TOLR_ECOLI
ID TOLR_ECOLI Reviewed; 142 AA.
AC P0ABV6; P05829;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Tol-Pal system protein TolR {ECO:0000255|HAMAP-Rule:MF_02203, ECO:0000305};
GN Name=tolR {ECO:0000255|HAMAP-Rule:MF_02203, ECO:0000303|PubMed:3294803};
GN OrderedLocusNames=b0738, JW0728;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=3294803; DOI=10.1128/jb.169.6.2667-2674.1987;
RA Sun T.-P., Webster R.E.;
RT "Nucleotide sequence of a gene cluster involved in entry of E colicins and
RT single-stranded DNA of infecting filamentous bacteriophages into
RT Escherichia coli.";
RL J. Bacteriol. 169:2667-2674(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [5]
RP FUNCTION.
RX PubMed=1683466; DOI=10.1111/j.1365-2958.1991.tb01873.x;
RA Webster R.E.;
RT "The tol gene products and the import of macromolecules into Escherichia
RT coli.";
RL Mol. Microbiol. 5:1005-1011(1991).
RN [6]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=8331075; DOI=10.1128/jb.175.14.4485-4491.1993;
RA Kampfenkel K., Braun V.;
RT "Membrane topologies of the TolQ and TolR proteins of Escherichia coli:
RT inactivation of TolQ by a missense mutation in the proposed first
RT transmembrane segment.";
RL J. Bacteriol. 175:4485-4491(1993).
RN [7]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=8376353; DOI=10.1128/jb.175.18.6059-6061.1993;
RA Muller M.M., Vianney A., Lazzaroni J.-C., Webster R.E., Portalier R.;
RT "Membrane topology of the Escherichia coli TolR protein required for cell
RT envelope integrity.";
RL J. Bacteriol. 175:6059-6061(1993).
RN [8]
RP INTERACTION WITH TOLA.
RX PubMed=7744737; DOI=10.1074/jbc.270.19.11078;
RA Derouiche R., Benedetti H., Lazzaroni J.C., Lazdunski C., Lloubes R.;
RT "Protein complex within Escherichia coli inner membrane. TolA N-terminal
RT domain interacts with TolQ and TolR proteins.";
RL J. Biol. Chem. 270:11078-11084(1995).
RN [9]
RP SUBUNIT, INTERACTION WITH TOLA AND TOLQ, AND DOMAIN.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=10419942; DOI=10.1128/jb.181.15.4476-4484.1999;
RA Journet L., Rigal A., Lazdunski C., Benedetti H.;
RT "Role of TolR N-terminal, central, and C-terminal domains in dimerization
RT and interaction with TolA and tolQ.";
RL J. Bacteriol. 181:4476-4484(1999).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF ASP-23.
RX PubMed=11722743; DOI=10.1046/j.1365-2958.2001.02673.x;
RA Cascales E., Lloubes R., Sturgis J.N.;
RT "The TolQ-TolR proteins energize TolA and share homologies with the
RT flagellar motor proteins MotA-MotB.";
RL Mol. Microbiol. 42:795-807(2001).
RN [11]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=17233825; DOI=10.1111/j.1365-2958.2006.05571.x;
RA Gerding M.A., Ogata Y., Pecora N.D., Niki H., de Boer P.A.;
RT "The trans-envelope Tol-Pal complex is part of the cell division machinery
RT and required for proper outer-membrane invagination during cell
RT constriction in E. coli.";
RL Mol. Microbiol. 63:1008-1025(2007).
RN [12]
RP PROTEIN COPY NUMBER.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=24766808; DOI=10.1016/j.cell.2014.02.033;
RA Li G.W., Burkhardt D., Gross C., Weissman J.S.;
RT "Quantifying absolute protein synthesis rates reveals principles underlying
RT allocation of cellular resources.";
RL Cell 157:624-635(2014).
RN [13]
RP FUNCTION.
RX PubMed=24720726; DOI=10.1111/mmi.12609;
RA Santos T.M., Lin T.Y., Rajendran M., Anderson S.M., Weibel D.B.;
RT "Polar localization of Escherichia coli chemoreceptors requires an intact
RT Tol-Pal complex.";
RL Mol. Microbiol. 92:985-1004(2014).
RN [14]
RP MODELING OF FUNCTION, DOMAIN, AND PEPTIDOGLYCAN-BINDING.
