ftsW

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0000917 division septum assembly	NAS PMID:28419603 Assembly and activation of the Escherichia coli divisome.	ACCEPT	Summary: FtsW is a divisome protein acting at the division septum. Reason: The annotation is appropriately septation-specific. FtsW is the SEDS peptidoglycan polymerase half of the FtsW/FtsI septal synthase, and a divisome review describes E. coli division as being mediated by the divisome. Supporting Evidence: PMID:9603865 FtsW, another essential cell division protein, was also localized to the septum. PMID:33495624 Combined with the recent evidence that purified FtsW possesses PGTase activity5, our results in live E.coli cells strongly support the notion that FtsW is an essential septal PGTase in vivo.
GO:0005515 protein binding	IDA PMID:14663069 Use of a two-hybrid assay to study the assembly of a complex...	REMOVE	Summary: The two-hybrid study surveyed FtsW contacts across the E. coli septosome. Reason: The interaction evidence is credible, but GO:0005515 is an uninformative generic binding term. FtsW's core molecular activity is septal peptidoglycan glycosyltransferase activity; this row should not be kept as a stand-alone molecular-function annotation. Supporting Evidence: PMID:14663069 The ability of each of the nine Escherichia coli division proteins (FtsZ, FtsA, ZipA, FtsK, FtsQ, FtsL, FtsW, FtsI, FtsN) to interact with itself and with each of the remaining eight proteins was studied in 43 possible combinations of protein pairs by the two-hybrid system previously developed by the authors' group.
GO:0005515 protein binding	IPI PMID:15774864 Interaction network among Escherichia coli membrane proteins...	REMOVE	Summary: Bacterial two-hybrid analysis supports FtsW-FtsI divisome interactions. Reason: The FtsW-FtsI interaction is biologically important for septal peptidoglycan synthesis, but the generic protein-binding term does not state a specific activity or complex function and is less informative than the accepted septal glycosyltransferase and divisome annotations. Supporting Evidence: PMID:15774864 In the present study, we used a bacterial two-hybrid system based on interaction-mediated reconstitution of a cyclic AMP (cAMP) signaling cascade to unravel the molecular basis of septum assembly by analyzing the protein interaction network among E. coli cell division proteins.
GO:0005515 protein binding	IPI PMID:15774864 Interaction network among Escherichia coli membrane proteins...	REMOVE	Summary: Bacterial two-hybrid analysis supports interactions with divisome partners. Reason: Physical interaction with FtsI/FtsN helps place FtsW in the late divisome, but GO:0005515 is too generic to describe FtsW's molecular role. Supporting Evidence: PMID:15774864 In the present study, we used a bacterial two-hybrid system based on interaction-mediated reconstitution of a cyclic AMP (cAMP) signaling cascade to unravel the molecular basis of septum assembly by analyzing the protein interaction network among E. coli cell division proteins.
GO:0005515 protein binding	IPI PMID:15774864 Interaction network among Escherichia coli membrane proteins...	REMOVE	Summary: The bacterial two-hybrid study places FtsW in a septal network. Reason: Protein interaction evidence should be captured through the divisome and septal synthesis context, not through a generic GO:0005515 molecular function row. Supporting Evidence: PMID:15774864 Altogether, these data suggest that the cell division machinery assembly is driven by the cooperative association among the different Fts proteins to form a dynamic multiprotein structure at the septum site.
GO:0005515 protein binding	IPI PMID:17185541 Three functional subdomains of the Escherichia coli FtsQ pro...	REMOVE	Summary: FtsW interaction with the divisome protein FtsQ was mapped experimentally. Reason: The FtsQ-FtsW contact is a divisome assembly interaction. The stand-alone GO:0005515 annotation is not a useful molecular function for a septal peptidoglycan glycosyltransferase. Supporting Evidence: PMID:17185541 FtsQ, an essential protein for the Escherichia coli divisome assembly, is able to interact with various division proteins, namely FtsI, FtsL, FtsN, FtsB and FtsW.
