onto the membrane lipid carrier undecaprenyl phosphate, forming lipid I and releasing UMP. The reaction is Mg2+-dependent and initiates the membrane-associated lipid cycle that supplies precursors for cell wall assembly. MraY belongs to the glycosyltransferase 4 family, MraY subfamily, and is broadly conserved across bacteria.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0005886 plasma membrane
IEA
GO_REF:0000120 		ACCEPT
Summary: MraY is a multi-pass integral protein of the bacterial inner (plasma) membrane, where it acts on the membrane lipid carrier undecaprenyl phosphate.
Reason: UniProt places MraY in the cell inner membrane as a multi-pass membrane protein, with ten predicted transmembrane helices, consistent with this localization.
Supporting Evidence:
file:PSEPK/mraY/mraY-uniprot.txt
SUBCELLULAR LOCATION: Cell inner membrane
file:PSEPK/mraY/mraY-uniprot.txt
Multi-pass membrane protein
GO:0008963 phospho-N-acetylmuramoyl-pentapeptide-transferase activity
IEA
GO_REF:0000120 		ACCEPT
Summary: This is the precise molecular function of MraY (translocase I; EC 2.7.8.13), the core catalytic activity of the gene product.
Reason: The GO term matches the UniProt RecName and EC number exactly, and describes transfer of phospho-MurNAc-pentapeptide onto undecaprenyl phosphate to form lipid I.
Supporting Evidence:
file:PSEPK/mraY/mraY-uniprot.txt
RecName: Full=Phospho-N-acetylmuramoyl-pentapeptide-transferase
file:PSEPK/mraY/mraY-uniprot.txt
transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc- pentapeptide onto the lipid carrier undecaprenyl phosphate
file:PSEPK/mraY/mraY-uniprot.txt
PANTHER; PTHR22926; PHOSPHO-N-ACETYLMURAMOYL-PENTAPEPTIDE-TRANSFERASE
GO:0009252 peptidoglycan biosynthetic process
IEA
GO_REF:0000120 		ACCEPT
Summary: MraY catalyzes the first committed lipid-linked step of peptidoglycan biosynthesis, so this is a core biological process for the gene.
Reason: UniProt assigns MraY to the cell wall biogenesis / peptidoglycan biosynthesis pathway, and it initiates the lipid cycle of peptidoglycan synthesis.
Supporting Evidence:
file:PSEPK/mraY/mraY-uniprot.txt
PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
file:PSEPK/mraY/mraY-uniprot.txt
Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan
GO:0016020 membrane
IEA
GO_REF:0000002 		MARK AS OVER ANNOTATED
Summary: Correct but broad; the specific plasma (inner) membrane localization is the informative term and is separately annotated.
Reason: GO:0016020 membrane is a broad parent of GO:0005886 plasma membrane, which is already annotated and more precisely describes the inner-membrane localization of MraY.
Supporting Evidence:
file:PSEPK/mraY/mraY-uniprot.txt
SUBCELLULAR LOCATION: Cell inner membrane
GO:0016780 phosphotransferase activity, for other substituted phosphate groups
IEA
GO_REF:0000120 		MARK AS OVER ANNOTATED
Summary: This is a broad parent of the specific phospho-N-acetylmuramoyl-pentapeptide-transferase activity already annotated for MraY.
Reason: GO:0008963 is the specific child term that precisely describes the MraY reaction, making the generic phosphotransferase parent less informative.
Supporting Evidence:
file:PSEPK/mraY/mraY-uniprot.txt
RecName: Full=Phospho-N-acetylmuramoyl-pentapeptide-transferase
GO:0044038 cell wall macromolecule biosynthetic process
IEA
GO_REF:0000118 		KEEP AS NON CORE
Summary: Correct but broad; the specific peptidoglycan biosynthetic process term captures MraY's role more precisely.
Reason: This TreeGrafter-derived term is a broader parent of GO:0009252 peptidoglycan biosynthetic process, which is the precise core process; retain as a correct but non-core generalization.
Supporting Evidence:
file:PSEPK/mraY/mraY-uniprot.txt
PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
GO:0051992 UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecaprenyl-phosphate transferase activity
IEA
GO_REF:0000116 		ACCEPT
Summary: This Rhea-mapped term describes the same catalytic reaction (RHEA:28386) at the substrate level and is an accurate, precise molecular function for MraY.
Reason: The term corresponds exactly to the UniProt catalytic activity (RHEA:28386, EC 2.7.8.13) using meso-diaminopimelate-containing precursor, the physiological substrate in Gram-negative Pseudomonas.
Supporting Evidence:
file:PSEPK/mraY/mraY-uniprot.txt
Xref=Rhea:RHEA:28386
file:PSEPK/mraY/mraY-uniprot.txt
meso- 2,6-diaminopimeloyl-D-alanyl-D-alanine + di-trans,octa-cis- undecaprenyl phosphate
GO:0071555 cell wall organization
IEA
GO_REF:0000118 		KEEP AS NON CORE
Summary: MraY contributes to building the peptidoglycan cell wall, so this broader cell wall organization process is correct but generic given that the specific peptidoglycan biosynthetic process (GO:0009252) is also annotated and captures the role precisely.
Reason: Correct but a broad generalization of MraY's role; the specific GO:0009252 peptidoglycan biosynthetic process is the core process term, so this broader cell-wall term is retained as non-core, consistent with the treatment of the other broad parent (GO:0044038).
Supporting Evidence:
file:PSEPK/mraY/mraY-uniprot.txt
Cell wall biogenesis/degradation
file:PSEPK/mraY/mraY-uniprot.txt
PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.

