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Protein

Cell division protein FtsN

Gene

ftsN

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 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

GO - Biological processi

  • barrier septum assembly Source: EcoCyc
  • cell division Source: CACAO
  • FtsZ-dependent cytokinesis Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Septation

Enzyme and pathway databases

BioCyciEcoCyc:EG11529-MONOMER.
ECOL316407:JW3904-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
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11529. ftsN.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 33CytoplasmicUniRule annotation1 PublicationAdd BLAST33
Transmembranei34 – 54HelicalUniRule annotationAdd BLAST21
Topological domaini55 – 319PeriplasmicUniRule annotation1 PublicationAdd BLAST265

GO - Cellular componenti

  • cell division site Source: UniProtKB-HAMAP
  • cell septum Source: EcoCyc
  • integral component of plasma membrane Source: UniProtKB-HAMAP
  • plasma membrane Source: EcoCyc
Complete GO annotation...

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 keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi5D → N: Causes significant impairment of the interaction with FtsA. 1 Publication1
Mutagenesisi83W → L or T: Lack of activity. 1 Publication1
Mutagenesisi85Y → S or W: Lack of activity. 1 Publication1
Mutagenesisi89L → S: Lack of activity. 1 Publication1
Mutagenesisi251Q → A: Reduces septal localization by a factor of at least 3. 1 Publication1
Mutagenesisi251Q → E: Severe localization defects. Binds peptidoglycan poorly. 1 Publication1
Mutagenesisi252C → A: Severely reduces stability of the protein. 1 Publication1
Mutagenesisi254S → A: Reduces septal localization by a factor of at least 3. 1 Publication1
Mutagenesisi254S → E: Binds peptidoglycan poorly. 1 Publication1
Mutagenesisi263T → D: Intermediate localization defects. 1 Publication1
Mutagenesisi270F → A: Intermediate localization defects. 1 Publication1
Mutagenesisi283W → A: Reduces septal localization by a factor of at least 3. 1 Publication1
Mutagenesisi283W → D: Severe localization defects. 1 Publication1
Mutagenesisi285R → A: Reduces septal localization by a factor of at least 3. Binds peptidoglycan poorly. 1 Publication1
Mutagenesisi312C → A: Severely reduces stability of the protein. 1 Publication1
Mutagenesisi313I → A: Reduces septal localization by a factor of at least 3. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000873761 – 319Cell division protein FtsNAdd BLAST319

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi252 ↔ 312UniRule annotation1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP29131.
PRIDEiP29131.

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

WithEntry#Exp.IntActNotes
blrP569763EBI-1134233,EBI-6419495
ftsAP0ABH07EBI-1134233,EBI-550562
ftsIP0AD683EBI-1134233,EBI-548564
ftsQP061367EBI-1134233,EBI-1130157
ftsWP0ABG43EBI-1134233,EBI-1214767
mrcBP029196EBI-1134233,EBI-909769

Protein-protein interaction databases

BioGridi4261592. 197 interactors.
DIPiDIP-9705N.
IntActiP29131. 24 interactors.
STRINGi511145.b3933.

Structurei

Secondary structure

1319
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi254 – 256Combined sources3
Helixi258 – 271Combined sources14
Beta strandi275 – 279Combined sources5
Beta strandi281 – 290Combined sources10
Turni293 – 295Combined sources3
Helixi296 – 307Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UTANMR-A243-319[»]
ProteinModelPortaliP29131.
SMRiP29131.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29131.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati115 – 1201-16
Repeati145 – 1501-26
Repeati197 – 2002-14
Repeati220 – 2232-24
Domaini242 – 316SPORUniRule annotationAdd BLAST75

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni4 – 6Mediates interaction with FtsAUniRule annotation1 Publication3
Regioni115 – 1502 X 6 AA repeatsAdd BLAST36
Regioni197 – 2232 X 4 AA repeatsAdd BLAST27

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
Contains 1 SPOR domain.UniRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG41063M6. Bacteria.
COG3087. LUCA.
HOGENOMiHOG000126695.
InParanoidiP29131.
KOiK03591.
OMAiLYFIAHN.

Family and domain databases

Gene3Di3.30.70.1070. 1 hit.
HAMAPiMF_02039. FtsN_entero. 1 hit.
InterProiIPR011930. FtsN.
IPR007730. SPOR_dom.
[Graphical view]
PfamiPF05036. SPOR. 1 hit.
[Graphical view]
SUPFAMiSSF110997. SSF110997. 1 hit.
TIGRFAMsiTIGR02223. ftsN. 1 hit.
PROSITEiPS51724. SPOR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P29131-1 [UniParc]FASTAAdd 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
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti29L → V (PubMed:8509333).Curated1
Sequence conflicti29L → V (Ref. 2) Curated1

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.
PIRiS40876.
RefSeqiNP_418368.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC76915; AAC76915; b3933.
BAE77377; BAE77377; BAE77377.
GeneIDi948428.
KEGGiecj:JW3904.
eco:b3933.
PATRICi32123381. VBIEscCol129921_4051.

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.
PIRiS40876.
RefSeqiNP_418368.1. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UTANMR-A243-319[»]
ProteinModelPortaliP29131.
SMRiP29131.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261592. 197 interactors.
DIPiDIP-9705N.
IntActiP29131. 24 interactors.
STRINGi511145.b3933.

Proteomic databases

PaxDbiP29131.
PRIDEiP29131.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76915; AAC76915; b3933.
BAE77377; BAE77377; BAE77377.
GeneIDi948428.
KEGGiecj:JW3904.
eco:b3933.
PATRICi32123381. VBIEscCol129921_4051.

Organism-specific databases

EchoBASEiEB1491.
EcoGeneiEG11529. ftsN.

Phylogenomic databases

eggNOGiENOG41063M6. Bacteria.
COG3087. LUCA.
HOGENOMiHOG000126695.
InParanoidiP29131.
KOiK03591.
OMAiLYFIAHN.

Enzyme and pathway databases

BioCyciEcoCyc:EG11529-MONOMER.
ECOL316407:JW3904-MONOMER.
MetaCyc:EG11529-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP29131.
PROiP29131.

Family and domain databases

Gene3Di3.30.70.1070. 1 hit.
HAMAPiMF_02039. FtsN_entero. 1 hit.
InterProiIPR011930. FtsN.
IPR007730. SPOR_dom.
[Graphical view]
PfamiPF05036. SPOR. 1 hit.
[Graphical view]
SUPFAMiSSF110997. SSF110997. 1 hit.
TIGRFAMsiTIGR02223. ftsN. 1 hit.
PROSITEiPS51724. SPOR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFTSN_ECOLI
AccessioniPrimary (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 2, 2016
This is version 147 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.