GO:0005515 protein binding	IPI PMID:18165305 The monofunctional glycosyltransferase of Escherichia coli l...	REMOVE	Summary: MtgA was reported to interact with FtsW and other divisome constituents. Reason: This interaction may reflect divisome-associated peptidoglycan assembly, but GO:0005515 adds no mechanistic function for FtsW and is not a core molecular-function annotation. Supporting Evidence: PMID:18165305 is able to interact with three constituents of the divisome, PBP3, FtsW, and FtsN
GO:0005515 protein binding	IPI PMID:20497333 Direct interactions of early and late assembling division pr...	REMOVE	Summary: FRET assays detected FtsN interactions with late divisome proteins. Reason: FtsN-FtsW proximity is part of the septal divisome interaction network; the GO:0005515 parent term is generic and should not be retained as a molecular-function assertion. Supporting Evidence: PMID:20497333 Interestingly, we find FtsN, one of the latest proteins in the divisome assembly, interacting with late assembling proteins FtsI and FtsW, but also with early (proto-ring) protein ZapA.
GO:0005515 protein binding	IPI PMID:20497333 Direct interactions of early and late assembling division pr...	REMOVE	Summary: Quantitative FRET detected an FtsW-FtsN interaction in E. coli cells. Reason: The evidence supports a physical divisome contact, but the generic binding term does not describe FtsW's SEDS glycosyltransferase function. Supporting Evidence: PMID:20497333 Interestingly, we find FtsN, one of the latest proteins in the divisome assembly, interacting with late assembling proteins FtsI and FtsW, but also with early (proto-ring) protein ZapA.
GO:0005515 protein binding	IPI PMID:20847002 The integral membrane FtsW protein and peptidoglycan synthas...	REMOVE	Summary: FtsW and PBP3/FtsI were shown to form a discrete subcomplex. Reason: The row reports a real FtsW-FtsI contact, but GO:0005515 is a generic parent term. The same biology is better represented by FtsW's septal peptidoglycan glycosyltransferase activity in the divisome. Supporting Evidence: PMID:20847002 These proteins are able to form a discrete complex independently of the other cell-division proteins.
GO:0005515 protein binding	IPI PMID:20847002 The integral membrane FtsW protein and peptidoglycan synthas...	REMOVE	Summary: The FtsW-FtsI/PBP3 subcomplex was characterized directly. Reason: Generic protein binding is not an informative molecular function for FtsW; this interaction belongs in the structural description of the septal SEDS-bPBP pair. Supporting Evidence: PMID:20847002 These proteins are able to form a discrete complex independently of the other cell-division proteins.
GO:0005515 protein binding	IPI PMID:20847002 The integral membrane FtsW protein and peptidoglycan synthas...	REMOVE	Summary: The paper resolved FtsW contacts with septal synthesis proteins. Reason: The underlying physical interaction evidence is useful, but the GO:0005515 row should be removed because it is a generic binding annotation with no specific FtsW activity. Supporting Evidence: PMID:20847002 The periplasmic loop 9/10 of FtsW appeared to be involved in the interaction with both PBP1B and PBP3.
GO:0005515 protein binding	IPI PMID:28233869 Interplay between Penicillin-binding proteins and SEDS prote...	REMOVE	Summary: FtsW, PBP3, and PBP1b were isolated as a ternary complex in vitro. Reason: The result informs how the divisome couples SEDS and PBP enzymes, but GO:0005515 remains a generic binding term and is not the molecular activity that FtsW performs. Supporting Evidence: PMID:28233869 PBP1b, PBP3 and FtsW form a ternary complex in vitro
GO:0005515 protein binding	IPI PMID:29176613 Global landscape of cell envelope protein complexes in Esche...	UNDECIDED	Summary: The full AP-MS article is accessible, but the target-specific interaction edge remains in unverified supplementary data. Reason: The ordinary outcome for adjudicated bare protein binding would be REMOVE as uninformative. Here the precise FtsW interaction underlying PMID:29176613 could not be checked, and the article-level network description is not target-specific support. Retain uncertainty instead of claiming either a false interaction or a narrower functional activity.
GO:0005886 plasma membrane	EXP PMID:11807049 The Escherichia coli cell division protein FtsW is required ...	ACCEPT	Summary: GFP-FtsW localizes to the E. coli septal membrane. Reason: FtsW is a multipass cytoplasmic-membrane protein; plasma membrane is the appropriate GO cellular-component term for the E. coli inner membrane. Supporting Evidence: PMID:11807049 Analysis of FtsW localization confirmed and extended these results; septal localization of FtsW required FtsZ, FtsA, FtsQ, and FtsL but not FtsI.