Core Functions

MraY catalyzes the Mg2+-dependent transfer of phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto undecaprenyl phosphate to form lipid I, the first committed lipid-linked step of peptidoglycan biosynthesis at the inner membrane.

Molecular Function:
phospho-N-acetylmuramoyl-pentapeptide-transferase activity
Directly Involved In:
peptidoglycan biosynthetic process
Cellular Locations:
plasma membrane
Supporting Evidence:
  • file:PSEPK/mraY/mraY-uniprot.txt
    transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc- pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
  • file:PSEPK/mraY/mraY-uniprot.txt
    PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.

References

GO_REF:0000002
Gene Ontology annotation through association of InterPro records with GO terms
GO_REF:0000116
Automatic Gene Ontology annotation based on Rhea mapping
GO_REF:0000118
TreeGrafter-generated GO annotations
GO_REF:0000120
Combined Automated Annotation using Multiple IEA Methods
file:interpro/panther/PTHR22926/PTHR22926-metadata.yaml
PANTHER family PTHR22926 (PHOSPHO-N-ACETYLMURAMOYL-PENTAPEPTIDE-TRANSFERASE) and subfamily PTHR22926:SF5 (PHOSPHO-N-ACETYLMURAMOYL-PENTAPEPTIDE-TRANSFERASE HOMOLOG)
  • MraY (Q88N79) is classified by PANTHER into family PTHR22926, phospho-N-acetylmuramoyl-pentapeptide-transferase, and subfamily PTHR22926:SF5, confirming the EC 2.7.8.13 phospho-MurNAc-pentapeptide transferase assignment for this gene.
  • The PANTHER subfamily-level placement (PTHR22926:SF5) is consistent with MraY translocase I function, supporting the GO:0008963 molecular function annotation.
PMID:12534463
Complete genome sequence and comparative analysis of the metabolically versatile Pseudomonas putida KT2440.
  • Source of the P. putida KT2440 genome sequence from which mraY (PP_1334) was identified; no direct functional characterization of MraY is reported.
    "Complete genome sequence and comparative analysis of the metabolically versatile Pseudomonas putida KT2440."

Suggested Questions for Experts

Q: Is P. putida KT2440 MraY essential for viability, and how does its activity integrate with the de novo and recycling routes that supply UDP-MurNAc-pentapeptide?

Suggested experts: Bacterial cell-wall biosynthesis experts

Q: Does Pseudomonas MraY display the same nucleoside-antibiotic (e.g. muraymycin, tunicamycin) inhibition profile observed for other bacterial MraY enzymes?

