FTSL_ECOLI
ID FTSL_ECOLI Reviewed; 121 AA.
AC P0AEN4; P22187; Q8KMX6;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Cell division protein FtsL {ECO:0000255|HAMAP-Rule:MF_00910};
GN Name=ftsL {ECO:0000255|HAMAP-Rule:MF_00910}; Synonyms=mraR, yabD;
GN OrderedLocusNames=b0083, JW0081;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, TOPOLOGY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=1332942;
RA Guzman L.-M., Barondess J.J., Beckwith J.;
RT "FtsL, an essential cytoplasmic membrane protein involved in cell division
RT in Escherichia coli.";
RL J. Bacteriol. 174:7716-7728(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1447153; DOI=10.1128/jb.174.23.7841-7843.1992;
RA Ueki M., Wachi M., Jung H.K., Ishino F., Matsuhashi M.;
RT "Escherichia coli mraR gene involved in cell growth and division.";
RL J. Bacteriol. 174:7841-7843(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8202364; DOI=10.1093/nar/22.9.1637;
RA Fujita N., Mori H., Yura T., Ishihama A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-
RT 4.1 min (110,917-193,643 bp) region.";
RL Nucleic Acids Res. 22:1637-1639(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=6350821; DOI=10.1007/bf00330881;
RA Nakamura M., Maruyama I.N., Soma M., Kato J., Suzuki H., Horota Y.;
RT "On the process of cellular division in Escherichia coli: nucleotide
RT sequence of the gene for penicillin-binding protein 3.";
RL Mol. Gen. Genet. 191:1-9(1983).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=2187182; DOI=10.1093/nar/18.9.2813;
RA Gomez M.J., Fluoret B., van Heijenoort J., Ayala J.A.;
RT "Nucleotide sequence of the regulatory region of the gene pbpB of
RT Escherichia coli.";
RL Nucleic Acids Res. 18:2813-2813(1990).
RN [8]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=10027987; DOI=10.1046/j.1365-2958.1999.01213.x;
RA Ghigo J.M., Weiss D.S., Chen J.C., Yarrow J.C., Beckwith J.;
RT "Localization of FtsL to the Escherichia coli septal ring.";
RL Mol. Microbiol. 31:725-737(1999).
RN [9]
RP FUNCTION, SUBUNIT, COILED-COIL DOMAIN, AND MUTAGENESIS OF LEU-70 AND
RP LEU-84.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=10613870; DOI=10.1128/jb.182.1.116-129.2000;
RA Ghigo J.M., Beckwith J.;
RT "Cell division in Escherichia coli: role of FtsL domains in septal
RT localization, function, and oligomerization.";
RL J. Bacteriol. 182:116-129(2000).
RN [10]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=11703663; DOI=10.1046/j.1365-2958.2001.02640.x;
RA Chen J.C., Beckwith J.;
RT "FtsQ, FtsL and FtsI require FtsK, but not FtsN, for co-localization with
RT FtsZ during Escherichia coli cell division.";
RL Mol. Microbiol. 42:395-413(2001).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=11948172; DOI=10.1128/jb.184.9.2552-2556.2002;
RA Hale C.A., de Boer P.A.J.;
RT "ZipA is required for recruitment of FtsK, FtsQ, FtsL, and FtsN to the
RT septal ring in Escherichia coli.";
RL J. Bacteriol. 184:2552-2556(2002).
RN [12]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=15165235; DOI=10.1111/j.1365-2958.2004.04044.x;
RA Buddelmeijer N., Beckwith J.;
RT "A complex of the Escherichia coli cell division proteins FtsL, FtsB and
RT FtsQ forms independently of its localization to the septal region.";
RL Mol. Microbiol. 52:1315-1327(2004).
RN [13]
RP INTERACTION WITH FTSB; FTSQ; FTSI; FTSN AND YMGF.
RC STRAIN=K12;
RX PubMed=15774864; DOI=10.1128/jb.187.7.2233-2243.2005;
RA Karimova G., Dautin N., Ladant D.;
RT "Interaction network among Escherichia coli membrane proteins involved in
RT cell division as revealed by bacterial two-hybrid analysis.";
RL J. Bacteriol. 187:2233-2243(2005).
RN [14]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH FTSB.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=19233928; DOI=10.1128/jb.01597-08;
RA Gonzalez M.D., Beckwith J.;
RT "Divisome under construction: distinct domains of the small membrane
RT protein FtsB are necessary for interaction with multiple cell division
RT proteins.";
RL J. Bacteriol. 191:2815-2825(2009).