GO:0005886 plasma membrane	EXP PMID:12423747 Topological characterization of the essential Escherichia co...	ACCEPT	Summary: Topology analysis confirmed that FtsW is a 10-pass membrane protein. Reason: The annotation is directly supported by membrane topology data and is consistent with FtsW's SEDS-family enzymatic role in the membrane. Supporting Evidence: PMID:12423747 N-terminal and C-terminal ends in the cytoplasm, 10 transmembrane segments and one large loop of 67 amino acids (E240-E306) located in the periplasm
GO:0005886 plasma membrane	EXP PMID:9603865 FtsI and FtsW are localized to the septum in Escherichia col...	ACCEPT	Summary: FtsW was localized to the septal inner membrane during E. coli division. Reason: Septal localization of an integral inner-membrane FtsW fusion supports plasma-membrane localization. Supporting Evidence: PMID:9603865 FtsW, another essential cell division protein, was also localized to the septum.
GO:0005886 plasma membrane	IBA GO_REF:0000033	ACCEPT	Summary: Phylogenetic transfer of SEDS inner-membrane localization is correct. Reason: The PANTHER node covers SEDS-family proteins that function as multipass cytoplasmic-membrane peptidoglycan glycosyltransferases; direct E. coli topology and localization evidence independently support the row. Supporting Evidence: PMID:12423747 N-terminal and C-terminal ends in the cytoplasm, 10 transmembrane segments and one large loop of 67 amino acids (E240-E306) located in the periplasm
GO:0005886 plasma membrane	IDA PMID:15919996 Global topology analysis of the Escherichia coli inner membr...	ACCEPT	Summary: The global E. coli topology survey supports FtsW membrane localization. Reason: FtsW has multiple experimentally and computationally supported transmembrane segments, so the directly assayed inner-membrane localization is appropriate. Supporting Evidence: PMID:15919996 we established the periplasmic or cytoplasmic locations of the C termini for 601 inner membrane proteins.
GO:0005886 plasma membrane	IDA PMID:21386816 Identification of FtsW as a transporter of lipid-linked cell...	ACCEPT	Summary: FtsW was assayed as an integral cytoplasmic-membrane protein. Reason: The membrane-vesicle and reconstitution experiments used FtsW as an integral membrane protein, in agreement with the established topology of the SEDS family. Supporting Evidence: PMID:21386816 the integral membrane protein FtsW, an essential protein of the bacterial division machinery, is a transporter of the lipid-linked peptidoglycan precursors across the cytoplasmic membrane.
GO:0005886 plasma membrane	IEA GO_REF:0000120	ACCEPT	Summary: Automated UniProt/UniRule plasma-membrane localization is correct. Reason: The IEA repeats an experimentally supported inner-membrane localization for a 10-pass SEDS membrane enzyme. Supporting Evidence: PMID:12423747 N-terminal and C-terminal ends in the cytoplasm, 10 transmembrane segments and one large loop of 67 amino acids (E240-E306) located in the periplasm
GO:0005886 plasma membrane	NAS PMID:28419603 Assembly and activation of the Escherichia coli divisome.	ACCEPT	Summary: FtsW is a membrane component of the divisome. Reason: Although the cited review is secondary, direct topology and septal localization papers make the plasma-membrane annotation sound. Supporting Evidence: PMID:12423747 N-terminal and C-terminal ends in the cytoplasm, 10 transmembrane segments and one large loop of 67 amino acids (E240-E306) located in the periplasm
GO:0005886 plasma membrane	RCA PMID:7961485 Identification of FtsW and characterization of a new ftsW di...	ACCEPT	Summary: Early FtsW characterization is consistent with inner-membrane localization. Reason: FtsW's anomalous migration and similarity to RodA were early evidence for a membrane-associated polytopic protein, and later topology work confirmed the plasma-membrane localization. Supporting Evidence: PMID:7961485 The product of the ftsW gene has been identified as a polypeptide that, like the related RodA protein, shows anomalous mobility on sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
GO:0008360 regulation of cell shape	IBA GO_REF:0000033	ACCEPT	Summary: Septal glycan synthesis by FtsW contributes to cell surface geometry during constriction. Reason: GO:0008360 covers modulation of cell surface configuration, not only maintenance of lateral rod shape. FtsW itself polymerizes septal wall material and shapes constricting poles; this is direct morphogenetic work, not merely the filamentation phenotype of an essential-gene knockout. PMID:9006034 includes division-block and ftsW rodA double-mutant morphology, while PMID:33495624 connects FtsW inhibition to septal glycan labeling and abnormal septa/poles. This does not assign the RodA lateral-elongation role to FtsW. Supporting Evidence: PMID:33495624 Combined with the recent evidence that purified FtsW possesses PGTase activity5, our results in live E.coli cells strongly support the notion that FtsW is an essential septal PGTase in vivo.
