UniProtKB - P29131 (FTSN_ECOLI)

BLAST

>sp|P29131|FTSN_ECOLI Cell division protein FtsN OS=Escherichia coli (strain K12) OX=83333 GN=ftsN PE=1 SV=3
MAQRDYVRRSQPAPSRRKKSTSRKKQRNLPAVSPAMVAIAAAVLVTFIGGLYFITHHKKE
ESETLQSQKVTGNGLPPKPEERWRYIKELESRQPGVRAPTEPSAGGEVKTPEQLTPEQRQ
LLEQMQADMRQQPTQLVEVPWNEQTPEQRQQTLQRQRQAQQLAEQQRLAQQSRTTEQSWQ
QQTRTSQAAPVQAQPRQSKPASSQQPYQDLLQTPAHTTAQSKPQQAAPVARAADAPKPTA
EKKDERRWMVQCGSFRGAEQAETVRAQLAFEGFDSKITTNNGWNRVVIGPVKGKENADST
LNRLKMAGHTNCIRLAAGG

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History
Entry version 158 (07 Nov 2018)
Sequence version 3 (29 Aug 2003)
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Protein

Cell division protein FtsN

Gene

ftsN

Organism

Escherichia coli (strain K12)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Essential cell division protein that activates septal peptidoglycan synthesis and constriction of the cell. Acts on both sides of the membrane, via interaction with FtsA in the cytoplasm and interaction with the FtsQBL complex in the periplasm. These interactions may induce a conformational switch in both FtsA and FtsQBL, leading to septal peptidoglycan synthesis by FtsI and associated synthases (Probable) (PubMed:25496160). Required for full FtsI activity (PubMed:25496160). Required for recruitment of AmiC to the septal ring (PubMed:12787347).2 Publications2 Publications

GO - Molecular functionⁱ

peptidoglycan binding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cell division
Source: CACAO
Inferred from direct assayⁱ
- 8509333
cytokinetic process
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
division septum assembly
Source: EcoCyc
Inferred from mutant phenotypeⁱ
- 9282742
FtsZ-dependent cytokinesis Source: UniProtKB-UniRule

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Biological process	Cell cycle, Cell division, Septation

Biological process

Cell cycle, Cell division, Septation

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG11529-MONOMER MetaCyc:EG11529-MONOMER

BioCycⁱ

EcoCyc:EG11529-MONOMER
MetaCyc:EG11529-MONOMER

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Cell division protein FtsNUniRule annotationCurated
Gene namesⁱ	Name:ftsNUniRule annotation Synonyms:msgA Ordered Locus Names:b3933, JW3904
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	EG11529 ftsN

EcoGeneⁱ

EG11529 ftsN

Subcellular locationⁱ

Cell inner membrane
1 Publication
Manual assertion based on experiment inⁱ
- Ref.6
  "Topological characterization of the essential Escherichia coli cell division protein FtsN."
  Dai K., Xu Y., Lutkenhaus J.
  J. Bacteriol. 178:1328-1334(1996) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBCELLULAR LOCATION, TOPOLOGY.
; Single-pass type II membrane protein
1 Publication
Manual assertion based on experiment inⁱ
- Ref.6
  "Topological characterization of the essential Escherichia coli cell division protein FtsN."
  Dai K., Xu Y., Lutkenhaus J.
  J. Bacteriol. 178:1328-1334(1996) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBCELLULAR LOCATION, TOPOLOGY.

Note:

Localizes to the septum (PubMed:9282742, PubMed:19684127, PubMed:24750258). Localizes to the midcell via interaction with the early cell division protein FtsA and via the periplasmic SPOR domain (PubMed:9282742, PubMed:19684127, PubMed:24750258). FtsA-dependent localization precedes SPOR-dependent localization, and both are needed for efficient localization (PubMed:24750258). Localization depends upon FtsZ, FtsA, ZipA, FtsQ and FtsI (PubMed:9282742, PubMed:11948172).4 Publications

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	1 – 33	CytoplasmicUniRule annotation1 PublicationAdd BLAST	33
Transmembraneⁱ	34 – 54	HelicalUniRule annotationAdd BLAST	21
Topological domainⁱ	55 – 319	PeriplasmicUniRule annotation1 PublicationAdd BLAST	265

