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Protein

Lipid II flippase FtsW

Gene

ftsW

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential cell division protein. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane. Required for localization of FtsI. May play a role in the stabilization of the FtsZ ring during cell division.UniRule annotation3 Publications

GO - Molecular functioni

  • lipid-linked peptidoglycan transporter activity Source: EcoCyc

GO - Biological processi

  • cell division Source: EcoliWiki
  • cell wall organization Source: UniProtKB-KW
  • FtsZ-dependent cytokinesis Source: UniProtKB-HAMAP
  • lipid-linked peptidoglycan transport Source: GOC
  • peptidoglycan biosynthetic process Source: UniProtKB-KW
  • regulation of cell shape Source: EcoliWiki
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis, Transport

Enzyme and pathway databases

BioCyciEcoCyc:EG10344-MONOMER.
ECOL316407:JW0087-MONOMER.
MetaCyc:EG10344-MONOMER.

Protein family/group databases

TCDBi2.A.103.1.1. the bacterial murein precursor exporter (mpe) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipid II flippase FtsW
Alternative name(s):
Cell division protein FtsWUniRule annotation
Gene namesi
Name:ftsWUniRule annotation
Ordered Locus Names:b0089, JW0087
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10344. ftsW.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1212CytoplasmicSequence analysisAdd
BLAST
Transmembranei13 – 3321HelicalUniRule annotationAdd
BLAST
Topological domaini34 – 4714PeriplasmicSequence analysisAdd
BLAST
Transmembranei48 – 6821HelicalUniRule annotationAdd
BLAST
Topological domaini69 – 8618CytoplasmicSequence analysisAdd
BLAST
Transmembranei87 – 10721HelicalUniRule annotationAdd
BLAST
Topological domaini108 – 1114PeriplasmicSequence analysis
Transmembranei112 – 13221HelicalUniRule annotationAdd
BLAST
Topological domaini133 – 17442CytoplasmicSequence analysisAdd
BLAST
Transmembranei175 – 19420HelicalUniRule annotationAdd
BLAST
Topological domaini195 – 1973PeriplasmicSequence analysis
Transmembranei198 – 21720HelicalUniRule annotationAdd
BLAST
Topological domaini218 – 2214CytoplasmicSequence analysis
Transmembranei222 – 24423HelicalUniRule annotationAdd
BLAST
Topological domaini245 – 30157PeriplasmicSequence analysisAdd
BLAST
Transmembranei302 – 32221HelicalUniRule annotationAdd
BLAST
Topological domaini323 – 34220CytoplasmicSequence analysisAdd
BLAST
Transmembranei343 – 36321HelicalUniRule annotationAdd
BLAST
Topological domaini364 – 37310PeriplasmicSequence analysis
Transmembranei374 – 39421HelicalUniRule annotationAdd
BLAST
Topological domaini395 – 41420CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell division site Source: EcoliWiki
  • integral component of plasma membrane Source: EcoCyc
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi145 – 1451R → A: Loss of flippase activity. Does not affect localization at the division site. 1 Publication
Mutagenesisi150 – 1523ELT → AAA: Does not affect flippase activity. 1 Publication
Mutagenesisi153 – 1531K → N: Loss of flippase activity. Does not affect localization at the division site. 1 Publication
Mutagenesisi154 – 1563LSL → AAA: Does not affect flippase activity. 1 Publication
Mutagenesisi170 – 1701E → K in ftsW201; TS; blocks division at the initiation stage.
Mutagenesisi172 – 1721R → S: Does not affect localization, but affects its thermosensitivity. 1 Publication
Mutagenesisi181 – 1811P → L in ftsW1640; TS; blocks division at a late stage.
Mutagenesisi243 – 2431R → Q: Lack of activity. 1 Publication
Mutagenesisi253 – 2531P → L in ftsW263; TS; blocks division at the initiation stage.
Mutagenesisi311 – 3111G → D: Thermosensitive. Fails to localize to the division site at 42 degrees Celsius. 1 Publication
Mutagenesisi368 – 3681P → A: Can not recruit FtsI at the division site; when associated with A-375. 1 Publication
Mutagenesisi375 – 3751P → A: Can not recruit FtsI at the division site; when associated with A-368. 1 Publication
Mutagenesisi402 – 4021R → Q: Does not affect localization and activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 414414Lipid II flippase FtsWPRO_0000062700Add
BLAST

Proteomic databases

PaxDbiP0ABG4.
PRIDEiP0ABG4.

Interactioni

Subunit structurei

Forms a complex with FtsI. Interacts also with FtsL, FtsQ and FtsN.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ftsIP0AD687EBI-1214767,EBI-548564
ftsNP291313EBI-1214767,EBI-1134233
ftsQP061363EBI-1214767,EBI-1130157

Protein-protein interaction databases

BioGridi4261096. 481 interactions.
DIPiDIP-47989N.
IntActiP0ABG4. 10 interactions.
STRINGi511145.b0089.