GO:0008360 regulation of cell shape	IMP PMID:9006034 Two polypeptide products of the Escherichia coli cell divisi...	ACCEPT	Summary: Septal glycan synthesis by FtsW contributes to cell surface geometry during constriction. Reason: GO:0008360 covers modulation of cell surface configuration, not only maintenance of lateral rod shape. FtsW itself polymerizes septal wall material and shapes constricting poles; this is direct morphogenetic work, not merely the filamentation phenotype of an essential-gene knockout. PMID:9006034 includes division-block and ftsW rodA double-mutant morphology, while PMID:33495624 connects FtsW inhibition to septal glycan labeling and abnormal septa/poles. This does not assign the RodA lateral-elongation role to FtsW. Supporting Evidence: PMID:33495624 Combined with the recent evidence that purified FtsW possesses PGTase activity5, our results in live E.coli cells strongly support the notion that FtsW is an essential septal PGTase in vivo.
GO:0008955 peptidoglycan glycosyltransferase activity	IEA GO_REF:0000120	ACCEPT	Summary: FtsW supplies septal peptidoglycan glycan-polymerization activity. Reason: The direct purified-protein assays in PMID:30692671 used S. thermophilus, S. aureus and P. aeruginosa orthologs expressed in E. coli; they were not assays of E. coli FtsW. Target-specific PMID:33495624 used E. coli BW25113-derived strains, an MTSES-sensitive FtsW variant, selective inhibition of other polymerases and alkyne-NAM incorporation to assign septal polymerization to FtsW in vivo. The original PMID:27525505 SEDS discovery reinforces family chemistry but does not itself establish every FtsW ortholog. Together these lines support the target claim and direct biosynthetic participation. Supporting Evidence: PMID:33495624 Combined with the recent evidence that purified FtsW possesses PGTase activity5, our results in live E.coli cells strongly support the notion that FtsW is an essential septal PGTase in vivo. PMID:30692671 We conclude that FtsW is a peptidoglycan polymerase that requires divalent cations and the presence of a bPBP for activity.
GO:0009252 peptidoglycan biosynthetic process	IEA GO_REF:0000120	ACCEPT	Summary: FtsW supplies septal peptidoglycan glycan-polymerization activity. Reason: The direct purified-protein assays in PMID:30692671 used S. thermophilus, S. aureus and P. aeruginosa orthologs expressed in E. coli; they were not assays of E. coli FtsW. Target-specific PMID:33495624 used E. coli BW25113-derived strains, an MTSES-sensitive FtsW variant, selective inhibition of other polymerases and alkyne-NAM incorporation to assign septal polymerization to FtsW in vivo. The original PMID:27525505 SEDS discovery reinforces family chemistry but does not itself establish every FtsW ortholog. Together these lines support the target claim and direct biosynthetic participation. Supporting Evidence: PMID:33495624 Combined with the recent evidence that purified FtsW possesses PGTase activity5, our results in live E.coli cells strongly support the notion that FtsW is an essential septal PGTase in vivo. PMID:30692671 We conclude that FtsW is a peptidoglycan polymerase that requires divalent cations and the presence of a bPBP for activity.
GO:0009252 peptidoglycan biosynthetic process	RCA PMID:27525505 SEDS proteins are a widespread family of bacterial cell wall...	ACCEPT	Summary: FtsW supplies septal peptidoglycan glycan-polymerization activity. Reason: The direct purified-protein assays in PMID:30692671 used S. thermophilus, S. aureus and P. aeruginosa orthologs expressed in E. coli; they were not assays of E. coli FtsW. Target-specific PMID:33495624 used E. coli BW25113-derived strains, an MTSES-sensitive FtsW variant, selective inhibition of other polymerases and alkyne-NAM incorporation to assign septal polymerization to FtsW in vivo. The original PMID:27525505 SEDS discovery reinforces family chemistry but does not itself establish every FtsW ortholog. Together these lines support the target claim and direct biosynthetic participation. Supporting Evidence: PMID:33495624 Combined with the recent evidence that purified FtsW possesses PGTase activity5, our results in live E.coli cells strongly support the notion that FtsW is an essential septal PGTase in vivo. PMID:30692671 We conclude that FtsW is a peptidoglycan polymerase that requires divalent cations and the presence of a bPBP for activity.
