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Cell division protein FtsQ

 FTSQ_ECOLI              Reviewed;         276 AA.
P06136;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-JAN-1988, sequence version 1.
28-MAR-2018, entry version 147.
RecName: Full=Cell division protein FtsQ {ECO:0000255|HAMAP-Rule:MF_00911};
Name=ftsQ {ECO:0000255|HAMAP-Rule:MF_00911};
OrderedLocusNames=b0093, JW0091;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=2995680; DOI=10.1016/0022-2836(85)90290-6;
Yi Q.-M., Rockenbach S., Ward J.E. Jr., Lutkenhaus J.;
"Structure and expression of the cell division genes ftsQ, ftsA and
ftsZ.";
J. Mol. Biol. 184:399-412(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=6094474;
Robinson A.C., Kenan D.J., Hatfull G.F., Sullivan N.F.,
Spiegelberg R., Donachie W.D.;
"DNA sequence and transcriptional organization of essential cell
division genes ftsQ and ftsA of Escherichia coli: evidence for
overlapping transcriptional units.";
J. Bacteriol. 160:546-555(1984).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2228979; DOI=10.1128/jb.172.11.6611-6614.1990;
Dewar S.J., Donachie W.D.;
"Regulation of expression of the ftsA cell division gene by sequences
in upstream genes.";
J. Bacteriol. 172:6611-6614(1990).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12;
PubMed=1630901; DOI=10.1093/nar/20.13.3305;
Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N.,
Isono K., Mizobuchi K., Nakata A.;
"Systematic sequencing of the Escherichia coli genome: analysis of the
0-2.4 min region.";
Nucleic Acids Res. 20:3305-3308(1992).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
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.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
STRAIN=K12;
PubMed=3528126; DOI=10.1128/jb.167.3.809-817.1986;
Robinson A.C., Kenan D.J., Sweeney J., Donachie W.D.;
"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.";
J. Bacteriol. 167:809-817(1986).
[8]
SUBCELLULAR LOCATION, AND TOPOLOGY.
PubMed=2007547; DOI=10.1128/jb.173.7.2187-2195.1991;
Carson M.J., Barondess J., Beckwith J.;
"The FtsQ protein of Escherichia coli: membrane topology, abundance,
and cell division phenotypes due to overproduction and insertion
mutations.";
J. Bacteriol. 173:2187-2195(1991).
[9]
SUBCELLULAR LOCATION, AND DOMAIN.
PubMed=9829918;
Buddelmeijer N., Aarsman M.E., Kolk A.H., Vicente M., Nanninga N.;
"Localization of cell division protein FtsQ by immunofluorescence
microscopy in dividing and nondividing cells of Escherichia coli.";
J. Bacteriol. 180:6107-6116(1998).
[10]
SUBCELLULAR LOCATION, AND DOMAIN.
PubMed=9882666;
Chen J.C., Weiss D.S., Ghigo J.M., Beckwith J.;
"Septal localization of FtsQ, an essential cell division protein in
Escherichia coli.";
J. Bacteriol. 181:521-530(1999).
[11]
SUBCELLULAR LOCATION.
PubMed=11415986; DOI=10.1093/embo-reports/kve108;
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.;
"Sec-dependent membrane protein insertion: sequential interaction of
nascent FtsQ with SecY and YidC.";
EMBO Rep. 2:524-529(2001).
[12]
SUBCELLULAR LOCATION.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=11703663; DOI=10.1046/j.1365-2958.2001.02640.x;
Chen J.C., Beckwith J.;
"FtsQ, FtsL and FtsI require FtsK, but not FtsN, for co-localization
with FtsZ during Escherichia coli cell division.";
Mol. Microbiol. 42:395-413(2001).
[13]
SUBCELLULAR LOCATION.
PubMed=11948172; DOI=10.1128/JB.184.9.2552-2556.2002;
Hale C.A., de Boer P.A.J.;
"ZipA is required for recruitment of FtsK, FtsQ, FtsL, and FtsN to the
septal ring in Escherichia coli.";
J. Bacteriol. 184:2552-2556(2002).
[14]
SUBUNIT, INTERACTION WITH FTSL AND FTSB, AND SUBCELLULAR LOCATION.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=15165235; DOI=10.1111/j.1365-2958.2004.04044.x;
Buddelmeijer N., Beckwith J.;
"A complex of the Escherichia coli cell division proteins FtsL, FtsB
and FtsQ forms independently of its localization to the septal
region.";
Mol. Microbiol. 52:1315-1327(2004).