RX PubMed=30713026; DOI=10.1016/j.str.2019.01.001;
RA Boags A.T., Samsudin F., Khalid S.;
RT "Binding from both sides: TolR and full-length OmpA bind and maintain the
RT local structure of the E. coli cell wall.";
RL Structure 27:713-724(2019).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=32152098; DOI=10.1073/pnas.1919267117;
RA Yakhnina A.A., Bernhardt T.G.;
RT "The Tol-Pal system is required for peptidoglycan-cleaving enzymes to
RT complete bacterial cell division.";
RL Proc. Natl. Acad. Sci. U.S.A. 117:6777-6783(2020).
RN [16] {ECO:0007744|PDB:5BY4}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 36-142, SUBUNIT, AND DOMAIN.
RC STRAIN=K12;
RX PubMed=26354441; DOI=10.1074/jbc.m115.671586;
RA Wojdyla J.A., Cutts E., Kaminska R., Papadakos G., Hopper J.T.,
RA Stansfeld P.J., Staunton D., Robinson C.V., Kleanthous C.;
RT "Structure and function of the Escherichia coli Tol-Pal stator protein
RT TolR.";
RL J. Biol. Chem. 290:26675-26687(2015).
CC -!- FUNCTION: Part of the Tol-Pal system, which plays a role in outer
CC membrane invagination during cell division and is important for
CC maintaining outer membrane integrity (PubMed:1683466, PubMed:17233825).
CC Required, with TolQ, for the proton motive force-dependent activation
CC of TolA and for TolA-Pal interaction (PubMed:11722743). The Tol-Pal
CC system is also required for polar localization of chemoreceptors
CC clusters (PubMed:24720726). The system also appears to be required for
CC the activity of several outer membrane-localized enzymes with cell wall
CC remodeling activity (PubMed:32152098). Modeling suggests that non-
CC covalent binding of OmpA (from the outer membrane) and TolR (from the
CC inner membrane) to peptidoglycan maintains the position of the cell
CC wall in the periplasm, holding it approximately equidistant from both
CC the inner and outer membranes. Trimeric Lpp controls the width of the
CC periplasm, adjusts its tilt angle to accommodate to the available
CC space, and can compensate in part for an absence of OmpA (Probable).
CC {ECO:0000269|PubMed:11722743, ECO:0000269|PubMed:1683466,
CC ECO:0000269|PubMed:17233825, ECO:0000269|PubMed:24720726,
CC ECO:0000269|PubMed:32152098, ECO:0000305|PubMed:30713026}.
CC -!- FUNCTION: (Microbial infection) Involved in the uptake of group A
CC colicins (colicins A, E1, E2, E3, and K) and in the uptake of
CC filamentous phage DNA. {ECO:0000269|PubMed:1683466,
CC ECO:0000269|PubMed:3294803}.
CC -!- SUBUNIT: The Tol-Pal system is composed of five core proteins: the
CC inner membrane proteins TolA, TolQ and TolR, the periplasmic protein
CC TolB and the outer membrane protein Pal. They form a network linking
CC the inner and outer membranes and the peptidoglycan layer
CC (PubMed:17233825). TolR forms homodimers (PubMed:10419942,
CC PubMed:26354441). Interacts with the N-terminal domain of TolA and with
CC TolQ (PubMed:7744737, PubMed:10419942). {ECO:0000269|PubMed:10419942,
CC ECO:0000269|PubMed:26354441, ECO:0000269|PubMed:7744737,
CC ECO:0000305|PubMed:17233825}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_02203, ECO:0000269|PubMed:8331075, ECO:0000269|PubMed:8376353};
CC Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_02203,
CC ECO:0000269|PubMed:8376353, ECO:0000305|PubMed:8331075}.
CC Note=Accumulates at cell constriction sites. Recruitment to the
CC division site is dependent on FtsN activity.
CC {ECO:0000269|PubMed:17233825}.
CC -!- DOMAIN: The N-terminal transmembrane domain is involved in interaction
CC with TolA and TolQ, while the central and C-terminal domains are
CC involved in dimerization. The C-terminal domain is also involved in
CC interaction with TolA and in association with the membranes
CC (PubMed:10419942). May undergo large scale structural remodeling, where
CC the N- and C-terminal sequences unfold in order for the protein to both
CC reach and bind the peptidoglycan layer around 90 Angstroms away from
CC the inner membrane (PubMed:26354441). {ECO:0000269|PubMed:10419942,
CC ECO:0000269|PubMed:26354441}.
CC -!- DISRUPTION PHENOTYPE: Mutants lacking the tol-pal cluster suffer
CC delayed outer membrane invagination and contain large outer membrane
CC blebs at constriction sites and cell poles (PubMed:17233825). Tol-pal
CC mutants fail to complete division and form cell chains, and fail to
CC process denuded peptidoglycans at the septum (PubMed:32152098).