GO - Cellular componentⁱ

cell division site
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
cell septum
Source: EcoCyc
Inferred from direct assayⁱ
- 9282742
integral component of plasma membrane
Source: EcoCyc
Inferred from direct assayⁱ
- 8631709
plasma membrane
Source: EcoCyc
Inferred from direct assayⁱ
- 17309111

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechⁱ

Disruption phenotypeⁱ

Depletion does not affect localization of FtsZ, FtsA, ZipA, FtsQ, FtsL and FtsI to the division site (PubMed:11703663). Cells containing low levels of FtsN stop dividing while their mean cell length increases (PubMed:20345660). Absence of FtsN is followed by an inverse sequential disassembly of already assembled divisome compounds (PubMed:20345660).2 Publications

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	5	D → N: Causes significant impairment of the interaction with FtsA. 1 Publication	1
Mutagenesisⁱ	83	W → L or T: Lack of activity. 1 Publication	1
Mutagenesisⁱ	85	Y → S or W: Lack of activity. 1 Publication	1
Mutagenesisⁱ	89	L → S: Lack of activity. 1 Publication	1
Mutagenesisⁱ	251	Q → A: Reduces septal localization by a factor of at least 3. 1 Publication	1
Mutagenesisⁱ	251	Q → E: Severe localization defects. Binds peptidoglycan poorly. 1 Publication	1
Mutagenesisⁱ	252	C → A: Severely reduces stability of the protein. 1 Publication	1
Mutagenesisⁱ	254	S → A: Reduces septal localization by a factor of at least 3. 1 Publication	1
Mutagenesisⁱ	254	S → E: Binds peptidoglycan poorly. 1 Publication	1
Mutagenesisⁱ	263	T → D: Intermediate localization defects. 1 Publication	1
Mutagenesisⁱ	270	F → A: Intermediate localization defects. 1 Publication	1
Mutagenesisⁱ	283	W → A: Reduces septal localization by a factor of at least 3. 1 Publication	1
Mutagenesisⁱ	283	W → D: Severe localization defects. 1 Publication	1
Mutagenesisⁱ	285	R → A: Reduces septal localization by a factor of at least 3. Binds peptidoglycan poorly. 1 Publication	1
Mutagenesisⁱ	312	C → A: Severely reduces stability of the protein. 1 Publication	1
Mutagenesisⁱ	313	I → A: Reduces septal localization by a factor of at least 3. 1 Publication	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000087376	1 – 319	Cell division protein FtsNAdd BLAST		319

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Disulfide bondⁱ	252 ↔ 312	UniRule annotation1 Publication

Keywords - PTMⁱ

Disulfide bond

Proteomic databases

PaxDbⁱ	P29131
PRIDEⁱ	P29131

Interactionⁱ

Subunit structureⁱ

Interacts with FtsA via its N-terminal cytoplasmic domain (PubMed:22328664, PubMed:24750258, PubMed:25496160, PubMed:25496259). Interacts with ZapA, FtsQ, FtsW and FtsI (PubMed:17185541, PubMed:20497333).6 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
blr	P56976	3	EBI-1134233,EBI-6419495
ftsA	P0ABH0	7	EBI-1134233,EBI-550562
ftsI	P0AD68	3	EBI-1134233,EBI-548564
ftsQ	P06136	7	EBI-1134233,EBI-1130157
ftsW	P0ABG4	3	EBI-1134233,EBI-1214767
mrcB	P02919	7	EBI-1134233,EBI-909769

Protein-protein interaction databases

BioGridⁱ	4261592, 198 interactors
Database of interacting proteins More...DIPⁱ	DIP-9705N
IntActⁱ	P29131, 24 interactors
Molecular INTeraction database More...MINTⁱ	P29131
STRINGⁱ	316385.ECDH10B_4122

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	254 – 256	Combined sources	3
Helixⁱ	258 – 271	Combined sources	14
Beta strandⁱ	275 – 279	Combined sources	5
Beta strandⁱ	281 – 290	Combined sources	10
Turnⁱ	293 – 295	Combined sources	3
Helixⁱ	296 – 307	Combined sources	12

Show more details

3D structure databases

ProteinModelPortalⁱ	P29131
SMRⁱ	P29131
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P29131