[15]
INTERACTION WITH FTSL; FTSA; FTSI; FTSN; FTSX AND YMGF.
STRAIN=K12;
PubMed=15774864; DOI=10.1128/JB.187.7.2233-2243.2005;
Karimova G., Dautin N., Ladant D.;
"Interaction network among Escherichia coli membrane proteins involved
in cell division as revealed by bacterial two-hybrid analysis.";
J. Bacteriol. 187:2233-2243(2005).
[16]
SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF LEU-29; LEU-32 AND
VAL-38.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=17693520; DOI=10.1128/JB.00723-07;
Scheffers D.J., Robichon C., Haan G.J., den Blaauwen T.,
Koningstein G., van Bloois E., Beckwith J., Luirink J.;
"Contribution of the FtsQ transmembrane segment to localization to the
cell division site.";
J. Bacteriol. 189:7273-7280(2007).
[17]
FUNCTION, SUBUNIT, DOMAIN, AND INTERACTION WITH FTSK; FTSW; FTSI AND
FTSN.
STRAIN=K12;
PubMed=17185541; DOI=10.1099/mic.0.2006/000265-0;
D'Ulisse V., Fagioli M., Ghelardini P., Paolozzi L.;
"Three functional subdomains of the Escherichia coli FtsQ protein are
involved in its interaction with the other division proteins.";
Microbiology 153:124-138(2007).
[18]
FUNCTION, SUBUNIT, AND INTERACTION WITH FTSB.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=19233928; DOI=10.1128/JB.01597-08;
Gonzalez M.D., Beckwith J.;
"Divisome under construction: distinct domains of the small membrane
protein FtsB are necessary for interaction with multiple cell division
proteins.";
J. Bacteriol. 191:2815-2825(2009).
[19]
INDUCTION BY HYDROXYUREA.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=20005847; DOI=10.1016/j.molcel.2009.11.024;
Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J.,
Walker G.C.;
"Hydroxyurea induces hydroxyl radical-mediated cell death in
Escherichia coli.";
Mol. Cell 36:845-860(2009).
[20]
3D-STRUCTURE MODELING OF THE FTSB/FTSL/FTSQ COMPLEX.
PubMed=21672257; DOI=10.1186/1472-6807-11-28;
Villanelo F., Ordenes A., Brunet J., Lagos R., Monasterio O.;
"A model for the Escherichia coli FtsB/FtsL/FtsQ cell division
complex.";
BMC Struct. Biol. 11:28-28(2011).
[21]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 58-276, DOMAIN, AND
MUTAGENESIS OF ASP-91; LYS-113; GLU-125 AND ASP-237.
PubMed=18312270; DOI=10.1111/j.1365-2958.2008.06141.x;
van den Ent F., Vinkenvleugel T.M., Ind A., West P., Veprintsev D.,
Nanninga N., den Blaauwen T., Lowe J.;
"Structural and mutational analysis of the cell division protein
FtsQ.";
Mol. Microbiol. 68:110-123(2008).
[22]
STRUCTURE BY NMR OF 22-103.
PubMed=21499241; DOI=10.1038/nsmb.2026;
Frauenfeld J., Gumbart J., Sluis E.O., Funes S., Gartmann M.,
Beatrix B., Mielke T., Berninghausen O., Becker T., Schulten K.,
Beckmann R.;
"Cryo-EM structure of the ribosome-SecYE complex in the membrane
environment.";
Nat. Struct. Mol. Biol. 18:614-621(2011).
-!- 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.
{ECO:0000255|HAMAP-Rule:MF_00911, ECO:0000269|PubMed:17185541,
ECO:0000269|PubMed:19233928}.
-!- SUBUNIT: 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. {ECO:0000255|HAMAP-Rule:MF_00911,
ECO:0000269|PubMed:15165235, ECO:0000269|PubMed:15774864,
ECO:0000269|PubMed:17185541, ECO:0000269|PubMed:19233928}.