Structurei

3D structure databases

ProteinModelPortaliP0ABG4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The periplasmic loop between transmembrane domains 7 and 8 is essential for activity and the loop between transmembrane domains 9 and 10 is involved in the recruitment of FtsI at the division site.1 Publication

Sequence similaritiesi

Belongs to the SEDS family. FtsW subfamily.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105CNI. Bacteria.
COG0772. LUCA.
HOGENOMiHOG000282689.
InParanoidiP0ABG4.
KOiK03588.
OMAiNPWADPT.
OrthoDBiEOG68M4JQ.
PhylomeDBiP0ABG4.

Family and domain databases

HAMAPiMF_00913. FtsW_proteobact.
InterProiIPR018365. Cell_cycle_FtsW-rel_CS.
IPR001182. Cell_cycle_FtsW/RodA.
IPR013437. FtsW.
[Graphical view]
PANTHERiPTHR30474. PTHR30474. 1 hit.
PfamiPF01098. FTSW_RODA_SPOVE. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02614. ftsW. 1 hit.
PROSITEiPS00428. FTSW_RODA_SPOVE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0ABG4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLSLPRLKM PRLPGFSILV WISTALKGWV MGSREKDTDS LIMYDRTLLW
60 70 80 90 100
LTFGLAAIGF IMVTSASMPI GQRLTNDPFF FAKRDGVYLI LAFILAIITL
110 120 130 140 150
RLPMEFWQRY SATMLLGSII LLMIVLVVGS SVKGASRWID LGLLRIQPAE
160 170 180 190 200
LTKLSLFCYI ANYLVRKGDE VRNNLRGFLK PMGVILVLAV LLLAQPDLGT
210 220 230 240 250
VVVLFVTTLA MLFLAGAKLW QFIAIIGMGI SAVVLLILAE PYRIRRVTAF
260 270 280 290 300
WNPWEDPFGS GYQLTQSLMA FGRGELWGQG LGNSVQKLEY LPEAHTDFIF
310 320 330 340 350
AIIGEELGYV GVVLALLMVF FVAFRAMSIG RKALEIDHRF SGFLACSIGI
360 370 380 390 400
WFSFQALVNV GAAAGMLPTK GLTLPLISYG GSSLLIMSTA IMMLLRIDYE
410
TRLEKAQAFV RGSR
Length:414
Mass (Da):45,987
Last modified:October 25, 2005 - v1
Checksum:i7935EC952AD9A1F3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30807 Genomic DNA. Translation: AAA83859.1.
X55034 Genomic DNA. Translation: CAA38866.1.
U00096 Genomic DNA. Translation: AAC73200.1.
AP009048 Genomic DNA. Translation: BAB96657.1.
X52644 Genomic DNA. Translation: CAA36866.1.
PIRiA32581. CEECFW.
RefSeqiNP_414631.1. NC_000913.3.
WP_001295532.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73200; AAC73200; b0089.
BAB96657; BAB96657; BAB96657.
GeneIDi946322.
KEGGiecj:JW0087.
eco:b0089.
PATRICi32115283. VBIEscCol129921_0093.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30807 Genomic DNA. Translation: AAA83859.1.
X55034 Genomic DNA. Translation: CAA38866.1.
U00096 Genomic DNA. Translation: AAC73200.1.
AP009048 Genomic DNA. Translation: BAB96657.1.
X52644 Genomic DNA. Translation: CAA36866.1.
PIRiA32581. CEECFW.
RefSeqiNP_414631.1. NC_000913.3.
WP_001295532.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP0ABG4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261096. 481 interactions.
DIPiDIP-47989N.
IntActiP0ABG4. 10 interactions.
STRINGi511145.b0089.

Protein family/group databases

TCDBi2.A.103.1.1. the bacterial murein precursor exporter (mpe) family.

Proteomic databases

PaxDbiP0ABG4.
PRIDEiP0ABG4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73200; AAC73200; b0089.
BAB96657; BAB96657; BAB96657.
GeneIDi946322.
KEGGiecj:JW0087.
eco:b0089.
PATRICi32115283. VBIEscCol129921_0093.

Organism-specific databases

EchoBASEiEB0340.
EcoGeneiEG10344. ftsW.

Phylogenomic databases

eggNOGiENOG4105CNI. Bacteria.
COG0772. LUCA.
HOGENOMiHOG000282689.
InParanoidiP0ABG4.
KOiK03588.
OMAiNPWADPT.
OrthoDBiEOG68M4JQ.
PhylomeDBiP0ABG4.

