ftsL

Functionⁱ

Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. Can also mediate Zn²⁺-sensitivity probably by increasing the permeability of the inner membrane.UniRule annotation3 Publications

GO - Biological processⁱ

FtsZ-dependent cytokinesis
Source: EcoCyc
Inferred from mutant phenotypeⁱ
- 1332942

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:EG11086-MONOMER

BioCycⁱ

EcoCyc:EG11086-MONOMER

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Cell division protein FtsLUniRule annotation
Gene namesⁱ	Name:ftsLUniRule annotation Synonyms:mraR, yabD Ordered Locus Names:b0083, JW0081
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	EG11086 ftsL

EcoGeneⁱ

EG11086 ftsL

Subcellular locationⁱ

Cell inner membrane
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_00910
5 Publications
Manual assertion based on experiment inⁱ
- Ref.1
  "FtsL, an essential cytoplasmic membrane protein involved in cell division in Escherichia coli."
  Guzman L.-M., Barondess J.J., Beckwith J.
  J. Bacteriol. 174:7716-7728(1992) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, TOPOLOGY, DISRUPTION PHENOTYPE.
- Ref.8
  "Localization of FtsL to the Escherichia coli septal ring."
  Ghigo J.M., Weiss D.S., Chen J.C., Yarrow J.C., Beckwith J.
  Mol. Microbiol. 31:725-737(1999) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBCELLULAR LOCATION.
- Ref.10
  "FtsQ, FtsL and FtsI require FtsK, but not FtsN, for co-localization with FtsZ during Escherichia coli cell division."
  Chen J.C., Beckwith J.
  Mol. Microbiol. 42:395-413(2001) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBCELLULAR LOCATION.
- Ref.11
  "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.
  J. Bacteriol. 184:2552-2556(2002) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBCELLULAR LOCATION.
- Ref.12
  "A complex of the Escherichia coli cell division proteins FtsL, FtsB and FtsQ forms independently of its localization to the septal region."
  Buddelmeijer N., Beckwith J.
  Mol. Microbiol. 52:1315-1327(2004) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBUNIT, SUBCELLULAR LOCATION.
; Single-pass type II membrane protein
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_00910
5 Publications
Manual assertion based on experiment inⁱ
- Ref.1
  "FtsL, an essential cytoplasmic membrane protein involved in cell division in Escherichia coli."
  Guzman L.-M., Barondess J.J., Beckwith J.
  J. Bacteriol. 174:7716-7728(1992) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, TOPOLOGY, DISRUPTION PHENOTYPE.
- Ref.8
  "Localization of FtsL to the Escherichia coli septal ring."
  Ghigo J.M., Weiss D.S., Chen J.C., Yarrow J.C., Beckwith J.
  Mol. Microbiol. 31:725-737(1999) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBCELLULAR LOCATION.
- Ref.10
  "FtsQ, FtsL and FtsI require FtsK, but not FtsN, for co-localization with FtsZ during Escherichia coli cell division."
  Chen J.C., Beckwith J.
  Mol. Microbiol. 42:395-413(2001) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBCELLULAR LOCATION.
- Ref.11
  "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.
  J. Bacteriol. 184:2552-2556(2002) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBCELLULAR LOCATION.
- Ref.12
  "A complex of the Escherichia coli cell division proteins FtsL, FtsB and FtsQ forms independently of its localization to the septal region."
  Buddelmeijer N., Beckwith J.
  Mol. Microbiol. 52:1315-1327(2004) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBUNIT, SUBCELLULAR LOCATION.

Note:

Localizes to the division septum where it forms a ring structure. Localization requires FtsZ, FtsA, ZipA, FtsK, FtsQ and FtsB, but not FtsI and FtsN. Localization of FtsB and FtsL is codependent.

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	1 – 34	CytoplasmicUniRule annotationAdd BLAST	34
Transmembraneⁱ	35 – 57	HelicalUniRule annotationAdd BLAST	23
Topological domainⁱ	58 – 121	PeriplasmicUniRule annotationAdd BLAST	64

GO - Cellular componentⁱ

cell division site
Source: EcoCyc
Inferred from direct assayⁱ
- 10613870
integral component of plasma membrane
Source: EcoCyc
Inferred from direct assayⁱ
- 1332942

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechⁱ

Disruption phenotypeⁱ

Mutants show inhibition of cell division, formation of long, nonseptate filaments, ultimate cessation of growth and lysis.1 Publication