GO:0015648 lipid-linked peptidoglycan transporter activity	IBA GO_REF:0000033	MARK AS OVER ANNOTATED	Summary: FtsW-mediated transport of fluorescent lipid II is demonstrated in reconstituted membranes; its native contribution remains unresolved. Reason: Purified FtsW promoted lipid-II translocation in proteoliposomes, so the measured capacity is retained as real. However, MurJ performs the essential native flipping step, and no physiological contribution by FtsW is established. This exceeds support for a genuine secondary physiological function under the enzyme-specificity policy. The residual-FtsW caveat in the depletion study prevents a confident claim of zero in-vivo capacity; no quantitative low-efficiency comparison establishes promiscuous noise. MARK_AS_OVER_ANNOTATED therefore records uncertain physiological relevance without discarding the assay or calling it a demonstrated secondary function. Propagation Review Root cause: UNRESOLVED Sources checked: PANTHER:PTN000767103 UNRESOLVED Frozen GOA traces this IBA to PTN000767103 with target P0ABG4 among its descendants. The target has genuine direct in-vitro flippase evidence, so its appearance is not circular. The issue is whether that measured capacity warrants a physiological transporter function given the native MurJ evidence; this review does not infer an erroneous evolutionary node placement or a lineage-specific loss without the tree evidence. Supporting Evidence: PMID:21386816 purified FtsW induced the transbilayer movement of Lipid II in model membranes PMID:25013077 We found that lipid II flipping remained robust in this background (Figs. S8–S9). PMID:25013077 Although it is possible that residual FtsW in these cells was sufficient for the observed activity, this result suggests that SEDS proteins are not responsible for lipid II flippase activity in vivo.
GO:0015648 lipid-linked peptidoglycan transporter activity	IDA PMID:21386816 Identification of FtsW as a transporter of lipid-linked cell...	MARK AS OVER ANNOTATED	Summary: FtsW-mediated transport of fluorescent lipid II is demonstrated in reconstituted membranes; its native contribution remains unresolved. Reason: Purified FtsW promoted lipid-II translocation in proteoliposomes, so the measured capacity is retained as real. However, MurJ performs the essential native flipping step, and no physiological contribution by FtsW is established. This exceeds support for a genuine secondary physiological function under the enzyme-specificity policy. The residual-FtsW caveat in the depletion study prevents a confident claim of zero in-vivo capacity; no quantitative low-efficiency comparison establishes promiscuous noise. MARK_AS_OVER_ANNOTATED therefore records uncertain physiological relevance without discarding the assay or calling it a demonstrated secondary function. Supporting Evidence: PMID:21386816 purified FtsW induced the transbilayer movement of Lipid II in model membranes PMID:25013077 We found that lipid II flipping remained robust in this background (Figs. S8–S9). PMID:25013077 Although it is possible that residual FtsW in these cells was sufficient for the observed activity, this result suggests that SEDS proteins are not responsible for lipid II flippase activity in vivo.
GO:0015836 lipid-linked peptidoglycan transport	IEA GO_REF:0000108	MARK AS OVER ANNOTATED	Summary: FtsW-mediated transport of fluorescent lipid II is demonstrated in reconstituted membranes; its native contribution remains unresolved. Reason: Purified FtsW promoted lipid-II translocation in proteoliposomes, so the measured capacity is retained as real. However, MurJ performs the essential native flipping step, and no physiological contribution by FtsW is established. This exceeds support for a genuine secondary physiological function under the enzyme-specificity policy. The residual-FtsW caveat in the depletion study prevents a confident claim of zero in-vivo capacity; no quantitative low-efficiency comparison establishes promiscuous noise. MARK_AS_OVER_ANNOTATED therefore records uncertain physiological relevance without discarding the assay or calling it a demonstrated secondary function. Supporting Evidence: PMID:21386816 purified FtsW induced the transbilayer movement of Lipid II in model membranes PMID:25013077 We found that lipid II flipping remained robust in this background (Figs. S8–S9). PMID:25013077 Although it is possible that residual FtsW in these cells was sufficient for the observed activity, this result suggests that SEDS proteins are not responsible for lipid II flippase activity in vivo.
