FTSL_BACSU
ID FTSL_BACSU Reviewed; 117 AA.
AC Q07867;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Cell division protein FtsL {ECO:0000255|HAMAP-Rule:MF_00910};
GN Name=ftsL {ECO:0000255|HAMAP-Rule:MF_00910};
GN Synonyms=yllD {ECO:0000303|PubMed:8244929}, ylxB;
GN OrderedLocusNames=BSU15150;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=8244929; DOI=10.1128/jb.175.23.7604-7616.1993;
RA Yanouri A., Daniel R.A., Errington J., Buchanan C.E.;
RT "Cloning and sequencing of the cell division gene pbpB, which encodes
RT penicillin-binding protein 2B in Bacillus subtilis.";
RL J. Bacteriol. 175:7604-7616(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=8636036; DOI=10.1128/jb.178.8.2343-2350.1996;
RA Daniel R.A., Williams A.M., Errington J.;
RT "A complex four-gene operon containing essential cell division gene pbpB in
RT Bacillus subtilis.";
RL J. Bacteriol. 178:2343-2350(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP SUBCELLULAR LOCATION.
RC STRAIN=168;
RX PubMed=10792716; DOI=10.1046/j.1365-2958.2000.01857.x;
RA Daniel R.A., Errington J.;
RT "Intrinsic instability of the essential cell division protein FtsL of
RT Bacillus subtilis and a role for DivIB protein in FtsL turnover.";
RL Mol. Microbiol. 36:278-289(2000).
RN [5]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=168;
RX PubMed=10844672; DOI=10.1046/j.1365-2958.2000.01895.x;
RA Sievers J., Errington J.;
RT "The Bacillus subtilis cell division protein FtsL localizes to sites of
RT septation and interacts with DivIC.";
RL Mol. Microbiol. 36:846-855(2000).
RN [6]
RP SUBUNIT, SUBCELLULAR LOCATION, AND THERMODYNAMIC INSTABILITY.
RX PubMed=11994149; DOI=10.1046/j.1365-2958.2002.02920.x;
RA Robson S.A., Michie K.A., Mackay J.P., Harry E., King G.F.;
RT "The Bacillus subtilis cell division proteins FtsL and DivIC are
RT intrinsically unstable and do not interact with one another in the absence
RT of other septasomal components.";
RL Mol. Microbiol. 44:663-674(2002).
RN [7]
RP INTERACTION WITH DIVIB AND DIVIC, SUBUNIT, SUBCELLULAR LOCATION, AND
RP THERMODYNAMIC INSTABILITY.
RC STRAIN=168;
RX PubMed=16936019; DOI=10.1128/jb.01031-06;
RA Daniel R.A., Noirot-Gros M.F., Noirot P., Errington J.;
RT "Multiple interactions between the transmembrane division proteins of
RT Bacillus subtilis and the role of FtsL instability in divisome assembly.";
RL J. Bacteriol. 188:7396-7404(2006).
RN [8]
RP FUNCTION.
RC STRAIN=CRK6000;
RX PubMed=16549676; DOI=10.1099/mic.0.28497-0;
RA Kawai Y., Ogasawara N.;
RT "Bacillus subtilis EzrA and FtsL synergistically regulate FtsZ ring
RT dynamics during cell division.";
RL Microbiology 152:1129-1141(2006).
RN [9]
RP FUNCTION, DOMAIN, AND CLEAVAGE.
RX PubMed=17020588; DOI=10.1111/j.1365-2958.2006.05402.x;
RA Bramkamp M., Weston L., Daniel R.A., Errington J.;
RT "Regulated intramembrane proteolysis of FtsL protein and the control of
RT cell division in Bacillus subtilis.";
RL Mol. Microbiol. 62:580-591(2006).
RN [10]
RP INTERACTION WITH DIVIC.
RC STRAIN=168;
RX PubMed=20644139; DOI=10.1128/jb.00287-10;
RA Wadenpohl I., Bramkamp M.;
RT "DivIC stabilizes FtsL against RasP cleavage.";
RL J. Bacteriol. 192:5260-5263(2010).
CC -!- FUNCTION: Essential cell division protein that may play a structural
CC role. Probably involved in the regulation of the timing of cell
CC division. Also required for sporulation. {ECO:0000255|HAMAP-
CC Rule:MF_00910, ECO:0000269|PubMed:10844672,
CC ECO:0000269|PubMed:16549676, ECO:0000269|PubMed:17020588}.