-!- INTERACTION:
Self; NbExp=6; IntAct=EBI-1130157, EBI-1130157;
P0A6S5:ftsB; NbExp=10; IntAct=EBI-1130157, EBI-1113953;
P0AD68:ftsI; NbExp=5; IntAct=EBI-1130157, EBI-548564;
P46889:ftsK; NbExp=3; IntAct=EBI-1130157, EBI-550795;
P0AEN4:ftsL; NbExp=11; IntAct=EBI-1130157, EBI-1119082;
P29131:ftsN; NbExp=7; IntAct=EBI-1130157, EBI-1134233;
P0ABG4:ftsW; NbExp=3; IntAct=EBI-1130157, EBI-1214767;
P58034:ymgF; NbExp=3; IntAct=EBI-1130157, EBI-1214577;
-!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
Rule:MF_00911, ECO:0000269|PubMed:11415986,
ECO:0000269|PubMed:11703663, ECO:0000269|PubMed:11948172,
ECO:0000269|PubMed:15165235, ECO:0000269|PubMed:17693520,
ECO:0000269|PubMed:2007547, ECO:0000269|PubMed:9829918,
ECO:0000269|PubMed:9882666}; Single-pass type II membrane protein
{ECO:0000255|HAMAP-Rule:MF_00911, ECO:0000269|PubMed:11415986,
ECO:0000269|PubMed:11703663, ECO:0000269|PubMed:11948172,
ECO:0000269|PubMed:15165235, ECO:0000269|PubMed:17693520,
ECO:0000269|PubMed:2007547, ECO:0000269|PubMed:9829918,
ECO:0000269|PubMed:9882666}. 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.
-!- INDUCTION: Repressed by hydroxyurea.
{ECO:0000269|PubMed:20005847}.
-!- 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. {ECO:0000269|PubMed:17185541,
ECO:0000269|PubMed:17693520, ECO:0000269|PubMed:18312270,
ECO:0000269|PubMed:9829918, ECO:0000269|PubMed:9882666}.
-!- SIMILARITY: Belongs to the FtsQ/DivIB family. FtsQ subfamily.
{ECO:0000255|HAMAP-Rule:MF_00911}.
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EMBL; M14029; AAA23673.1; -; Genomic_DNA.
EMBL; K02668; AAA23816.1; -; Genomic_DNA.
EMBL; X55034; CAA38870.1; -; Genomic_DNA.
EMBL; U00096; AAC73204.1; -; Genomic_DNA.
EMBL; AP009048; BAB96661.1; -; Genomic_DNA.
PIR; S10852; CEECQ.
RefSeq; NP_414635.1; NC_000913.3.
RefSeq; WP_000075748.1; NZ_LN832404.1.
PDB; 2VH1; X-ray; 2.70 A; A/B=58-276.
PDB; 4UE4; EM; 7.00 A; B=29-50.
PDB; 4V6M; EM; 7.1 A; Z=22-103.
PDBsum; 2VH1; -.
PDBsum; 4UE4; -.
PDBsum; 4V6M; -.
ProteinModelPortal; P06136; -.
SMR; P06136; -.
BioGrid; 4261112; 336.
DIP; DIP-9706N; -.
IntAct; P06136; 19.
MINT; P06136; -.
STRING; 316385.ECDH10B_0075; -.
PaxDb; P06136; -.
PRIDE; P06136; -.
EnsemblBacteria; AAC73204; AAC73204; b0093.
EnsemblBacteria; BAB96661; BAB96661; BAB96661.
GeneID; 944823; -.
KEGG; ecj:JW0091; -.
KEGG; eco:b0093; -.
PATRIC; fig|1411691.4.peg.2187; -.
EchoBASE; EB0338; -.
EcoGene; EG10342; ftsQ.
eggNOG; ENOG4105K7E; Bacteria.
eggNOG; COG1589; LUCA.
HOGENOM; HOG000255872; -.
InParanoid; P06136; -.
KO; K03589; -.
OMA; MARIQRF; -.
PhylomeDB; P06136; -.
BioCyc; EcoCyc:EG10342-MONOMER; -.
EvolutionaryTrace; P06136; -.
PRO; PR:P06136; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0032153; C:cell division site; IDA:EcoCyc.
GO; GO:0016021; C:integral component of membrane; IDA:EcoliWiki.
GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0051301; P:cell division; IMP:EcoliWiki.
GO; GO:0000917; P:division septum assembly; IMP:EcoliWiki.
GO; GO:0043093; P:FtsZ-dependent cytokinesis; IMP:EcoCyc.
HAMAP; MF_00911; FtsQ_subfam; 1.
InterPro; IPR005548; Cell_div_FtsQ/DivIB.
InterPro; IPR026579; FtsQ.
InterPro; IPR034746; POTRA.
InterPro; IPR013685; POTRA_FtsQ_type.
PANTHER; PTHR35851; PTHR35851; 1.
Pfam; PF03799; FtsQ; 1.
Pfam; PF08478; POTRA_1; 1.
PROSITE; PS51779; POTRA; 1.
1: Evidence at protein level;
3D-structure; Cell cycle; Cell division; Cell inner membrane;
Cell membrane; Complete proteome; Membrane; Reference proteome;
Transmembrane; Transmembrane helix.