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Repeatⁱ	115 – 120	1-1	6
Repeatⁱ	145 – 150	1-2	6
Repeatⁱ	197 – 200	2-1	4
Repeatⁱ	220 – 223	2-2	4
Domainⁱ	242 – 316	SPORUniRule annotationAdd BLAST	75

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	4 – 6	Mediates interaction with FtsAUniRule annotation1 Publication	3
Regionⁱ	115 – 150	2 X 6 AA repeatsAdd BLAST	36
Regionⁱ	197 – 223	2 X 4 AA repeatsAdd BLAST	27

Domainⁱ

The cytoplasmic region is required for interaction with FtsA (PubMed:24750258). The periplasmic region is composed of a membrane-proximal region containing three short partially formed helices (H1, H2 and H3), followed by an unstructured glutamine-rich linker, and a C-terminal globular SPOR domain (PubMed:15101973, PubMed:19684127). Essential function of FtsN is accomplished by a small region of at most 35 residues that is centered about the H2 helix (PubMed:19684127). The SPOR domain, which exhibits a ribonucleoprotein (RNP) fold, binds peptidoglycan and is a strong septal localization determinant, but it seems not essential for cell division (PubMed:15466024, PubMed:19684127, PubMed:24056104).5 Publications

Sequence similaritiesⁱ

Belongs to the FtsN family.UniRule annotationCurated

Keywords - Domainⁱ

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGⁱ	ENOG41063M6 Bacteria COG3087 LUCA
HOGENOMⁱ	HOG000126695
InParanoidⁱ	P29131
KEGG Orthology (KO) More...KOⁱ	K03591

Family and domain databases

Gene3Dⁱ	3.30.70.1070, 1 hit
HAMAPⁱ	MF_02039 FtsN_entero, 1 hit
InterProⁱ	View protein in InterPro IPR011930 FtsN IPR007730 SPOR-like_dom IPR036680 SPOR-like_sf
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF05036 SPOR, 1 hit
SUPFAMⁱ	SSF110997 SSF110997, 1 hit
TIGRFAMsⁱ	TIGR02223 ftsN, 1 hit
PROSITEⁱ	View protein in PROSITE PS51724 SPOR, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P29131-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MAQRDYVRRS QPAPSRRKKS TSRKKQRNLP AVSPAMVAIA AAVLVTFIGG 
        60         70         80         90        100
LYFITHHKKE ESETLQSQKV TGNGLPPKPE ERWRYIKELE SRQPGVRAPT 
       110        120        130        140        150
EPSAGGEVKT PEQLTPEQRQ LLEQMQADMR QQPTQLVEVP WNEQTPEQRQ 
       160        170        180        190        200
QTLQRQRQAQ QLAEQQRLAQ QSRTTEQSWQ QQTRTSQAAP VQAQPRQSKP 
       210        220        230        240        250
ASSQQPYQDL LQTPAHTTAQ SKPQQAAPVA RAADAPKPTA EKKDERRWMV 
       260        270        280        290        300
QCGSFRGAEQ AETVRAQLAF EGFDSKITTN NGWNRVVIGP VKGKENADST 
       310 
LNRLKMAGHT NCIRLAAGG

Length:319

Mass (Da):35,793

Last modified:August 29, 2003 - v3

Checksum:ⁱ21CEA5771FF3FB66

Sequence cautionⁱ

The sequence AAA23935 differs from that shown. Reason: Frameshift at several positions.Curated

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	29	L → V (PubMed:8509333).Curated		1
Sequence conflictⁱ	29	L → V (Ref. 2) Curated		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	L14281 Genomic DNA Translation: AAA23814.1 L06547 Genomic DNA Translation: AAA23935.1 Frameshift. L19201 Genomic DNA Translation: AAB03065.1 U00096 Genomic DNA Translation: AAC76915.1 AP009048 Genomic DNA Translation: BAE77377.1
PIRⁱ	S40876
NCBI Reference Sequences More...RefSeqⁱ	NP_418368.1, NC_000913.3 WP_000068828.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC76915; AAC76915; b3933 BAE77377; BAE77377; BAE77377
GeneIDⁱ	948428
KEGGⁱ	ecj:JW3904 eco:b3933
PATRICⁱ	fig\|511145.12.peg.4051

