ftsX

Functionⁱ

Part of the ABC transporter FtsEX involved in cellular division. Important for assembly or stability of the septal ring. Encoded in an operon consisting of genes ftsY, ftsE and ftsX.2 Publications

Miscellaneous

Overexpression leads to strong inhibition of growth, cell filamentation and eventually cell death.

GO - Biological processⁱ

cell cycle Source: UniProtKB-KW
cell division
Source: EcoliWiki
Inferred from mutant phenotypeⁱ
- 14729705

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Biological process	Cell cycle, Cell division

Biological process

Cell cycle, Cell division

Enzyme and pathway databases

BioCycⁱ	EcoCyc:FTSX-MONOMER

BioCycⁱ

EcoCyc:FTSX-MONOMER

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Cell division protein FtsX
Gene namesⁱ	Name:ftsX Synonyms:ftsS Ordered Locus Names:b3462, JW3427
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Organism-specific databases

EcoGeneⁱ	EG10345 ftsX

EcoGeneⁱ

EG10345 ftsX

Subcellular locationⁱ

Cell inner membrane
3 Publications
Manual assertion based on experiment inⁱ
- Ref.6
  "The Escherichia coli cell division proteins FtsY, FtsE and FtsX are inner membrane-associated."
  Gill D.R., Salmond G.P.
  Mol. Gen. Genet. 210:504-508(1987) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBCELLULAR LOCATION, OPERON STRUCTURE.
- Ref.7
  "Molecular characterization of Escherichia coli FtsE and FtsX."
  de Leeuw E., Graham B., Phillips G.J., ten Hagen-Jongman C.M., Oudega B., Luirink J.
  Mol. Microbiol. 31:983-993(1999) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, INTERACTION WITH FTSE, SUBCELLULAR LOCATION, OVEREXPRESSION.
- Ref.8
  "A predicted ABC transporter, FtsEX, is needed for cell division in Escherichia coli."
  Schmidt K.L., Peterson N.D., Kustusch R.J., Wissel M.C., Graham B., Phillips G.J., Weiss D.S.
  J. Bacteriol. 186:785-793(2004) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, SUBCELLULAR LOCATION.
; Multi-pass membrane protein
3 Publications
Manual assertion based on experiment inⁱ
- Ref.6
  "The Escherichia coli cell division proteins FtsY, FtsE and FtsX are inner membrane-associated."
  Gill D.R., Salmond G.P.
  Mol. Gen. Genet. 210:504-508(1987) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBCELLULAR LOCATION, OPERON STRUCTURE.
- Ref.7
  "Molecular characterization of Escherichia coli FtsE and FtsX."
  de Leeuw E., Graham B., Phillips G.J., ten Hagen-Jongman C.M., Oudega B., Luirink J.
  Mol. Microbiol. 31:983-993(1999) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, INTERACTION WITH FTSE, SUBCELLULAR LOCATION, OVEREXPRESSION.
- Ref.8
  "A predicted ABC transporter, FtsEX, is needed for cell division in Escherichia coli."
  Schmidt K.L., Peterson N.D., Kustusch R.J., Wissel M.C., Graham B., Phillips G.J., Weiss D.S.
  J. Bacteriol. 186:785-793(2004) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, SUBCELLULAR LOCATION.

Note:

Localizes to the septal ring at the later stages of cell growth and remains there until division is complete. This localization is dependent on localization of FtsZ, FtsA and ZipA, but not on the downstream division proteins FtsK, FtsQ or FtsI.

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	1 – 74	CytoplasmicSequence analysisAdd BLAST	74
Transmembraneⁱ	75 – 95	HelicalSequence analysisAdd BLAST	21
Topological domainⁱ	96 – 223	PeriplasmicSequence analysisAdd BLAST	128
Transmembraneⁱ	224 – 244	HelicalSequence analysisAdd BLAST	21
Topological domainⁱ	245 – 275	CytoplasmicSequence analysisAdd BLAST	31
Transmembraneⁱ	276 – 296	HelicalSequence analysisAdd BLAST	21
Topological domainⁱ	297 – 322	PeriplasmicSequence analysisAdd BLAST	26
Transmembraneⁱ	323 – 343	HelicalSequence analysisAdd BLAST	21
Topological domainⁱ	344 – 352	CytoplasmicSequence analysis	9