GO:0016020 membrane	IEA GO_REF:0000002	MODIFY	Summary: FtsW is an integral protein of the E. coli inner membrane. Reason: The generic membrane annotation is correct but the plasma membrane descendant is already supported by the topology and localization annotations. Refine to GO:0005886 rather than treating a true broad location as an over-annotation. Proposed replacements: plasma membrane Supporting Evidence: PMID:9603865 FtsW, another essential cell division protein, was also localized to the septum.
GO:0032153 cell division site	IBA GO_REF:0000033	ACCEPT	Summary: PAINT transfer of division-site localization is appropriate for FtsW. Reason: FtsW is a late septal SEDS protein whose localization to potential division sites has direct E. coli support. Supporting Evidence: PMID:11807049 Analysis of FtsW localization confirmed and extended these results; septal localization of FtsW required FtsZ, FtsA, FtsQ, and FtsL but not FtsI.
GO:0032153 cell division site	IDA PMID:9603865 FtsI and FtsW are localized to the septum in Escherichia col...	ACCEPT	Summary: FtsW was experimentally localized to septa in E. coli. Reason: This is the precise subcellular location for the septal SEDS-bPBP peptidoglycan synthase containing FtsW. Supporting Evidence: PMID:9603865 FtsW, another essential cell division protein, was also localized to the septum.
GO:0032153 cell division site	IEA GO_REF:0000104	ACCEPT	Summary: Sequence-feature transfer to cell division site is consistent with FtsW. Reason: Proteobacterial FtsW proteins are specialized for divisome function, and E. coli FtsW has direct septal localization evidence. Supporting Evidence: PMID:11807049 Thus, FtsW is a late recruit to the division site and is essential for subsequent recruitment of its cognate transpeptidase FtsI but not for stabilization of FtsZ rings.
GO:0032153 cell division site	NAS PMID:28419603 Assembly and activation of the Escherichia coli divisome.	ACCEPT	Summary: Review-level division-site annotation agrees with direct localization. Reason: FtsW functions at the septum as part of the divisome, so the cell division site component is correct. Supporting Evidence: PMID:9603865 FtsW, another essential cell division protein, was also localized to the septum.
GO:0043093 FtsZ-dependent cytokinesis	IEA GO_REF:0000104	ACCEPT	Summary: UniRule transfer correctly places FtsW in FtsZ-dependent cytokinesis. Reason: E. coli FtsW is recruited downstream of FtsZ/FtsA/FtsQ/FtsL and is essential for septal peptidoglycan synthesis and subsequent division. Supporting Evidence: PMID:11807049 septal localization of FtsW required FtsZ, FtsA, FtsQ, and FtsL but not FtsI.
GO:0043093 FtsZ-dependent cytokinesis	NAS PMID:28419603 Assembly and activation of the Escherichia coli divisome.	ACCEPT	Summary: FtsW belongs to the FtsZ-dependent bacterial cytokinetic machinery. Reason: FtsW is a core membrane synthase of the FtsZ-organized divisome. Supporting Evidence: PMID:9603865 FtsW, another essential cell division protein, was also localized to the septum. PMID:33495624 Combined with the recent evidence that purified FtsW possesses PGTase activity5, our results in live E.coli cells strongly support the notion that FtsW is an essential septal PGTase in vivo.
GO:0051301 cell division	IBA GO_REF:0000033	MODIFY	Summary: FtsW synthesizes the septal glycan framework used in FtsZ-dependent cell division. Reason: FtsW performs the glycan-polymerization step in the FtsZ-organized divisome. GO:0043093 is a verified descendant of cell division and is already asserted in this review. Use that supported division subtype consistently across the genetic, phylogenetic and electronic rows. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN000767103 · PTN000767103 SUPPORTS TRANSFER The source IBD asserts cell division on the FtsW lineage. The target-specific E. coli localization and polymerization evidence supports that inherited claim; refinement here adds the established FtsZ-dependent subtype without declaring the ancestral assertion wrong or requiring the same subtype for every descendant. The lineage loss check found no IRD/IKR. Proposed replacements: FtsZ-dependent cytokinesis Supporting Evidence: PMID:33495624 Combined with the recent evidence that purified FtsW possesses PGTase activity5, our results in live E.coli cells strongly support the notion that FtsW is an essential septal PGTase in vivo. PMID:9603865 FtsW, another essential cell division protein, was also localized to the septum.