Suggested experts: Antibacterial target / translocase inhibitor experts

Suggested Experiments

Experiment: Heterologously express and purify P. putida MraY in membrane/detergent and assay lipid I formation from UDP-MurNAc-pentapeptide and undecaprenyl phosphate, confirming EC 2.7.8.13 activity and Mg2+ dependence.

Type: in vitro membrane transferase (lipid I formation) assay

Experiment: Test essentiality and effect on cell shape/division via conditional depletion or attempted deletion of mraY (PP_1334) in KT2440, monitoring peptidoglycan precursor pools and morphology.

Type: conditional gene depletion and phenotypic / morphological analysis

📚 Additional Documentation

Notes

(mraY-notes.md)

mraY (Q88N79, PP_1334) — Pseudomonas putida KT2440

Identity

  • UniProt: Q88N79 (MRAY_PSEPK), Reviewed/Swiss-Prot.
  • Gene: mraY; OrderedLocusNames=PP_1334.
  • Product: Phospho-N-acetylmuramoyl-pentapeptide-transferase; EC 2.7.8.13.
  • AltName: UDP-MurNAc-pentapeptide phosphotransferase.
  • 360 AA; integral membrane protein (10 predicted transmembrane helices).
  • Evidence level PE 3 (inferred from homology); annotations largely UniRule/IEA (HAMAP-Rule:MF_00038).
  • Family: glycosyltransferase 4 family, MraY subfamily [UniProt "Belongs to the glycosyltransferase 4 family. MraY subfamily."].

FUNCTION

MraY catalyzes the first committed, lipid-linked (membrane) step of peptidoglycan
biosynthesis: transfer of the phospho-MurNAc-pentapeptide moiety from the soluble
nucleotide precursor UDP-MurNAc-pentapeptide onto the membrane lipid carrier
undecaprenyl phosphate (bactoprenyl phosphate), generating lipid I and releasing UMP.
[UniProt "Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I."]

This is the committed entry point to the membrane-associated ("lipid cycle") stage of
PG synthesis; lipid I is subsequently converted to lipid II by MurG and flipped across
the inner membrane for transglycosylation/transpeptidation.

CATALYTIC ACTIVITY

UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine
+ di-trans,octa-cis-undecaprenyl phosphate = di-trans,octa-cis-undecaprenyl diphospho-N-acetyl-
MurNAc-pentapeptide + UMP. EC=2.7.8.13; Rhea:RHEA:28386.
[UniProt "EC=2.7.8.13"] [UniProt "Xref=Rhea:RHEA:28386"]

COFACTOR

Mg(2+)-dependent transferase. [UniProt "Name=Mg(2+); Xref=ChEBI:CHEBI:18420;"]
Note: "metal ion binding" (GO:0046872) and "magnesium ion binding" are broad relative to
the specific transferase activity; magnesium is a catalytic cofactor, not the core MF.

PATHWAY

Cell wall biogenesis; peptidoglycan biosynthesis. [UniProt "PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis."]
UniPathway: UPA00219.

SUBCELLULAR LOCATION

Cell inner membrane (plasma membrane); multi-pass / polytopic membrane protein.
[UniProt "SUBCELLULAR LOCATION: Cell inner membrane"] [UniProt "Multi-pass membrane protein"]
Ten predicted transmembrane helices (FT TRANSMEM 25..45 through 338..358).

