P06136 (FTSQ_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cell division protein FtsQ

Gene names

Name:	ftsQ
Ordered Locus Names:	b0093, JW0091

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	276 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.17 Ref.18
Subunit structure	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. Ref.14 Ref.15 Ref.17 Ref.18
Subcellular location	Cell inner membrane; Single-pass type II membrane protein. Note: Localizes to the division septum. Localization requires FtsZ, FtsA, ZipA and FtsK, but not FtsL, FtsI and FtsN. Insertion into the membrane requires YidC and the Sec translocase. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16
Domain	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. Ref.9 Ref.10 Ref.16 Ref.17 Ref.20
Sequence similarities	Belongs to the FtsQ/DivIB family. FtsQ subfamily.

Ontologies

Keywords
Biological process	Cell cycle Cell division
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	barrier septum assembly Inferred from mutant phenotype Ref.8. Source: EcoliWiki cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cytokinesis by binary fission Inferred from mutant phenotype PubMed 6998961. Source: EcoCyc
Cellular_component	cell division site part Inferred from direct assay Ref.9Ref.10. Source: EcoCyc integral to plasma membrane Inferred from direct assay Ref.8. Source: EcoCyc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		6	EBI-1130157,EBI-1130157
ftsB	P0A6S5	10	EBI-1130157,EBI-1113953
ftsI	P0AD68	5	EBI-1130157,EBI-548564
ftsK	P46889	3	EBI-1130157,EBI-550795
ftsL	P0AEN4	11	EBI-1130157,EBI-1119082
ftsN	P29131	5	EBI-1130157,EBI-1134233
ftsW	P0ABG4	3	EBI-1130157,EBI-1214767
ymgF	P58034	3	EBI-1130157,EBI-1214577

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 276

276

Cell division protein FtsQ HAMAP-Rule MF_00911

PRO_0000160580

Regions

Topological domain

1 – 27

27

Cytoplasmic Potential

Transmembrane

28 – 48

21

Helical; Potential

Topological domain

49 – 276

228

Periplasmic Potential

Experimental info

Mutagenesis

29

1

L → 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. Ref.16

Mutagenesis

32

1

L → 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. Ref.16

Mutagenesis

38

1

V → P: No change in activity. Does not insert into the membrane and lack of activity; when associated with R-29 and R-32. Ref.16

Mutagenesis

91

1

D → K or Q: Does not affect localization. Ref.20

Mutagenesis

113

1

K → D: Impairs localization. Ref.20

Mutagenesis

125

1

E → K: Impairs localization. Ref.20

Mutagenesis

237

1

D → N: Localizes to mid-cell, but is unable to form a functional complex with FtsL/FtsB. Ref.20

Secondary structure

1

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276

Helix Strand Turn

Details...

