Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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.

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11529. ftsN.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3333CytoplasmicUniRule annotation1 PublicationAdd
BLAST
Transmembranei34 – 5421HelicalUniRule annotationAdd
BLAST
Topological domaini55 – 319265PeriplasmicUniRule annotation1 PublicationAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi5 – 51D → N: Causes significant impairment of the interaction with FtsA. 1 Publication
Mutagenesisi83 – 831W → L or T: Lack of activity. 1 Publication
Mutagenesisi85 – 851Y → S or W: Lack of activity. 1 Publication
Mutagenesisi89 – 891L → S: Lack of activity. 1 Publication
Mutagenesisi251 – 2511Q → A: Reduces septal localization by a factor of at least 3. 1 Publication
Mutagenesisi251 – 2511Q → E: Severe localization defects. Binds peptidoglycan poorly. 1 Publication
Mutagenesisi252 – 2521C → A: Severely reduces stability of the protein. 1 Publication
Mutagenesisi254 – 2541S → A: Reduces septal localization by a factor of at least 3. 1 Publication
Mutagenesisi254 – 2541S → E: Binds peptidoglycan poorly. 1 Publication
Mutagenesisi263 – 2631T → D: Intermediate localization defects. 1 Publication
Mutagenesisi270 – 2701F → A: Intermediate localization defects. 1 Publication
Mutagenesisi283 – 2831W → A: Reduces septal localization by a factor of at least 3. 1 Publication
Mutagenesisi283 – 2831W → D: Severe localization defects. 1 Publication
Mutagenesisi285 – 2851R → A: Reduces septal localization by a factor of at least 3. Binds peptidoglycan poorly. 1 Publication
Mutagenesisi312 – 3121C → A: Severely reduces stability of the protein. 1 Publication
Mutagenesisi313 – 3131I → A: Reduces septal localization by a factor of at least 3. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 319319Cell division protein FtsNPRO_0000087376Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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 interactions.
DIPiDIP-9705N.
IntActiP29131. 24 interactions.
STRINGi511145.b3933.

Structurei

Secondary structure

1
319
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi254 – 2563Combined sources
Helixi258 – 27114Combined sources
Beta strandi275 – 2795Combined sources
Beta strandi281 – 29010Combined sources
Turni293 – 2953Combined sources
Helixi296 – 30712Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UTANMR-A243-319[»]
ProteinModelPortaliP29131.
SMRiP29131. Positions 243-319.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29131.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati115 – 12061-1
Repeati145 – 15061-2
Repeati197 – 20042-1
Repeati220 – 22342-2
Domaini242 – 31675SPORUniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni4 – 63Mediates interaction with FtsAUniRule annotation1 Publication
Regioni115 – 150362 X 6 AA repeatsAdd
BLAST
Regioni197 – 223272 X 4 AA repeatsAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti29 – 291L → V (PubMed:8509333).Curated
Sequence conflicti29 – 291L → V (Ref. 2) Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1UTANMR-A243-319[»]
ProteinModelPortaliP29131.
SMRiP29131. Positions 243-319.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261592. 197 interactions.
DIPiDIP-9705N.
IntActiP29131. 24 interactions.
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.

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: September 7, 2016
This is version 145 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.