Annotation-review reasoning

  • Core MF: GO:0008963 phospho-N-acetylmuramoyl-pentapeptide-transferase activity — ACCEPT (exact EC 2.7.8.13 reaction).
  • GO:0051992 (the Rhea-mapped undecaprenyl-phosphate transferase activity, RHEA:28386) is the same reaction described at substrate level — ACCEPT as a precise (equivalent) MF.
  • GO:0016780 phosphotransferase activity, for other substituted phosphate groups — broad parent of GO:0008963; MARK_AS_OVER_ANNOTATED.
  • GO:0009252 peptidoglycan biosynthetic process — ACCEPT (core BP, matches PATHWAY).
  • GO:0071555 cell wall organization — ACCEPT (broad but correct BP; UniProtKB-KW Cell wall biogenesis/degradation).
  • GO:0044038 cell wall macromolecule biosynthetic process — correct but is a broad TreeGrafter parent; KEEP_AS_NON_CORE (peptidoglycan biosynthetic process is the precise term).
  • GO:0005886 plasma membrane — ACCEPT (matches Cell inner membrane location).
  • GO:0016020 membrane — broad parent of plasma membrane; MARK_AS_OVER_ANNOTATED.
  • No "metal ion binding"/"magnesium ion binding" GO annotations are present in this GOA, only the Mg2+ KW/COFACTOR; no removal needed for those terms.

References

  • PMID:12534463 Nelson et al. 2002, Environ Microbiol — KT2440 genome sequence (source of the sequence; no functional MraY characterization).