GO - Cellular componentⁱ

cell division site
Source: EcoliWiki
Inferred from direct assayⁱ
- 14729705
Gram-negative-bacterium-type cell wall
Source: UniProtKB
Inferred from direct assayⁱ
- 10048040
- 3323846
integral component of membrane
Source: EcoliWiki
Inferred from direct assayⁱ
- 10048040
plasma membrane
Source: EcoCyc
Inferred from direct assayⁱ
- 15919996
- 17309111

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechⁱ

Disruption phenotypeⁱ

Double deletion mutant FtsEX grows well on plates with LB medium with 1% NaCl forming healthy colonies at 30 degrees Celsius, whereas at 37 or 42 degrees Celsius, the colonies are very tiny and sick. In culture medium it exhibits mild elongation of cells at 30 degrees Celsius, and become very extensive at higher temperatures. This double mutant does not grow on LB culture medium without NaCl (LBON) at any temperature, possibly due to excessive lethal filamentation. Supplementation with any of a variety of osmolytes, such as glucose, sucrose, glycerol, or NaCl, completely rescues the growth on LBON medium. Though the growth is completely inhibited on LBON plates, the cultures grown in LBON broth show an initial increase in cell mass before the cessation of growth, and at this stage, the culture is extremely filamentous. The filaments grown in LB at 42 degrees Celsius or in LBON at 30 degrees Celsius are very long and appear to have elongated cells. They are normal and regularly spaced without any significant chromosomal aberrations or partition defects.1 Publication

Chemistry databases

ChEMBLⁱ	CHEMBL3309011

ChEMBLⁱ

CHEMBL3309011

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000166792	1 – 352	Cell division protein FtsXAdd BLAST		352

Proteomic databases

PaxDbⁱ	P0AC30
PRIDEⁱ	P0AC30

Interactionⁱ

Subunit structureⁱ

Forms a membrane-associated complex with FtsE.

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
envC	P37690	2	EBI-1119111,EBI-15948725

With

Entry

#Exp.

IntAct

Notes

envC

P37690

2

EBI-1119111,EBI-15948725

Protein-protein interaction databases

BioGridⁱ	4262498, 606 interactors
Database of interacting proteins More...DIPⁱ	DIP-35993N
IntActⁱ	P0AC30, 6 interactors
STRINGⁱ	316385.ECDH10B_3636

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	P0AC30
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the ABC-4 integral membrane protein family. FtsX subfamily.Curated

Keywords - Domainⁱ

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGⁱ	ENOG4105CRP Bacteria COG2177 LUCA
HOGENOMⁱ	HOG000270397
InParanoidⁱ	P0AC30
KEGG Orthology (KO) More...KOⁱ	K09811
PhylomeDBⁱ	P0AC30

Family and domain databases

InterProⁱ	View protein in InterPro IPR003838 ABC_permease_dom IPR004513 ABC_transpt_FtsX
PANTHERⁱ	PTHR30489:SF5 PTHR30489:SF5, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF02687 FtsX, 1 hit
PIRSFⁱ	PIRSF003097 FtsX, 1 hit
TIGRFAMsⁱ	TIGR00439 ftsX, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P0AC30-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MNKRDAINHI RQFGGRLDRF RKSVGGSGDG GRNAPKRAKS SPKPVNRKTN 
        60         70         80         90        100
VFNEQVRYAF HGALQDLKSK PFATFLTVMV IAISLTLPSV CYMVYKNVNQ 
       110        120        130        140        150
AATQYYPSPQ ITVYLQKTLD DDAAAGVVAQ LQAEQGVEKV NYLSREDALG 
       160        170        180        190        200
EFRNWSGFGG ALDMLEENPL PAVAVVIPKL DFQGTESLNT LRDRITQING 
       210        220        230        240        250
IDEVRMDDSW FARLAALTGL VGRVSAMIGV LMVAAVFLVI GNSVRLSIFA 
       260        270        280        290        300
RRDSINVQKL IGATDGFILR PFLYGGALLG FSGALLSLIL SEILVLRLSS 
       310        320        330        340        350
AVAEVAQVFG TKFDINGLSF DECLLLLLVC SMIGWVAAWL ATVQHLRHFT 