Beta strand

59 – 64

6

Helix

71 – 79

9

Helix

87 – 89

3

Helix

92 – 102

11

Beta strand

106 – 114

9

Turn

115 – 117

3

Beta strand

118 – 125

8

Beta strand

128 – 132

5

Turn

133 – 135

3

Beta strand

136 – 139

4

Helix

149 – 151

3

Turn

152 – 154

3

Beta strand

159 – 161

3

Helix

167 – 182

16

Beta strand

190 – 193

4

Beta strand

195 – 197

3

Beta strand

199 – 202

4

Beta strand

204 – 206

3

Beta strand

208 – 214

7

Helix

216 – 236

21

Beta strand

239 – 248

10

Beta strand

251 – 258

8

Sequences

	Sequence		Length	Mass (Da)
	P06136 [UniParc]. Last modified January 1, 1988. Version 1. Checksum: 839A3D34B948CEAB	FASTA	276	31,434
	10 20 30 40 50 60 MSQAALNTRN SEEEVSSRRN NGTRLAGILF LLTVLTTVLV SGWVVLGWME DAQRLPLSKL 70 80 90 100 110 120 VLTGERHYTR NDDIRQSILA LGEPGTFMTQ DVNIIQTQIE QRLPWIKQVS VRKQWPDELK 130 140 150 160 170 180 IHLVEYVPIA RWNDQHMVDA EGNTFSVPPE RTSKQVLPML YGPEGSANEV LQGYREMGQM 190 200 210 220 230 240 LAKDRFTLKE AAMTARRSWQ LTLNNDIKLN LGRGDTMKRL ARFVELYPVL QQQAQTDGKR 250 260 270 ISYVDLRYDS GAAVGWAPLP PEESTQQQNQ AQAEQQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and expression of the cell division genes ftsQ, ftsA and ftsZ." Yi Q.-M., Rockenbach S., Ward J.E. Jr., Lutkenhaus J. J. Mol. Biol. 184:399-412(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"DNA sequence and transcriptional organization of essential cell division genes ftsQ and ftsA of Escherichia coli: evidence for overlapping transcriptional units." Robinson A.C., Kenan D.J., Hatfull G.F., Sullivan N.F., Spiegelberg R., Donachie W.D. J. Bacteriol. 160:546-555(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[3]	"Regulation of expression of the ftsA cell division gene by sequences in upstream genes." Dewar S.J., Donachie W.D. J. Bacteriol. 172:6611-6614(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region." Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A. Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12.
[5]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[6]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]	"Further evidence for overlapping transcriptional units in an Escherichia coli cell envelope-cell division gene cluster: DNA sequence and transcriptional organization of the ddl ftsQ region." Robinson A.C., Kenan D.J., Sweeney J., Donachie W.D. J. Bacteriol. 167:809-817(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28. Strain: K12.
[8]	"The FtsQ protein of Escherichia coli: membrane topology, abundance, and cell division phenotypes due to overproduction and insertion mutations." Carson M.J., Barondess J., Beckwith J. J. Bacteriol. 173:2187-2195(1991) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, TOPOLOGY.
[9]	"Localization of cell division protein FtsQ by immunofluorescence microscopy in dividing and nondividing cells of Escherichia coli." Buddelmeijer N., Aarsman M.E., Kolk A.H., Vicente M., Nanninga N. J. Bacteriol. 180:6107-6116(1998) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, DOMAIN.
[10]	"Septal localization of FtsQ, an essential cell division protein in Escherichia coli." Chen J.C., Weiss D.S., Ghigo J.M., Beckwith J. J. Bacteriol. 181:521-530(1999) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, DOMAIN.
[11]	"Sec-dependent membrane protein insertion: sequential interaction of nascent FtsQ with SecY and YidC." Urbanus M.L., Scotti P.A., Froderberg L., Saaf A., de Gier J.W., Brunner J., Samuelson J.C., Dalbey R.E., Oudega B., Luirink J. EMBO Rep. 2:524-529(2001) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[12]	"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. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[13]	"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.
[14]	"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, INTERACTION WITH FTSL AND FTSB, SUBCELLULAR LOCATION. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[15]	"Interaction network among Escherichia coli membrane proteins involved in cell division as revealed by bacterial two-hybrid analysis." Karimova G., Dautin N., Ladant D. J. Bacteriol. 187:2233-2243(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FTSL; FTSA; FTSI; FTSN; FTSX AND YMGF. Strain: K12.
[16]	"Contribution of the FtsQ transmembrane segment to localization to the cell division site." Scheffers D.J., Robichon C., Haan G.J., den Blaauwen T., Koningstein G., van Bloois E., Beckwith J., Luirink J. J. Bacteriol. 189:7273-7280(2007) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF LEU-29; LEU-32 AND VAL-38. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[17]	"Three functional subdomains of the Escherichia coli FtsQ protein are involved in its interaction with the other division proteins." D'Ulisse V., Fagioli M., Ghelardini P., Paolozzi L. Microbiology 153:124-138(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT, DOMAIN, INTERACTION WITH FTSK; FTSW; FTSI AND FTSN. Strain: K12.
[18]	"Divisome under construction: distinct domains of the small membrane protein FtsB are necessary for interaction with multiple cell division proteins." Gonzalez M.D., Beckwith J. J. Bacteriol. 191:2815-2825(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT, INTERACTION WITH FTSB. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[19]	"A model for the Escherichia coli FtsB/FtsL/FtsQ cell division complex." Villanelo F., Ordenes A., Brunet J., Lagos R., Monasterio O. BMC Struct. Biol. 11:28-28(2011) [PubMed] [Europe PMC] [Abstract] Cited for: 3D-STRUCTURE MODELING OF THE FTSB/FTSL/FTSQ COMPLEX.
[20]	"Structural and mutational analysis of the cell division protein FtsQ." van den Ent F., Vinkenvleugel T.M., Ind A., West P., Veprintsev D., Nanninga N., den Blaauwen T., Lowe J. Mol. Microbiol. 68:110-123(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 58-276, DOMAIN, MUTAGENESIS OF ASP-91; LYS-113; GLU-125 AND ASP-237.
[21]	"Cryo-EM structure of the ribosome-SecYE complex in the membrane environment." Frauenfeld J., Gumbart J., Sluis E.O., Funes S., Gartmann M., Beatrix B., Mielke T., Berninghausen O., Becker T., Schulten K., Beckmann R. Nat. Struct. Mol. Biol. 18:614-621(2011) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 22-103.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

CEECQ. S10852.

RefSeq

NP_414635.1. NC_000913.2.
YP_488398.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2VH1	X-ray	2.70	A/B	58-276	[»]
3J00	electron microscopy	-	Z	22-103	[»]

ProteinModelPortal

P06136.

SMR

P06136. Positions 22-260.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-9706N.

IntAct

P06136. 15 interactions.

STRING

511145.b0093.

Proteomic databases

PaxDb

P06136.

PRIDE

P06136.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73204; AAC73204; b0093.
BAB96661; BAB96661; BAB96661.

GeneID

12932118.
944823.

KEGG

ecj:Y75_p0092.
eco:b0093.

PATRIC

32115291. VBIEscCol129921_0097.

Organism-specific databases

EchoBASE

EB0338.

EcoGene

EG10342. ftsQ.

Phylogenomic databases

eggNOG

COG1589.

HOGENOM

HOG000255872.

KO

K03589.

OMA

RERGSWF.

ProtClustDB

PRK10775.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10342-MONOMER.
ECOL316407:JW0091-MONOMER.

Gene expression databases

Genevestigator

P06136.

Family and domain databases

HAMAP

MF_00911. FtsQ_subfam.

InterPro

IPR005548. Cell_div_FtsQ/DivIB.
IPR026579. FtsQ.
IPR013685. POTRA_FtsQ_type.
[Graphical view]

Pfam

PF03799. FtsQ. 1 hit.
PF08478. POTRA_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P06136.

Entry information

Entry name

FTSQ_ECOLI

Accession

Primary (citable) accession number: P06136

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 1, 1988
Last modified:	May 1, 2013
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program