Mutagenesis

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Mutagenesisⁱ	70	L → H: Impairs both localization and function, and reduces the efficiency of dimerization. 1 Publication		1
Mutagenesisⁱ	84	L → D: Impairs both localization and function, and reduces the efficiency of dimerization. 1 Publication		1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000087371	1 – 121	Cell division protein FtsLAdd BLAST		121

Proteomic databases

PaxDbⁱ	P0AEN4
PRIDEⁱ	P0AEN4

Interactionⁱ

Subunit structureⁱ

Part of a complex composed of FtsB, FtsL and FtsQ. The complex can be formed before its localization to the division site. This tripartite complex can be divided further into a subcomplex of FtsB and FtsL, which forms in the absence of FtsQ. Interacts also with FtsI, FtsN and YmgF. Homodimer in vitro. May form multimers.UniRule annotation5 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
blr	P56976	3	EBI-1119082,EBI-6419495
ftsB	P0A6S5	18	EBI-1119082,EBI-1113953
ftsI	P0AD68	4	EBI-1119082,EBI-548564
ftsQ	P06136	11	EBI-1119082,EBI-1130157
ymgF	P58034	3	EBI-1119082,EBI-1214577

Show more details

Protein-protein interaction databases

BioGridⁱ	4261638, 332 interactors
ComplexPortalⁱ	CPX-3099 FtsQBL complex CPX-3299 FtsBL complex
Database of interacting proteins More...DIPⁱ	DIP-47987N
IntActⁱ	P0AEN4, 17 interactors
Molecular INTeraction database More...MINTⁱ	P0AEN4
STRINGⁱ	316385.ECDH10B_0065

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	P0AEN4
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Coiled coil

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Coiled coilⁱ	63 – 91	Sequence analysisAdd BLAST		29

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	58 – 85	Leucine zipper-likeAdd BLAST		28

Domainⁱ

The cytoplasmic region is involved in recruitment of the downstream cell division protein FtsW. The transmembrane segment and the membrane-proximal periplasmic region form a coiled-coil structure and are required for septal localization and interaction with FtsB. The C-terminal region is required for interaction with FtsQ. Contains a leucine zipper-like (LZ) motif, which is required for optimal interaction with FtsB.2 Publications

Sequence similaritiesⁱ

Belongs to the FtsL family.UniRule annotation

Keywords - Domainⁱ

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGⁱ	ENOG41063Y6 Bacteria COG3116 LUCA
HOGENOMⁱ	HOG000255861
InParanoidⁱ	P0AEN4
KEGG Orthology (KO) More...KOⁱ	K03586
OMAⁱ	DLWHHKW

Family and domain databases

HAMAPⁱ	MF_00910 FtsL, 1 hit
InterProⁱ	View protein in InterPro IPR011922 Cell_div_FtsL
PANTHERⁱ	PTHR37479 PTHR37479, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF04999 FtsL, 1 hit
TIGRFAMsⁱ	TIGR02209 ftsL_broad, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P0AEN4-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MISRVTEALS KVKGSMGSHE RHALPGVIGD DLLRFGKLPL CLFICIILTA 
        60         70         80         90        100
VTVVTTAHHT RLLTAQREQL VLERDALDIE WRNLILEENA LGDHSRVERI 
       110        120 
ATEKLQMQHV DPSQENIVVQ K

Length:121

Mass (Da):13,627

Last modified:December 20, 2005 - v1

Checksum:ⁱ6DD5DF7B2ECB7090

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	S49875 Genomic DNA Translation: AAB24309.1 S49802 Genomic DNA Translation: AAB24311.1 X55034 Genomic DNA Translation: CAA38860.1 U00096 Genomic DNA Translation: AAC73194.1 AP009048 Genomic DNA Translation: BAB96651.2 K00137 Genomic DNA Translation: AAA24299.1 X52063 Genomic DNA Translation: CAA36285.1
PIRⁱ	A45278
NCBI Reference Sequences More...RefSeqⁱ	NP_414625.1, NC_000913.3 WP_000625658.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC73194; AAC73194; b0083 BAB96651; BAB96651; BAB96651
GeneIDⁱ	944803
KEGGⁱ	ecj:JW0081 eco:b0083
PATRICⁱ	fig\|1411691.4.peg.2197