CC -!- SUBUNIT: Monomer. Interacts with DivIB and DivIC. Interaction with
CC DivIC stabilizes FtsL against RasP cleavage.
CC {ECO:0000269|PubMed:10844672, ECO:0000269|PubMed:11994149,
CC ECO:0000269|PubMed:16936019, ECO:0000269|PubMed:20644139}.
CC -!- INTERACTION:
CC Q07867; P37471: divIC; NbExp=4; IntAct=EBI-5245735, EBI-5243468;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00910,
CC ECO:0000269|PubMed:10792716, ECO:0000269|PubMed:10844672,
CC ECO:0000269|PubMed:11994149, ECO:0000269|PubMed:16936019}; Single-pass
CC type II membrane protein {ECO:0000255|HAMAP-Rule:MF_00910,
CC ECO:0000269|PubMed:10792716, ECO:0000269|PubMed:10844672,
CC ECO:0000269|PubMed:11994149, ECO:0000269|PubMed:16936019}.
CC Note=Localizes to the division septum where it forms a ring structure.
CC Remains localized at mid-cell during the whole septation process.
CC Localization requires FtsZ, DivIB, DivIC and PBP-2B.
CC -!- INDUCTION: Transcribed at a low constant level in all growth phases.
CC Part of the mraZ-rsmH-ftsL-pbpB operon. {ECO:0000269|PubMed:8636036}.
CC -!- DOMAIN: The cytoplasmic region is involved in protein stability.
CC {ECO:0000269|PubMed:17020588}.
CC -!- PTM: Cleaved by RasP. Cleavage is important for turnover and function
CC of FtsL.
CC -!- DISRUPTION PHENOTYPE: Essential, it cannot be deleted.
CC {ECO:0000269|PubMed:8244929, ECO:0000269|PubMed:8636036}.
CC -!- MISCELLANEOUS: Is thermodynamically highly unstable and is likely to be
CC rapidly degraded unless stabilized by interaction with other septasomal
CC proteins.
CC -!- SIMILARITY: Belongs to the FtsL family. {ECO:0000255|HAMAP-
CC Rule:MF_00910}.
CC -!- CAUTION: The question of whether FtsL and DivIC interact directly
CC (PubMed:16936019) or indirectly (PubMed:11994149) remains
CC controversial. {ECO:0000305|PubMed:11994149,
CC ECO:0000305|PubMed:16936019}.
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DR EMBL; L09703; AAC36836.1; -; Unassigned_DNA.
DR EMBL; Z68230; CAA92526.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13388.1; -; Genomic_DNA.
DR PIR; B53292; B53292.
DR RefSeq; NP_389398.1; NC_000964.3.
DR RefSeq; WP_003232200.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; Q07867; -.
DR SMR; Q07867; -.
DR IntAct; Q07867; 17.
DR STRING; 224308.BSU15150; -.
DR PaxDb; Q07867; -.
DR PRIDE; Q07867; -.
DR EnsemblBacteria; CAB13388; CAB13388; BSU_15150.
DR GeneID; 50133630; -.
DR GeneID; 939860; -.
DR KEGG; bsu:BSU15150; -.
DR PATRIC; fig|224308.179.peg.1651; -.
DR eggNOG; COG4839; Bacteria.
DR OMA; MAVEKIY; -.
DR BioCyc; BSUB:BSU15150-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0032153; C:cell division site; IEA:UniProtKB-UniRule.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00910; FtsL; 1.
DR InterPro; IPR011922; Cell_div_FtsL.
DR TIGRFAMs; TIGR02209; ftsL_broad; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..117
FT /note="Cell division protein FtsL"
FT /id="PRO_0000087367"
FT TOPO_DOM 1..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00910"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00910"
FT TOPO_DOM 57..117
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00910"
SQ SEQUENCE 117 AA; 13073 MW; 8198D434E6F788FE CRC64;
MSNLAYQPEK QQRHAISPEK KVIVKKRASI TLGEKVLLVL FAAAVLSVSL LIVSKAYAAY
QTNIEVQKLE EQISSENKQI GDLEKSVADL SKPQRIMDIA KKNGLNLKDK KVKNIQE
