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 FtsQ

Gene

ftsQ

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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. May control correct divisome assembly.UniRule annotation2 Publications

GO - Molecular functioni

  • identical protein binding Source: IntAct

GO - Biological processi

  • cell division Source: EcoliWiki
  • division septum assembly Source: EcoliWiki
  • FtsZ-dependent cytokinesis Source: EcoCyc

Keywordsi

Biological processCell cycle, Cell division

Enzyme and pathway databases

BioCyciEcoCyc:EG10342-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division protein FtsQUniRule annotation
Gene namesi
Name:ftsQUniRule annotation
Ordered Locus Names:b0093, JW0091
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10342 ftsQ

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 27CytoplasmicUniRule annotationAdd BLAST27
Transmembranei28 – 48HelicalUniRule annotationAdd BLAST21
Topological domaini49 – 276PeriplasmicUniRule annotationAdd BLAST228

GO - Cellular componenti

  • cell division site Source: EcoCyc
  • integral component of membrane Source: EcoliWiki
  • integral component of plasma membrane Source: EcoCyc
  • plasma membrane Source: EcoCyc

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi29L → R: No change in activity. Correctly assembled, interacts with FtsB and FtsL, but fails to localize efficiently to the cell division site; when associated with R-32. Does not insert into the membrane and lack of activity; when associated with R-32 and P-38. 1 Publication1
Mutagenesisi32L → R: No change in activity. Correctly assembled, interacts with FtsB and FtsL, but fails to localize efficiently to the cell division site; when associated with R-29. Does not insert into the membrane and lack of activity; when associated with R-29 and P-38. 1 Publication1
Mutagenesisi38V → P: No change in activity. Does not insert into the membrane and lack of activity; when associated with R-29 and R-32. 1 Publication1
Mutagenesisi91D → K or Q: Does not affect localization. 1 Publication1
Mutagenesisi113K → D: Impairs localization. 1 Publication1
Mutagenesisi125E → K: Impairs localization. 1 Publication1
Mutagenesisi237D → N: Localizes to mid-cell, but is unable to form a functional complex with FtsL/FtsB. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001605801 – 276Cell division protein FtsQAdd BLAST276

Proteomic databases

PaxDbiP06136
PRIDEiP06136

Expressioni

Inductioni

Repressed by hydroxyurea.1 Publication

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 with FtsA, FtsK, FtsL, FtsB, FtsW, FtsI, FtsN, FtsX and YmgF.UniRule annotation4 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4261112, 336 interactors
ComplexPortaliCPX-3099 FtsQBL complex
DIPiDIP-9706N
IntActiP06136, 19 interactors
MINTiP06136
STRINGi316385.ECDH10B_0075

Structurei

Secondary structure

1276
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi59 – 64Combined sources6
Helixi71 – 79Combined sources9
Helixi87 – 89Combined sources3
Helixi92 – 102Combined sources11
Beta strandi106 – 114Combined sources9
Turni115 – 117Combined sources3
Beta strandi118 – 125Combined sources8
Beta strandi128 – 132Combined sources5
Turni133 – 135Combined sources3
Beta strandi136 – 139Combined sources4
Helixi149 – 151Combined sources3
Turni152 – 154Combined sources3
Beta strandi159 – 161Combined sources3
Helixi167 – 182Combined sources16
Beta strandi190 – 193Combined sources4
Beta strandi195 – 197Combined sources3
Beta strandi199 – 202Combined sources4
Beta strandi204 – 206Combined sources3
Beta strandi208 – 214Combined sources7
Helixi216 – 236Combined sources21
Beta strandi239 – 248Combined sources10
Beta strandi251 – 258Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2VH1X-ray2.70A/B58-276[»]
4UE4electron microscopy7.00B29-50[»]
4V6Melectron microscopy7.1Z22-103[»]
ProteinModelPortaliP06136
SMRiP06136
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06136

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini55 – 126POTRAPROSITE-ProRule annotationAdd BLAST72

Domaini

The C-terminal periplasmic region is necessary and sufficient for septal targeting. The transmembrane region contributes to localization to the cell division site. Three periplasmic subdomains are involved in the interactions with other cell division proteins. Localization and recruitment require two separate domains.5 Publications

Sequence similaritiesi

Belongs to the FtsQ/DivIB family. FtsQ subfamily.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105K7E Bacteria
COG1589 LUCA
HOGENOMiHOG000255872
InParanoidiP06136
KOiK03589
OMAiMARIQRF
PhylomeDBiP06136

Family and domain databases

HAMAPiMF_00911 FtsQ_subfam, 1 hit
InterProiView protein in InterPro
IPR005548 Cell_div_FtsQ/DivIB
IPR026579 FtsQ
IPR034746 POTRA
IPR013685 POTRA_FtsQ_type
PANTHERiPTHR35851 PTHR35851, 1 hit
PfamiView protein in Pfam
PF03799 FtsQ, 1 hit
PF08478 POTRA_1, 1 hit
PROSITEiView protein in PROSITE
PS51779 POTRA, 1 hit

Sequencei

Sequence statusi: Complete.

P06136-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQAALNTRN SEEEVSSRRN NGTRLAGILF LLTVLTTVLV SGWVVLGWME
60 70 80 90 100
DAQRLPLSKL VLTGERHYTR NDDIRQSILA LGEPGTFMTQ DVNIIQTQIE
110 120 130 140 150
QRLPWIKQVS VRKQWPDELK IHLVEYVPIA RWNDQHMVDA EGNTFSVPPE
160 170 180 190 200
RTSKQVLPML YGPEGSANEV LQGYREMGQM LAKDRFTLKE AAMTARRSWQ
210 220 230 240 250
LTLNNDIKLN LGRGDTMKRL ARFVELYPVL QQQAQTDGKR ISYVDLRYDS
260 270
GAAVGWAPLP PEESTQQQNQ AQAEQQ
Length:276
Mass (Da):31,434
Last modified:January 1, 1988 - v1
Checksum:i839A3D34B948CEAB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14029 Genomic DNA Translation: AAA23673.1
K02668 Genomic DNA Translation: AAA23816.1
X55034 Genomic DNA Translation: CAA38870.1
U00096 Genomic DNA Translation: AAC73204.1
AP009048 Genomic DNA Translation: BAB96661.1
PIRiS10852 CEECQ
RefSeqiNP_414635.1, NC_000913.3
WP_000075748.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC73204; AAC73204; b0093
BAB96661; BAB96661; BAB96661
GeneIDi944823
KEGGiecj:JW0091
eco:b0093
PATRICifig|1411691.4.peg.2187

Similar proteinsi

Entry informationi

Entry nameiFTSQ_ECOLI
AccessioniPrimary (citable) accession number: P06136
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: June 20, 2018
This is version 148 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health