RN [15]
RP SUBUNIT, COILED-COIL DOMAIN, AND DOMAIN.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=20363951; DOI=10.1128/jb.01609-09;
RA Gonzalez M.D., Akbay E.A., Boyd D., Beckwith J.;
RT "Multiple interaction domains in FtsL, a protein component of the widely
RT conserved bacterial FtsLBQ cell division complex.";
RL J. Bacteriol. 192:2757-2768(2010).
RN [16]
RP FUNCTION.
RX PubMed=21708137; DOI=10.1016/j.bbrc.2011.06.083;
RA Blencowe D.K., Al Jubori S., Morby A.P.;
RT "Identification of a novel function for the FtsL cell division protein from
RT Escherichia coli K12.";
RL Biochem. Biophys. Res. Commun. 411:44-49(2011).
RN [17]
RP 3D-STRUCTURE MODELING OF THE FTSB/FTSL/FTSQ COMPLEX.
RX PubMed=21672257; DOI=10.1186/1472-6807-11-28;
RA Villanelo F., Ordenes A., Brunet J., Lagos R., Monasterio O.;
RT "A model for the Escherichia coli FtsB/FtsL/FtsQ cell division complex.";
RL BMC Struct. Biol. 11:28-28(2011).
RN [18]
RP DOMAIN, AND LEUCINE ZIPPER-LIKE MOTIF.
RX PubMed=21784946; DOI=10.1128/jb.00324-11;
RA Robichon C., Karimova G., Beckwith J., Ladant D.;
RT "Role of leucine zipper motifs in association of the Escherichia coli cell
RT division proteins FtsL and FtsB.";
RL J. Bacteriol. 193:4988-4992(2011).
CC -!- FUNCTION: Essential cell division protein. May link together the
CC upstream cell division proteins, which are predominantly cytoplasmic,
CC with the downstream cell division proteins, which are predominantly
CC periplasmic. Can also mediate Zn(2+)-sensitivity probably by increasing
CC the permeability of the inner membrane. {ECO:0000255|HAMAP-
CC Rule:MF_00910, ECO:0000269|PubMed:10613870,
CC ECO:0000269|PubMed:19233928, ECO:0000269|PubMed:21708137}.
CC -!- SUBUNIT: Part of a complex composed of FtsB, FtsL and FtsQ. The complex
CC can be formed before its localization to the division site. This
CC tripartite complex can be divided further into a subcomplex of FtsB and
CC FtsL, which forms in the absence of FtsQ. Interacts also with FtsI,
CC FtsN and YmgF. Homodimer in vitro. May form multimers.
CC {ECO:0000255|HAMAP-Rule:MF_00910, ECO:0000269|PubMed:10613870,
CC ECO:0000269|PubMed:15165235, ECO:0000269|PubMed:15774864,
CC ECO:0000269|PubMed:19233928, ECO:0000269|PubMed:20363951}.
CC -!- INTERACTION:
CC P0AEN4; P56976: blr; NbExp=3; IntAct=EBI-1119082, EBI-6419495;
CC P0AEN4; P0A6S5: ftsB; NbExp=18; IntAct=EBI-1119082, EBI-1113953;
CC P0AEN4; P0AD68: ftsI; NbExp=4; IntAct=EBI-1119082, EBI-548564;
CC P0AEN4; P06136: ftsQ; NbExp=12; IntAct=EBI-1119082, EBI-1130157;
CC P0AEN4; P58034: ymgF; NbExp=3; IntAct=EBI-1119082, EBI-1214577;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00910, ECO:0000269|PubMed:10027987,
CC ECO:0000269|PubMed:11703663, ECO:0000269|PubMed:11948172,
CC ECO:0000269|PubMed:1332942, ECO:0000269|PubMed:15165235}; Single-pass
CC type II membrane protein {ECO:0000255|HAMAP-Rule:MF_00910,
CC ECO:0000269|PubMed:10027987, ECO:0000269|PubMed:11703663,
CC ECO:0000269|PubMed:11948172, ECO:0000269|PubMed:1332942,
CC ECO:0000269|PubMed:15165235}. Note=Localizes to the division septum
CC where it forms a ring structure. Localization requires FtsZ, FtsA,
CC ZipA, FtsK, FtsQ and FtsB, but not FtsI and FtsN. Localization of FtsB
CC and FtsL is codependent.
CC -!- DOMAIN: The cytoplasmic region is involved in recruitment of the
CC downstream cell division protein FtsW. The transmembrane segment and
CC the membrane-proximal periplasmic region form a coiled-coil structure
CC and are required for septal localization and interaction with FtsB. The
CC C-terminal region is required for interaction with FtsQ. Contains a
CC leucine zipper-like (LZ) motif, which is required for optimal
CC interaction with FtsB. {ECO:0000269|PubMed:20363951,
CC ECO:0000269|PubMed:21784946}.