PE

Length:352

Mass (Da):38,544

Last modified:November 8, 2005 - v1

Checksum:ⁱC006ED56043739AE

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X04398 Genomic DNA Translation: CAA27986.1 U00039 Genomic DNA Translation: AAB18437.1 U00096 Genomic DNA Translation: AAC76487.1 AP009048 Genomic DNA Translation: BAE77831.1
PIRⁱ	S03132 CEECFX
NCBI Reference Sequences More...RefSeqⁱ	NP_417919.1, NC_000913.3 WP_001042003.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC76487; AAC76487; b3462 BAE77831; BAE77831; BAE77831
GeneIDⁱ	947969
KEGGⁱ	ecj:JW3427 eco:b3462
PATRICⁱ	fig\|511145.12.peg.3561

Protein	Similar proteins		Species	Score	Length	Source
P0AC30	Cell division protein FtsX		ECOL6		352	UniRef100_P0AC31
Cell division protein FtsX		SHIFL		352
Cell division protein FtsX		ECOLX		361
Cell division protein ftsX		Shigella dysenteriae WRSd3		361
Uncharacterized protein		Escherichia coli M056		361
+164

Protein	Similar proteins		Species	Score	Length	Source
P0AC30	Cell division protein FtsX		ECOL6		352	UniRef90_P0AC31
Cell division protein FtsX		SHIFL		352
Cell division protein FtsX		ECOLX		361
Cell division protein ftsX		Shigella dysenteriae WRSd3		361
Uncharacterized protein		Escherichia coli M056		361
+890

Protein	Similar proteins		Species	Score	Length	Source
P0AC30	Cell division protein FtsX		ECOL6		352	UniRef50_P0AC31
Cell division protein FtsX		SHIFL		352
Cell division protein FtsX		ECOLX		361
Cell division protein ftsX		Shigella dysenteriae WRSd3		361
Uncharacterized protein		Escherichia coli M056		361
+1583

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X04398 Genomic DNA Translation: CAA27986.1 U00039 Genomic DNA Translation: AAB18437.1 U00096 Genomic DNA Translation: AAC76487.1 AP009048 Genomic DNA Translation: BAE77831.1
PIRⁱ	S03132 CEECFX
RefSeqⁱ	NP_417919.1, NC_000913.3 WP_001042003.1, NZ_LN832404.1

3D structure databases

ProteinModelPortalⁱ	P0AC30
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4262498, 606 interactors
DIPⁱ	DIP-35993N
IntActⁱ	P0AC30, 6 interactors
STRINGⁱ	316385.ECDH10B_3636

Chemistry databases

ChEMBLⁱ	CHEMBL3309011

ChEMBLⁱ

CHEMBL3309011

Proteomic databases

PaxDbⁱ	P0AC30
PRIDEⁱ	P0AC30

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC76487; AAC76487; b3462 BAE77831; BAE77831; BAE77831
GeneIDⁱ	947969
KEGGⁱ	ecj:JW3427 eco:b3462
PATRICⁱ	fig\|511145.12.peg.3561

Organism-specific databases

EchoBASEⁱ	EB0341
EcoGeneⁱ	EG10345 ftsX

Phylogenomic databases

eggNOGⁱ	ENOG4105CRP Bacteria COG2177 LUCA
HOGENOMⁱ	HOG000270397
InParanoidⁱ	P0AC30
KOⁱ	K09811
PhylomeDBⁱ	P0AC30

Enzyme and pathway databases

BioCycⁱ	EcoCyc:FTSX-MONOMER

BioCycⁱ

EcoCyc:FTSX-MONOMER

Miscellaneous databases

Protein Ontology More...PROⁱ	PR:P0AC30

PROⁱ

PR:P0AC30

Family and domain databases

InterProⁱ	View protein in InterPro IPR003838 ABC_permease_dom IPR004513 ABC_transpt_FtsX
PANTHERⁱ	PTHR30489:SF5 PTHR30489:SF5, 1 hit
Pfamⁱ	View protein in Pfam PF02687 FtsX, 1 hit
PIRSFⁱ	PIRSF003097 FtsX, 1 hit
TIGRFAMsⁱ	TIGR00439 ftsX, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	FTSX_ECOLI
Accessionⁱ	P0AC30Primary (citable) accession number: P0AC30 Secondary accession number(s): P10122, Q2M7C5
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
	Last sequence update:	November 8, 2005
	Last modified:	November 7, 2018
	This is version 103 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome, Reference proteome

Documents

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

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P0AC30 (FTSX_ECOLI)

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Cell division protein FtsX

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

GO - Cellular componenti

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

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<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

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Functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