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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
  • 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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10344. ftsW.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 12CytoplasmicSequence analysisAdd BLAST12
Transmembranei13 – 33HelicalUniRule annotationAdd BLAST21
Topological domaini34 – 47PeriplasmicSequence analysisAdd BLAST14
Transmembranei48 – 68HelicalUniRule annotationAdd BLAST21
Topological domaini69 – 86CytoplasmicSequence analysisAdd BLAST18
Transmembranei87 – 107HelicalUniRule annotationAdd BLAST21
Topological domaini108 – 111PeriplasmicSequence analysis4
Transmembranei112 – 132HelicalUniRule annotationAdd BLAST21
Topological domaini133 – 174CytoplasmicSequence analysisAdd BLAST42
Transmembranei175 – 194HelicalUniRule annotationAdd BLAST20
Topological domaini195 – 197PeriplasmicSequence analysis3
Transmembranei198 – 217HelicalUniRule annotationAdd BLAST20
Topological domaini218 – 221CytoplasmicSequence analysis4
Transmembranei222 – 244HelicalUniRule annotationAdd BLAST23
Topological domaini245 – 301PeriplasmicSequence analysisAdd BLAST57
Transmembranei302 – 322HelicalUniRule annotationAdd BLAST21
Topological domaini323 – 342CytoplasmicSequence analysisAdd BLAST20
Transmembranei343 – 363HelicalUniRule annotationAdd BLAST21
Topological domaini364 – 373PeriplasmicSequence analysis10
Transmembranei374 – 394HelicalUniRule annotationAdd BLAST21
Topological domaini395 – 414CytoplasmicSequence analysisAdd BLAST20

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)DescriptionActionsGraphical viewLength
Mutagenesisi145R → A: Loss of flippase activity. Does not affect localization at the division site. 1 Publication1
Mutagenesisi150 – 152ELT → AAA: Does not affect flippase activity. 1 Publication3
Mutagenesisi153K → N: Loss of flippase activity. Does not affect localization at the division site. 1 Publication1
Mutagenesisi154 – 156LSL → AAA: Does not affect flippase activity. 1 Publication3
Mutagenesisi170E → K in ftsW201; TS; blocks division at the initiation stage. 1
Mutagenesisi172R → S: Does not affect localization, but affects its thermosensitivity. 1 Publication1
Mutagenesisi181P → L in ftsW1640; TS; blocks division at a late stage. 1
Mutagenesisi243R → Q: Lack of activity. 1 Publication1
Mutagenesisi253P → L in ftsW263; TS; blocks division at the initiation stage. 1
Mutagenesisi311G → D: Thermosensitive. Fails to localize to the division site at 42 degrees Celsius. 1 Publication1
Mutagenesisi368P → A: Cannot recruit FtsI at the division site; when associated with A-375. 1 Publication1
Mutagenesisi375P → A: Cannot recruit FtsI at the division site; when associated with A-368. 1 Publication1
Mutagenesisi402R → Q: Does not affect localization and activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000627001 – 414Lipid II flippase FtsWAdd BLAST414

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 interactors.
DIPiDIP-47989N.
IntActiP0ABG4. 10 interactors.
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.
OMAiVMYDRTL.
PhylomeDBiP0ABG4.

Family and domain databases

HAMAPiMF_00913. FtsW_proteobact. 1 hit.
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 interactors.
DIPiDIP-47989N.
IntActiP0ABG4. 10 interactors.
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.
OMAiVMYDRTL.
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. 1 hit.
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...

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: November 2, 2016
This is version 101 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.