📄 View Raw YAML

 
id: Q88N79
gene_symbol: mraY
product_type: PROTEIN
status: COMPLETE
taxon:
  id: NCBITaxon:160488
  label: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
    / KT2440)
description: mraY encodes phospho-N-acetylmuramoyl-pentapeptide-transferase (translocase
  I; EC 2.7.8.13), a polytopic integral inner-membrane enzyme that catalyzes the first
  committed, lipid-linked step of peptidoglycan biosynthesis. It transfers the
  phospho-MurNAc-pentapeptide moiety from the soluble precursor UDP-MurNAc-pentapeptide
  onto the membrane lipid carrier undecaprenyl phosphate, forming lipid I and releasing
  UMP. The reaction is Mg2+-dependent and initiates the membrane-associated lipid cycle
  that supplies precursors for cell wall assembly. MraY belongs to the glycosyltransferase
  4 family, MraY subfamily, and is broadly conserved across bacteria.
existing_annotations:
- term:
    id: GO:0005886
    label: plasma membrane
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: located_in
  review:
    summary: MraY is a multi-pass integral protein of the bacterial inner (plasma) membrane,
      where it acts on the membrane lipid carrier undecaprenyl phosphate.
    action: ACCEPT
    reason: UniProt places MraY in the cell inner membrane as a multi-pass membrane protein,
      with ten predicted transmembrane helices, consistent with this localization.
    supported_by:
    - reference_id: file:PSEPK/mraY/mraY-uniprot.txt
      supporting_text: 'SUBCELLULAR LOCATION: Cell inner membrane'
    - reference_id: file:PSEPK/mraY/mraY-uniprot.txt
      supporting_text: Multi-pass membrane protein
- term:
    id: GO:0008963
    label: phospho-N-acetylmuramoyl-pentapeptide-transferase activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: enables
  review:
    summary: This is the precise molecular function of MraY (translocase I; EC 2.7.8.13),
      the core catalytic activity of the gene product.
    action: ACCEPT
    reason: The GO term matches the UniProt RecName and EC number exactly, and describes
      transfer of phospho-MurNAc-pentapeptide onto undecaprenyl phosphate to form lipid I.
    supported_by:
    - reference_id: file:PSEPK/mraY/mraY-uniprot.txt
      supporting_text: 'RecName: Full=Phospho-N-acetylmuramoyl-pentapeptide-transferase'
    - reference_id: file:PSEPK/mraY/mraY-uniprot.txt
      supporting_text: 'transfers
        peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-
        pentapeptide onto the lipid carrier undecaprenyl phosphate'
    - reference_id: file:PSEPK/mraY/mraY-uniprot.txt
      supporting_text: 'PANTHER; PTHR22926; PHOSPHO-N-ACETYLMURAMOYL-PENTAPEPTIDE-TRANSFERASE'
- term:
    id: GO:0009252
    label: peptidoglycan biosynthetic process
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: involved_in
  review:
    summary: MraY catalyzes the first committed lipid-linked step of peptidoglycan biosynthesis,
      so this is a core biological process for the gene.
    action: ACCEPT
    reason: UniProt assigns MraY to the cell wall biogenesis / peptidoglycan biosynthesis
      pathway, and it initiates the lipid cycle of peptidoglycan synthesis.
    supported_by:
    - reference_id: file:PSEPK/mraY/mraY-uniprot.txt
      supporting_text: 'PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.'
    - reference_id: file:PSEPK/mraY/mraY-uniprot.txt
      supporting_text: Catalyzes the initial step of the lipid cycle reactions in
        the biosynthesis of the cell wall peptidoglycan
- term:
    id: GO:0016020
    label: membrane
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: located_in
  review:
    summary: Correct but broad; the specific plasma (inner) membrane localization is the
      informative term and is separately annotated.
    action: MARK_AS_OVER_ANNOTATED
    reason: GO:0016020 membrane is a broad parent of GO:0005886 plasma membrane, which is
      already annotated and more precisely describes the inner-membrane localization of MraY.
    supported_by:
    - reference_id: file:PSEPK/mraY/mraY-uniprot.txt
      supporting_text: 'SUBCELLULAR LOCATION: Cell inner membrane'
- term:
    id: GO:0016780
    label: phosphotransferase activity, for other substituted phosphate groups
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: enables
  review:
    summary: This is a broad parent of the specific phospho-N-acetylmuramoyl-pentapeptide-transferase
      activity already annotated for MraY.
    action: MARK_AS_OVER_ANNOTATED
    reason: GO:0008963 is the specific child term that precisely describes the MraY reaction,
      making the generic phosphotransferase parent less informative.
    supported_by:
    - reference_id: file:PSEPK/mraY/mraY-uniprot.txt
      supporting_text: 'RecName: Full=Phospho-N-acetylmuramoyl-pentapeptide-transferase'
- term:
    id: GO:0044038
    label: cell wall macromolecule biosynthetic process
  evidence_type: IEA
  original_reference_id: GO_REF:0000118
  qualifier: involved_in
  review:
    summary: Correct but broad; the specific peptidoglycan biosynthetic process term captures
      MraY's role more precisely.
    action: KEEP_AS_NON_CORE
    reason: This TreeGrafter-derived term is a broader parent of GO:0009252 peptidoglycan
      biosynthetic process, which is the precise core process; retain as a correct but
      non-core generalization.
    supported_by:
    - reference_id: file:PSEPK/mraY/mraY-uniprot.txt
      supporting_text: 'PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.'
- term:
    id: GO:0051992
    label: UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecaprenyl-phosphate
