Cloning and characterization of ftsN, an essential cell division gene in Escherichia coli isolated as a multicopy suppressor of ftsA12(Ts).Dai K., Xu Y., Lutkenhaus J.View abstractCited forNUCLEOTIDE SEQUENCE [GENOMIC DNA]CategorySequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Bacteriol. 175:3790-3797 (1993)Cited in1
No title available.Wu B., Ang D.Cited forNUCLEOTIDE SEQUENCE [GENOMIC DNA]StrainXPH43CategorySequencesSourceUniProtKB reviewed (Swiss-Prot)Submission Submitted to EMBL/GenBank/DDBJ databases (NOV-1992)Cited in1
Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes.Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.View abstractCited forNUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]StrainK12 / MG1655 / ATCC 47076CategorySequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCNucleic Acids Res. 21:3391-3398 (1993)Cited in88
The complete genome sequence of Escherichia coli K-12.Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K.[...], Shao Y.View abstractCited forNUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]StrainK12 / MG1655 / ATCC 47076CategorySequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCScience 277:1453-1462 (1997)Cited in99+4
Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L.[...], Horiuchi T.View abstractCited forNUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]StrainK12 / W3110 / ATCC 27325 / DSM 5911CategorySequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCMol. Syst. Biol. 2:E1-E5 (2006)Cited in99+3
Topological characterization of the essential Escherichia coli cell division protein FtsN.Dai K., Xu Y., Lutkenhaus J.View abstractCited forSUBCELLULAR LOCATION, TOPOLOGYStrainK12CategorySubcellular LocationSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Bacteriol. 178:1328-1334 (1996)Cited in1
FtsN, a late recruit to the septum in Escherichia coli.Addinall S.G., Cao C., Lutkenhaus J.View abstractCited forSUBCELLULAR LOCATIONStrainK12CategorySubcellular LocationSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCMol. Microbiol. 25:303-309 (1997)Cited in3
FtsQ, FtsL and FtsI require FtsK, but not FtsN, for co-localization with FtsZ during Escherichia coli cell division.Chen J.C., Beckwith J.View abstractCited forDISRUPTION PHENOTYPECategoryPhenotypes & VariantsSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCMol. Microbiol. 42:395-413 (2001)Cited in5
ZipA is required for recruitment of FtsK, FtsQ, FtsL, and FtsN to the septal ring in Escherichia coli.Hale C.A., de Boer P.A.J.View abstractCited forSUBCELLULAR LOCATIONCategorySubcellular LocationSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Bacteriol. 184:2552-2556 (2002)Cited in5
The Escherichia coli amidase AmiC is a periplasmic septal ring component exported via the twin-arginine transport pathway.Bernhardt T.G., de Boer P.A.View abstractCited forFUNCTION IN RECRUITMENT OF AMICStrainK12CategoryFunctionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCMol. Microbiol. 48:1171-1182 (2003)Cited in3
Murein (peptidoglycan) binding property of the essential cell division protein FtsN from Escherichia coli.Ursinus A., van den Ent F., Brechtel S., de Pedro M., Hoeltje J.V., Loewe J., Vollmer W.View abstractCited forDOMAIN, BINDING TO PEPTIDOGLYCANCategoriesFamily & Domains, FunctionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Bacteriol. 186:6728-6737 (2004)Cited in1
Three functional subdomains of the Escherichia coli FtsQ protein are involved in its interaction with the other division proteins.D'Ulisse V., Fagioli M., Ghelardini P., Paolozzi L.View abstractCited forINTERACTION WITH FTSQCategoryInteractionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCMicrobiology 153:124-138 (2007)Cited in51Mapped to3
Self-enhanced accumulation of FtsN at division sites and roles for other proteins with a SPOR domain (DamX, DedD, and RlpA) in Escherichia coli cell constriction.Gerding M.A., Liu B., Bendezu F.O., Hale C.A., Bernhardt T.G., de Boer P.A.View abstractCited forSUBCELLULAR LOCATION, DOMAINCategoriesFamily & Domains, Subcellular LocationSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Bacteriol. 191:7383-7401 (2009)Cited in4