Protein	Similar proteins		Species	Score	Length
P0AEN4	Peptidoglycan D,D-transpeptidase FtsI		ECO57		588
Peptidoglycan D,D-transpeptidase FtsI		ECOLI		588
Peptidoglycan D,D-transpeptidase FtsI		Escherichia coli NCCP15648		588
Peptidoglycan D,D-transpeptidase FtsI		Klebsiella pneumoniae IS22		588
Peptidoglycan D,D-transpeptidase FtsI		Escherichia coli D6-113.11		588
+313

Protein	Similar proteins		Species	Score	Length
P0AEN4	Peptidoglycan D,D-transpeptidase FtsI		ECO57		588
Peptidoglycan D,D-transpeptidase FtsI		ECOLI		588
Peptidoglycan D,D-transpeptidase FtsI		Escherichia coli NCCP15648		588
Peptidoglycan D,D-transpeptidase FtsI		Klebsiella pneumoniae IS22		588
Peptidoglycan D,D-transpeptidase FtsI		Escherichia coli D6-113.11		588
+1400

Protein	Similar proteins		Species	Score	Length
P0AEN4	Peptidoglycan D,D-transpeptidase FtsI		ECO57		588
Peptidoglycan D,D-transpeptidase FtsI		ECOLI		588
Peptidoglycan D,D-transpeptidase FtsI		Escherichia coli NCCP15648		588
Peptidoglycan D,D-transpeptidase FtsI		Klebsiella pneumoniae IS22		588
Peptidoglycan D,D-transpeptidase FtsI		Escherichia coli D6-113.11		588
+3849

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	S49875 Genomic DNA Translation: AAB24309.1 S49802 Genomic DNA Translation: AAB24311.1 X55034 Genomic DNA Translation: CAA38860.1 U00096 Genomic DNA Translation: AAC73194.1 AP009048 Genomic DNA Translation: BAB96651.2 K00137 Genomic DNA Translation: AAA24299.1 X52063 Genomic DNA Translation: CAA36285.1
PIRⁱ	A45278
NCBI Reference Sequences More...RefSeqⁱ	NP_414625.1, NC_000913.3 WP_000625658.1, NZ_LN832404.1

3D structure databases

ProteinModelPortalⁱ	P0AEN4
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4261638, 332 interactors
ComplexPortalⁱ	CPX-3099 FtsQBL complex CPX-3299 FtsBL complex
Database of interacting proteins More...DIPⁱ	DIP-47987N
IntActⁱ	P0AEN4, 17 interactors
Molecular INTeraction database More...MINTⁱ	P0AEN4
STRINGⁱ	316385.ECDH10B_0065

Proteomic databases

PaxDbⁱ	P0AEN4
PRIDEⁱ	P0AEN4

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC73194; AAC73194; b0083 BAB96651; BAB96651; BAB96651
GeneIDⁱ	944803
KEGGⁱ	ecj:JW0081 eco:b0083
PATRICⁱ	fig\|1411691.4.peg.2197

Organism-specific databases

EchoBASEⁱ	EB1078
EcoGeneⁱ	EG11086 ftsL

Phylogenomic databases

eggNOGⁱ	ENOG41063Y6 Bacteria COG3116 LUCA
HOGENOMⁱ	HOG000255861
InParanoidⁱ	P0AEN4
KEGG Orthology (KO) More...KOⁱ	K03586
OMAⁱ	DLWHHKW

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG11086-MONOMER

BioCycⁱ

EcoCyc:EG11086-MONOMER

Miscellaneous databases

Protein Ontology More...PROⁱ	PR:P0AEN4

PROⁱ

PR:P0AEN4

Family and domain databases

HAMAPⁱ	MF_00910 FtsL, 1 hit
InterProⁱ	View protein in InterPro IPR011922 Cell_div_FtsL
PANTHERⁱ	PTHR37479 PTHR37479, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF04999 FtsL, 1 hit
TIGRFAMsⁱ	TIGR02209 ftsL_broad, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	FTSL_ECOLI
Accessionⁱ	P0AEN4Primary (citable) accession number: P0AEN4 Secondary accession number(s): P22187, Q8KMX6
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
	Last sequence update:	December 20, 2005
	Last modified:	June 20, 2018
	This is version 99 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

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

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P0AEN4 (FTSL_ECOLI)

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Cell division protein FtsL

Select a section on the left to see content.

<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

<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

<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 - 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

Mutagenesis

<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

Coiled coil

Motif

<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

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

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Sequence databases

3D structure databases

Protein-protein interaction 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

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<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

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