CC {ECO:0000269|PubMed:17233825, ECO:0000269|PubMed:32152098}.
CC -!- MISCELLANEOUS: There are about 900 TolR molecules per cell.
CC {ECO:0000269|PubMed:24766808}.
CC -!- SIMILARITY: Belongs to the ExbD/TolR family. {ECO:0000255|HAMAP-
CC Rule:MF_02203, ECO:0000305}.
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DR EMBL; M16489; AAA83921.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73832.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35404.1; -; Genomic_DNA.
DR PIR; C25980; BVECTR.
DR RefSeq; NP_415266.1; NC_000913.3.
DR RefSeq; WP_000090097.1; NZ_STEB01000035.1.
DR PDB; 5BY4; X-ray; 1.70 A; A=36-142.
DR PDBsum; 5BY4; -.
DR AlphaFoldDB; P0ABV6; -.
DR SMR; P0ABV6; -.
DR BioGRID; 4261829; 235.
DR BioGRID; 849704; 1.
DR ComplexPortal; CPX-5782; Tol-Pal cell envelope complex.
DR DIP; DIP-48143N; -.
DR IntAct; P0ABV6; 4.
DR STRING; 511145.b0738; -.
DR jPOST; P0ABV6; -.
DR PaxDb; P0ABV6; -.
DR PRIDE; P0ABV6; -.
DR EnsemblBacteria; AAC73832; AAC73832; b0738.
DR EnsemblBacteria; BAA35404; BAA35404; BAA35404.
DR GeneID; 66670992; -.
DR GeneID; 945328; -.
DR KEGG; ecj:JW0728; -.
DR KEGG; eco:b0738; -.
DR PATRIC; fig|1411691.4.peg.1534; -.
DR EchoBASE; EB1004; -.
DR eggNOG; COG0848; Bacteria.
DR HOGENOM; CLU_085305_1_3_6; -.
DR InParanoid; P0ABV6; -.
DR OMA; YITEKAM; -.
DR PhylomeDB; P0ABV6; -.
DR BioCyc; EcoCyc:EG11011-MON; -.
DR PRO; PR:P0ABV6; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0032153; C:cell division site; IDA:EcoCyc.
DR GO; GO:0016021; C:integral component of membrane; IDA:EcoliWiki.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoliWiki.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0043213; P:bacteriocin transport; IMP:EcoliWiki.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IC:ComplexPortal.
DR GO; GO:0015031; P:protein transport; IEA:InterPro.
DR GO; GO:1905153; P:regulation of membrane invagination; IC:ComplexPortal.
DR HAMAP; MF_02203; TolR; 1.
DR InterPro; IPR003400; ExbD.
DR InterPro; IPR014168; Tol-Pal_TolR.
DR PANTHER; PTHR30558; PTHR30558; 1.
DR Pfam; PF02472; ExbD; 1.
DR TIGRFAMs; TIGR02801; tolR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cell inner membrane;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..142
FT /note="Tol-Pal system protein TolR"
FT /id="PRO_0000129140"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:8331075,
FT ECO:0000305|PubMed:8376353"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02203"
FT TOPO_DOM 39..142
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:8376353,
FT ECO:0000305|PubMed:8331075"
FT MUTAGEN 23
FT /note="D->A: Decreases TolA-Pal interaction."
FT /evidence="ECO:0000269|PubMed:11722743"
FT MUTAGEN 23
FT /note="D->E: No change in TolA-Pal interaction."
FT /evidence="ECO:0000269|PubMed:11722743"
FT MUTAGEN 23
FT /note="D->R: Abolishes TolA-Pal interaction."
FT /evidence="ECO:0000269|PubMed:11722743"
FT HELIX 52..57
FT /evidence="ECO:0007829|PDB:5BY4"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:5BY4"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:5BY4"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:5BY4"
FT HELIX 88..101
FT /evidence="ECO:0007829|PDB:5BY4"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:5BY4"
FT HELIX 117..129
FT /evidence="ECO:0007829|PDB:5BY4"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:5BY4"
SQ SEQUENCE 142 AA; 15383 MW; 936FE0033172600B CRC64;
MARARGRGRR DLKSEINIVP LLDVLLVLLL IFMATAPIIT QSVEVDLPDA TESQAVSSND
NPPVIVEVSG IGQYTVVVEK DRLERLPPEQ VVAEVSSRFK ANPKTVFLIG GAKDVPYDEI
IKALNLLHSA GVKSVGLMTQ PI