Enzyme and pathway databases

BioCyciEcoCyc:EG10344-MONOMER.
ECOL316407:JW0087-MONOMER.
MetaCyc:EG10344-MONOMER.

Miscellaneous databases

PROiP0ABG4.

Family and domain databases

HAMAPiMF_00913. FtsW_proteobact.
InterProiIPR018365. Cell_cycle_FtsW-rel_CS.
IPR001182. Cell_cycle_FtsW/RodA.
IPR013437. FtsW.
[Graphical view]
PANTHERiPTHR30474. PTHR30474. 1 hit.
PfamiPF01098. FTSW_RODA_SPOVE. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02614. ftsW. 1 hit.
PROSITEiPS00428. FTSW_RODA_SPOVE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structural similarity among Escherichia coli FtsW and RodA proteins and Bacillus subtilis SpoVE protein, which function in cell division, cell elongation, and spore formation, respectively."
    Ikeda M., Sato T., Wachi M., Jung H.K., Ishino F., Kobayashi Y., Matsuhashi M.
    J. Bacteriol. 171:6375-6378(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region."
    Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.
    Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  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., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Nucleotide sequence involving murG and murC in the mra gene cluster region of Escherichia coli."
    Ikeda M., Wachi M., Jung H.K., Ishino F., Matsuhashi M.
    Nucleic Acids Res. 18:4014-4014(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 388-414.
    Strain: K12.
  6. Cited for: FUNCTION.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  7. "Identification of FtsW and characterization of a new ftsW division mutant of Escherichia coli."
    Khattar M.M., Begg K.J., Donachie W.D.
    J. Bacteriol. 176:7140-7147(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MUTANT ALLELE FTSW201.
    Strain: K12.
  8. "Two polypeptide products of the Escherichia coli cell division gene ftsW and a possible role for FtsW in FtsZ function."
    Khattar M.M., Addinall S.G., Stedul K.H., Boyle D.S., Lutkenhaus J., Donachie W.D.
    J. Bacteriol. 179:784-793(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MUTANT ALLELES FTSW263 AND FTSW1640.
    Strain: K12.
  9. "FtsI and FtsW are localized to the septum in Escherichia coli."
    Wang L., Khattar M.K., Donachie W.D., Lutkenhaus J.
    J. Bacteriol. 180:2810-2816(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
    Strain: K12.
  10. "Topological characterization of the essential Escherichia coli cell division protein FtsW."
    Lara B., Ayala J.A.
    FEMS Microbiol. Lett. 216:23-32(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TOPOLOGY.
  11. "The Escherichia coli cell division protein FtsW is required to recruit its cognate transpeptidase, FtsI (PBP3), to the division site."
    Mercer K.L., Weiss D.S.
    J. Bacteriol. 184:904-912(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
    Strain: K12.
  12. Cited for: DOMAIN, MUTAGENESIS OF ARG-172; ARG-243; GLY-311; PRO-368; PRO-375 AND ARG-402.
  13. "Interaction network among Escherichia coli membrane proteins involved in cell division as revealed by bacterial two-hybrid analysis."
    Karimova G., Dautin N., Ladant D.
    J. Bacteriol. 187:2233-2243(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FTSI; FTSL; FTSQ AND FTSN.
    Strain: K12.
  14. "Global topology analysis of the Escherichia coli inner membrane proteome."
    Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
    Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: K12 / MG1655 / ATCC 47076.
  15. "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.
    Microbiology 153:124-138(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FTSQ.
    Strain: K12.
  16. "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.
    Mol. Microbiol. 77:384-398(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FTSN.
  17. "Identification of FtsW as a transporter of lipid-linked cell wall precursors across the membrane."
    Mohammadi T., van Dam V., Sijbrandi R., Vernet T., Zapun A., Bouhss A., Diepeveen-de Bruin M., Nguyen-Disteche M., de Kruijff B., Breukink E.
    EMBO J. 30:1425-1432(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A FLIPPASE.
  18. "The integral membrane FtsW protein and peptidoglycan synthase PBP3 form a subcomplex in Escherichia coli."
    Fraipont C., Alexeeva S., Wolf B., van der Ploeg R., Schloesser M., den Blaauwen T., Nguyen-Disteche M.
    Microbiology 157:251-259(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FTSI.
  19. Cited for: FUNCTION AS A FLIPPASE, MUTAGENESIS OF ARG-145; 150-GLU--THR-152; LYS-153 AND 154-LEU--LEU-156.

Entry informationi

Entry nameiFTSW_ECOLI
AccessioniPrimary (citable) accession number: P0ABG4
Secondary accession number(s): P16457
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 25, 2005
Last modified: May 11, 2016
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

MurJ (AC P0AF16) is also proposed to act as a lipid II flippase. The identity of the lipid II flippase is controversial with conflicting in vivo and in vitro results.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.