CC -!- DISRUPTION PHENOTYPE: Mutants show inhibition of cell division,
CC formation of long, nonseptate filaments, ultimate cessation of growth
CC and lysis. {ECO:0000269|PubMed:1332942}.
CC -!- SIMILARITY: Belongs to the FtsL family. {ECO:0000255|HAMAP-
CC Rule:MF_00910}.
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DR EMBL; S49875; AAB24309.1; -; Genomic_DNA.
DR EMBL; S49802; AAB24311.1; -; Genomic_DNA.
DR EMBL; X55034; CAA38860.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73194.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96651.2; -; Genomic_DNA.
DR EMBL; K00137; AAA24299.1; -; Genomic_DNA.
DR EMBL; X52063; CAA36285.1; -; Genomic_DNA.
DR PIR; A45278; A45278.
DR RefSeq; NP_414625.1; NC_000913.3.
DR RefSeq; WP_000625658.1; NZ_STEB01000010.1.
DR AlphaFoldDB; P0AEN4; -.
DR SMR; P0AEN4; -.
DR BioGRID; 4261638; 332.
DR BioGRID; 849204; 1.
DR ComplexPortal; CPX-3099; FtsQBL complex.
DR ComplexPortal; CPX-3299; FtsBL complex.
DR DIP; DIP-47987N; -.
DR IntAct; P0AEN4; 17.
DR MINT; P0AEN4; -.
DR STRING; 511145.b0083; -.
DR PaxDb; P0AEN4; -.
DR PRIDE; P0AEN4; -.
DR EnsemblBacteria; AAC73194; AAC73194; b0083.
DR EnsemblBacteria; BAB96651; BAB96651; BAB96651.
DR GeneID; 67416156; -.
DR GeneID; 944803; -.
DR KEGG; ecj:JW0081; -.
DR KEGG; eco:b0083; -.
DR PATRIC; fig|1411691.4.peg.2197; -.
DR EchoBASE; EB1078; -.
DR eggNOG; COG3116; Bacteria.
DR HOGENOM; CLU_156524_2_0_6; -.
DR InParanoid; P0AEN4; -.
DR OMA; DLWHHKW; -.
DR PhylomeDB; P0AEN4; -.
DR BioCyc; EcoCyc:EG11086-MON; -.
DR PRO; PR:P0AEN4; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0032153; C:cell division site; IDA:EcoCyc.
DR GO; GO:1990586; C:divisome complex; IPI:ComplexPortal.
DR GO; GO:1990588; C:FtsBL complex; IC:ComplexPortal.
DR GO; GO:1990587; C:FtsQBL complex; IPI:ComplexPortal.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IC:ComplexPortal.
DR GO; GO:0051301; P:cell division; IC:ComplexPortal.
DR GO; GO:0000917; P:division septum assembly; IC:ComplexPortal.
DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IMP:EcoCyc.
DR HAMAP; MF_00910; FtsL; 1.
DR InterPro; IPR011922; Cell_div_FtsL.
DR PANTHER; PTHR37479; PTHR37479; 1.
DR Pfam; PF04999; FtsL; 1.
DR TIGRFAMs; TIGR02209; ftsL_broad; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cell inner membrane; Cell membrane; Coiled coil;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..121
FT /note="Cell division protein FtsL"
FT /id="PRO_0000087371"
FT TOPO_DOM 1..34
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00910"
FT TRANSMEM 35..57
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00910"
FT TOPO_DOM 58..121
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00910"
FT COILED 63..91
FT /evidence="ECO:0000255"
FT MOTIF 58..85
FT /note="Leucine zipper-like"
FT MUTAGEN 70
FT /note="L->H: Impairs both localization and function, and
FT reduces the efficiency of dimerization."
FT /evidence="ECO:0000269|PubMed:10613870"
FT MUTAGEN 84
FT /note="L->D: Impairs both localization and function, and
FT reduces the efficiency of dimerization."
FT /evidence="ECO:0000269|PubMed:10613870"
SQ SEQUENCE 121 AA; 13627 MW; 6DD5DF7B2ECB7090 CRC64;
MISRVTEALS KVKGSMGSHE RHALPGVIGD DLLRFGKLPL CLFICIILTA VTVVTTAHHT
RLLTAQREQL VLERDALDIE WRNLILEENA LGDHSRVERI ATEKLQMQHV DPSQENIVVQ
K