Protein	Similar proteins		Species	Score	Length	Source
P29131	Cell division protein FtsN		Shigella sp.		319	UniRef100_P29131
Cell division protein FtsN		ECOLX		319
Cell division protein FtsN		Escherichia coli G3/10		319
Cell division protein FtsN		SHIBO		319
Cell division protein FtsN		SHIDY		319
+76

Protein	Similar proteins		Species	Score	Length	Source
P29131	Cell division protein FtsN		Shigella sp.		319	UniRef90_P29131
Cell division protein FtsN		ECOLX		319
Cell division protein FtsN		Escherichia coli G3/10		319
Cell division protein FtsN		SHIBO		319
Cell division protein FtsN		SHIDY		319
+561

Protein	Similar proteins		Species	Score	Length	Source
P29131	Cell division protein FtsN		Shigella sp.		319	UniRef50_P29131
Cell division protein FtsN		ECOLX		319
Cell division protein FtsN		Escherichia coli G3/10		319
Cell division protein FtsN		SHIBO		319
Cell division protein FtsN		SHIDY		319
+1904

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	L14281 Genomic DNA Translation: AAA23814.1 L06547 Genomic DNA Translation: AAA23935.1 Frameshift. L19201 Genomic DNA Translation: AAB03065.1 U00096 Genomic DNA Translation: AAC76915.1 AP009048 Genomic DNA Translation: BAE77377.1
PIRⁱ	S40876
RefSeqⁱ	NP_418368.1, NC_000913.3 WP_000068828.1, NZ_LN832404.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1UTA	NMR	-	A	243-319	[»]
ProteinModelPortalⁱ	P29131
SMRⁱ	P29131
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4261592, 198 interactors
DIPⁱ	DIP-9705N
IntActⁱ	P29131, 24 interactors
MINTⁱ	P29131
STRINGⁱ	316385.ECDH10B_4122

Proteomic databases

PaxDbⁱ	P29131
PRIDEⁱ	P29131

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC76915; AAC76915; b3933 BAE77377; BAE77377; BAE77377
GeneIDⁱ	948428
KEGGⁱ	ecj:JW3904 eco:b3933
PATRICⁱ	fig\|511145.12.peg.4051

Organism-specific databases

EchoBASEⁱ	EB1491
EcoGeneⁱ	EG11529 ftsN

Phylogenomic databases

eggNOGⁱ	ENOG41063M6 Bacteria COG3087 LUCA
HOGENOMⁱ	HOG000126695
InParanoidⁱ	P29131
KOⁱ	K03591

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG11529-MONOMER MetaCyc:EG11529-MONOMER

BioCycⁱ

EcoCyc:EG11529-MONOMER
MetaCyc:EG11529-MONOMER

Miscellaneous databases

EvolutionaryTraceⁱ	P29131
Protein Ontology More...PROⁱ	PR:P29131

Family and domain databases

Gene3Dⁱ	3.30.70.1070, 1 hit
HAMAPⁱ	MF_02039 FtsN_entero, 1 hit
InterProⁱ	View protein in InterPro IPR011930 FtsN IPR007730 SPOR-like_dom IPR036680 SPOR-like_sf
Pfamⁱ	View protein in Pfam PF05036 SPOR, 1 hit
SUPFAMⁱ	SSF110997 SSF110997, 1 hit
TIGRFAMsⁱ	TIGR02223 ftsN, 1 hit
PROSITEⁱ	View protein in PROSITE PS51724 SPOR, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	FTSN_ECOLI
Accessionⁱ	P29131Primary (citable) accession number: P29131 Secondary accession number(s): Q2M8M9
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
	Last sequence update:	August 29, 2003
	Last modified:	November 7, 2018
	This is version 158 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

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

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Supporting data

UniProtKB - P29131 (FTSN_ECOLI)

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Cell division protein FtsN

ftsN

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 - Molecular functioni

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

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

Amino acid modifications

Keywords - PTMi

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

Secondary structure

3D structure databases

Miscellaneous 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

Domains and Repeats

Region

<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

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

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

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

Keywords - Technical termi

Documents

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Sequence cautionⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