CHAIN 1 276 Cell division protein FtsQ.
/FTId=PRO_0000160580.
TOPO_DOM 1 27 Cytoplasmic. {ECO:0000255|HAMAP-
Rule:MF_00911}.
TRANSMEM 28 48 Helical. {ECO:0000255|HAMAP-
Rule:MF_00911}.
TOPO_DOM 49 276 Periplasmic. {ECO:0000255|HAMAP-
Rule:MF_00911}.
DOMAIN 55 126 POTRA. {ECO:0000255|PROSITE-
ProRule:PRU01115}.
MUTAGEN 29 29 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.
{ECO:0000269|PubMed:17693520}.
MUTAGEN 32 32 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.
{ECO:0000269|PubMed:17693520}.
MUTAGEN 38 38 V->P: No change in activity. Does not
insert into the membrane and lack of
activity; when associated with R-29 and
R-32. {ECO:0000269|PubMed:17693520}.
MUTAGEN 91 91 D->K,Q: Does not affect localization.
{ECO:0000269|PubMed:18312270}.
MUTAGEN 113 113 K->D: Impairs localization.
{ECO:0000269|PubMed:18312270}.
MUTAGEN 125 125 E->K: Impairs localization.
{ECO:0000269|PubMed:18312270}.
MUTAGEN 237 237 D->N: Localizes to mid-cell, but is
unable to form a functional complex with
FtsL/FtsB. {ECO:0000269|PubMed:18312270}.
STRAND 59 64 {ECO:0000244|PDB:2VH1}.
HELIX 71 79 {ECO:0000244|PDB:2VH1}.
HELIX 87 89 {ECO:0000244|PDB:2VH1}.
HELIX 92 102 {ECO:0000244|PDB:2VH1}.
STRAND 106 114 {ECO:0000244|PDB:2VH1}.
TURN 115 117 {ECO:0000244|PDB:2VH1}.
STRAND 118 125 {ECO:0000244|PDB:2VH1}.
STRAND 128 132 {ECO:0000244|PDB:2VH1}.
TURN 133 135 {ECO:0000244|PDB:2VH1}.
STRAND 136 139 {ECO:0000244|PDB:2VH1}.
HELIX 149 151 {ECO:0000244|PDB:2VH1}.
TURN 152 154 {ECO:0000244|PDB:2VH1}.
STRAND 159 161 {ECO:0000244|PDB:2VH1}.
HELIX 167 182 {ECO:0000244|PDB:2VH1}.
STRAND 190 193 {ECO:0000244|PDB:2VH1}.
STRAND 195 197 {ECO:0000244|PDB:2VH1}.
STRAND 199 202 {ECO:0000244|PDB:2VH1}.
STRAND 204 206 {ECO:0000244|PDB:2VH1}.
STRAND 208 214 {ECO:0000244|PDB:2VH1}.
HELIX 216 236 {ECO:0000244|PDB:2VH1}.
STRAND 239 248 {ECO:0000244|PDB:2VH1}.
STRAND 251 258 {ECO:0000244|PDB:2VH1}.
SEQUENCE 276 AA; 31434 MW; 839A3D34B948CEAB CRC64;
MSQAALNTRN SEEEVSSRRN NGTRLAGILF LLTVLTTVLV SGWVVLGWME DAQRLPLSKL
VLTGERHYTR NDDIRQSILA LGEPGTFMTQ DVNIIQTQIE QRLPWIKQVS VRKQWPDELK
IHLVEYVPIA RWNDQHMVDA EGNTFSVPPE RTSKQVLPML YGPEGSANEV LQGYREMGQM
LAKDRFTLKE AAMTARRSWQ LTLNNDIKLN LGRGDTMKRL ARFVELYPVL QQQAQTDGKR
ISYVDLRYDS GAAVGWAPLP PEESTQQQNQ AQAEQQ


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U1888b CLIA Bos taurus,Bovine,CDC2,CDK1,CDK1,CDKN1,Cell division control protein 2 homolog,Cell division protein kinase 1,Cyclin-dependent kinase 1,p34 protein kinase 96T
U1888b CLIA kit Bos taurus,Bovine,CDC2,CDK1,CDK1,CDKN1,Cell division control protein 2 homolog,Cell division protein kinase 1,Cyclin-dependent kinase 1,p34 protein kinase 96T
E1888b ELISA Bos taurus,Bovine,CDC2,CDK1,CDK1,CDKN1,Cell division control protein 2 homolog,Cell division protein kinase 1,Cyclin-dependent kinase 1,p34 protein kinase 96T


 

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