      transferase activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000116
  qualifier: enables
  review:
    summary: This Rhea-mapped term describes the same catalytic reaction (RHEA:28386) at the
      substrate level and is an accurate, precise molecular function for MraY.
    action: ACCEPT
    reason: The term corresponds exactly to the UniProt catalytic activity (RHEA:28386,
      EC 2.7.8.13) using meso-diaminopimelate-containing precursor, the physiological
      substrate in Gram-negative Pseudomonas.
    supported_by:
    - reference_id: file:PSEPK/mraY/mraY-uniprot.txt
      supporting_text: Xref=Rhea:RHEA:28386
    - reference_id: file:PSEPK/mraY/mraY-uniprot.txt
      supporting_text: meso-
        2,6-diaminopimeloyl-D-alanyl-D-alanine + di-trans,octa-cis-
        undecaprenyl phosphate
- term:
    id: GO:0071555
    label: cell wall organization
  evidence_type: IEA
  original_reference_id: GO_REF:0000118
  qualifier: involved_in
  review:
    summary: MraY contributes to building the peptidoglycan cell wall, so this broader cell
      wall organization process is correct but generic given that the specific peptidoglycan
      biosynthetic process (GO:0009252) is also annotated and captures the role precisely.
    action: KEEP_AS_NON_CORE
    reason: Correct but a broad generalization of MraY's role; the specific GO:0009252 peptidoglycan
      biosynthetic process is the core process term, so this broader cell-wall term is retained
      as non-core, consistent with the treatment of the other broad parent (GO:0044038).
    supported_by:
    - reference_id: file:PSEPK/mraY/mraY-uniprot.txt
      supporting_text: Cell wall biogenesis/degradation
    - reference_id: file:PSEPK/mraY/mraY-uniprot.txt
      supporting_text: 'PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.'
references:
- id: GO_REF:0000002
  title: Gene Ontology annotation through association of InterPro records with GO
    terms
  findings: []
- id: GO_REF:0000116
  title: Automatic Gene Ontology annotation based on Rhea mapping
  findings: []
- id: GO_REF:0000118
  title: TreeGrafter-generated GO annotations
  findings: []
- id: GO_REF:0000120
  title: Combined Automated Annotation using Multiple IEA Methods
  findings: []
- id: file:interpro/panther/PTHR22926/PTHR22926-metadata.yaml
  title: PANTHER family PTHR22926 (PHOSPHO-N-ACETYLMURAMOYL-PENTAPEPTIDE-TRANSFERASE)
    and subfamily PTHR22926:SF5 (PHOSPHO-N-ACETYLMURAMOYL-PENTAPEPTIDE-TRANSFERASE
    HOMOLOG)
  findings:
  - statement: MraY (Q88N79) is classified by PANTHER into family PTHR22926, phospho-N-acetylmuramoyl-pentapeptide-transferase,
      and subfamily PTHR22926:SF5, confirming the EC 2.7.8.13 phospho-MurNAc-pentapeptide
      transferase assignment for this gene.
  - statement: The PANTHER subfamily-level placement (PTHR22926:SF5) is consistent
      with MraY translocase I function, supporting the GO:0008963 molecular function
      annotation.
- id: PMID:12534463
  title: Complete genome sequence and comparative analysis of the metabolically versatile
    Pseudomonas putida KT2440.
  findings:
  - statement: Source of the P. putida KT2440 genome sequence from which mraY (PP_1334)
      was identified; no direct functional characterization of MraY is reported.
    reference_section_type: TITLE
    supporting_text: Complete genome sequence and comparative analysis of the metabolically
      versatile Pseudomonas putida KT2440.
core_functions:
- description: MraY catalyzes the Mg2+-dependent transfer of phospho-MurNAc-pentapeptide
    from UDP-MurNAc-pentapeptide onto undecaprenyl phosphate to form lipid I, the first
    committed lipid-linked step of peptidoglycan biosynthesis at the inner membrane.
  molecular_function:
    id: GO:0008963
    label: phospho-N-acetylmuramoyl-pentapeptide-transferase activity
  directly_involved_in:
  - id: GO:0009252
    label: peptidoglycan biosynthetic process
  locations:
  - id: GO:0005886
    label: plasma membrane
  supported_by:
  - reference_id: file:PSEPK/mraY/mraY-uniprot.txt
    supporting_text: 'transfers
      peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-
      pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding
      undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.'
  - reference_id: file:PSEPK/mraY/mraY-uniprot.txt
    supporting_text: 'PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.'
proposed_new_terms: []
suggested_questions:
- question: Is P. putida KT2440 MraY essential for viability, and how does its activity
    integrate with the de novo and recycling routes that supply UDP-MurNAc-pentapeptide?
  experts:
  - Bacterial cell-wall biosynthesis experts
- question: Does Pseudomonas MraY display the same nucleoside-antibiotic (e.g. muraymycin,
    tunicamycin) inhibition profile observed for other bacterial MraY enzymes?
  experts:
  - Antibacterial target / translocase inhibitor experts
suggested_experiments:
- description: Heterologously express and purify P. putida MraY in membrane/detergent and
    assay lipid I formation from UDP-MurNAc-pentapeptide and undecaprenyl phosphate,
    confirming EC 2.7.8.13 activity and Mg2+ dependence.
  experiment_type: in vitro membrane transferase (lipid I formation) assay
- description: Test essentiality and effect on cell shape/division via conditional depletion
    or attempted deletion of mraY (PP_1334) in KT2440, monitoring peptidoglycan precursor
    pools and morphology.
  experiment_type: conditional gene depletion and phenotypic / morphological analysis