GO:0051301 cell division	IEA GO_REF:0000002	MODIFY	Summary: FtsW synthesizes the septal glycan framework used in FtsZ-dependent cell division. Reason: FtsW performs the glycan-polymerization step in the FtsZ-organized divisome. GO:0043093 is a verified descendant of cell division and is already asserted in this review. Use that supported division subtype consistently across the genetic, phylogenetic and electronic rows. Proposed replacements: FtsZ-dependent cytokinesis Supporting Evidence: PMID:33495624 Combined with the recent evidence that purified FtsW possesses PGTase activity5, our results in live E.coli cells strongly support the notion that FtsW is an essential septal PGTase in vivo. PMID:9603865 FtsW, another essential cell division protein, was also localized to the septum.
GO:0051301 cell division	IMP PMID:9006034 Two polypeptide products of the Escherichia coli cell divisi...	MODIFY	Summary: FtsW synthesizes the septal glycan framework used in FtsZ-dependent cell division. Reason: FtsW performs the glycan-polymerization step in the FtsZ-organized divisome. GO:0043093 is a verified descendant of cell division and is already asserted in this review. Use that supported division subtype consistently across the genetic, phylogenetic and electronic rows. Proposed replacements: FtsZ-dependent cytokinesis Supporting Evidence: PMID:33495624 Combined with the recent evidence that purified FtsW possesses PGTase activity5, our results in live E.coli cells strongly support the notion that FtsW is an essential septal PGTase in vivo. PMID:9603865 FtsW, another essential cell division protein, was also localized to the septum.
GO:0051301 cell division	IMP PMID:9603865 FtsI and FtsW are localized to the septum in Escherichia col...	MODIFY	Summary: FtsW synthesizes the septal glycan framework used in FtsZ-dependent cell division. Reason: FtsW performs the glycan-polymerization step in the FtsZ-organized divisome. GO:0043093 is a verified descendant of cell division and is already asserted in this review. Use that supported division subtype consistently across the genetic, phylogenetic and electronic rows. Proposed replacements: FtsZ-dependent cytokinesis Supporting Evidence: PMID:33495624 Combined with the recent evidence that purified FtsW possesses PGTase activity5, our results in live E.coli cells strongly support the notion that FtsW is an essential septal PGTase in vivo. PMID:9603865 FtsW, another essential cell division protein, was also localized to the septum.
GO:0051301 cell division	NAS PMID:28419603 Assembly and activation of the Escherichia coli divisome.	MODIFY	Summary: FtsW synthesizes the septal glycan framework used in FtsZ-dependent cell division. Reason: FtsW performs the glycan-polymerization step in the FtsZ-organized divisome. GO:0043093 is a verified descendant of cell division and is already asserted in this review. Use that supported division subtype consistently across the genetic, phylogenetic and electronic rows. Proposed replacements: FtsZ-dependent cytokinesis Supporting Evidence: PMID:33495624 Combined with the recent evidence that purified FtsW possesses PGTase activity5, our results in live E.coli cells strongly support the notion that FtsW is an essential septal PGTase in vivo. PMID:9603865 FtsW, another essential cell division protein, was also localized to the septum.
GO:1990586 divisome complex	NAS PMID:28419603 Assembly and activation of the Escherichia coli divisome.	ACCEPT	Summary: FtsW is a late membrane component of the divisome. Reason: FtsW acts with FtsI/PBP3 in the divisome to make septal peptidoglycan, and its septal recruitment depends on upstream Fts proteins. Supporting Evidence: PMID:11807049 Thus, FtsW is a late recruit to the division site and is essential for subsequent recruitment of its cognate transpeptidase FtsI but not for stabilization of FtsZ rings.

Gene Description

Existing Annotations Review

Core Functions

References

Suggested Questions for Experts

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Notes

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