Direct interactions of early and late assembling division proteins in Escherichia coli cells resolved by FRET.Alexeeva S., Gadella T.W. Jr., Verheul J., Verhoeven G.S., den Blaauwen T.View abstractCited forINTERACTION WITH ZAPA; FTSW AND FTSICategoryInteractionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCMol. Microbiol. 77:384-398 (2010)Cited in2
Role of Escherichia coli FtsN protein in the assembly and stability of the cell division ring.Rico A.I., Garcia-Ovalle M., Palacios P., Casanova M., Vicente M.View abstractCited forDISRUPTION PHENOTYPECategoryPhenotypes & VariantsSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCMol. Microbiol. 76:760-771 (2010)Cited in1
The early divisome protein FtsA interacts directly through its 1c subdomain with the cytoplasmic domain of the late divisome protein FtsN.Busiek K.K., Eraso J.M., Wang Y., Margolin W.View abstractCited forINTERACTION WITH FTSACategoryInteractionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Bacteriol. 194:1989-2000 (2012)Cited in2
Identification of SPOR domain amino acids important for septal localization, peptidoglycan binding, and a disulfide bond in the cell division protein FtsN.Duncan T.R., Yahashiri A., Arends S.J., Popham D.L., Weiss D.S.View abstractCited forDOMAIN, DISULFIDE BOND, MUTAGENESIS OF GLN-251; CYS-252; SER-254; THR-263; PHE-270; TRP-283; ARG-285; CYS-312 AND ILE-313CategoriesFamily & Domains, PTM / Processing, Phenotypes & VariantsSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Bacteriol. 195:5308-5315 (2013)Cited in1
A role for FtsA in SPOR-independent localization of the essential Escherichia coli cell division protein FtsN.Busiek K.K., Margolin W.View abstractCited forINTERACTION WITH FTSA, SUBCELLULAR LOCATION, DOMAINCategoriesFamily & Domains, Interaction, Subcellular LocationSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCMol. Microbiol. 92:1212-1226 (2014)Cited in2
A role for the FtsQLB complex in cytokinetic ring activation revealed by an ftsL allele that accelerates division.Tsang M.J., Bernhardt T.G.View abstractCited forFUNCTIONCategoryFunctionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCMol. Microbiol. 95:925-944 (2015)Cited in1
Roles for both FtsA and the FtsBLQ subcomplex in FtsN-stimulated cell constriction in Escherichia coli.Liu B., Persons L., Lee L., de Boer P.A.View abstractCited forFUNCTION, INTERACTION WITH FTSA, MUTAGENESIS OF TRP-83; TYR-85 AND LEU-89CategoriesFunction, Interaction, Phenotypes & VariantsSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCMol. Microbiol. 95:945-970 (2015)Cited in1
The bypass of ZipA by overexpression of FtsN requires a previously unknown conserved FtsN motif essential for FtsA-FtsN interaction supporting a model in which FtsA monomers recruit late cell division proteins to the Z ring.Pichoff S., Du S., Lutkenhaus J.View abstractCited forINTERACTION WITH FTSA, MUTAGENESIS OF ASP-5CategoriesInteraction, Phenotypes & VariantsSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCMol. Microbiol. 95:971-987 (2015)Cited in1
Last but not least: new insights into how FtsN triggers constriction during Escherichia coli cell division.Weiss D.S.View abstractCited forFUNCTION, REVIEWCategoryFunctionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCMol. Microbiol. 95:903-909 (2015)Cited in1
Solution structure and domain architecture of the divisome protein FtsN.Yang J.C., Van Den Ent F., Neuhaus D., Brevier J., Lowe J.View abstractCited forSTRUCTURE BY NMR OF 243-319, DOMAINCategoriesFamily & Domains, StructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCMol. Microbiol. 52:651-660 (2004)Cited in1
The bacterial cell division protein fragment <sup>E</sup>FtsN binds to and activates the major peptidoglycan synthase PBP1b.Boes A., Kerff F., Herman R., Touze T., Breukink E., Terrak M.View abstractCategoryStructureSourcePDB: 6YN0PubMedEurope PMCJ Biol Chem 295:18256-18265 (2020)Mapped to2
The binary protein-protein interaction landscape of Escherichia coli.Rajagopala S.V., Sikorski P., Kumar A., Mosca R., Vlasblom J., Arnold R., Franca-Koh J., Pakala S.B., Phanse S.[...], Uetz P.View abstractCategoryInteractionSourceIntAct: P29131PubMedEurope PMCNat Biotechnol 32:285-290 (2014)Mapped to99+