TOLQ_ECOLI
ID TOLQ_ECOLI Reviewed; 230 AA.
AC P0ABU9; P05828;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Tol-Pal system protein TolQ {ECO:0000255|HAMAP-Rule:MF_02202, ECO:0000305};
GN Name=tolQ {ECO:0000255|HAMAP-Rule:MF_02202, ECO:0000303|PubMed:3294803};
GN Synonyms=fii {ECO:0000303|PubMed:3294803}; OrderedLocusNames=b0737, JW0727;
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=8300535; DOI=10.1128/jb.176.3.822-829.1994;
RA Vianney A., Lewin T.M., Beyer W.F. Jr., Lazzaroni J.C., Portalier R.,
RA Webster R.E.;
RT "Membrane topology and mutational analysis of the TolQ protein of
RT Escherichia coli required for the uptake of macromolecules and cell
RT envelope integrity.";
RL J. Bacteriol. 176:822-829(1994).
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 INTERACTION WITH TOLR.
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 ALA-177.
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 TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [12]
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 [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 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).
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 TolR, 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). Is involved in the uptake of
CC group A colicins (colicins A, E1, E2, E3, and K) and in the uptake of
CC filamentous phage DNA (PubMed:1683466, PubMed:3294803).
CC {ECO:0000269|PubMed:11722743, ECO:0000269|PubMed:1683466,
CC ECO:0000269|PubMed:17233825, ECO:0000269|PubMed:24720726,
CC ECO:0000269|PubMed:32152098, ECO:0000269|PubMed:3294803,
CC ECO:0000305|PubMed:1683466}.
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). TolQ interacts with the N-terminal domain of TolA
CC and with TolR (PubMed:7744737, PubMed:10419942).
CC {ECO:0000269|PubMed:10419942, ECO:0000269|PubMed:7744737,
CC ECO:0000305|PubMed:17233825}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_02202, ECO:0000269|PubMed:8300535, ECO:0000269|PubMed:8331075};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_02202,
CC ECO:0000269|PubMed:8300535, 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 -!- 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 -!- SIMILARITY: Belongs to the ExbB/TolQ family. {ECO:0000255|HAMAP-
CC Rule:MF_02202, ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M16489; AAA83919.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73831.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35403.1; -; Genomic_DNA.
DR PIR; B25980; BVECTQ.
DR RefSeq; NP_415265.1; NC_000913.3.
DR RefSeq; WP_000131314.1; NZ_STEB01000035.1.
DR AlphaFoldDB; P0ABU9; -.
DR SMR; P0ABU9; -.
DR BioGRID; 4259453; 275.
DR ComplexPortal; CPX-5782; Tol-Pal cell envelope complex.
DR DIP; DIP-11008N; -.
DR STRING; 511145.b0737; -.
DR TCDB; 1.A.30.2.2; the h(+)- or na(+)-translocating bacterial flagellar motor/exbbd outer membrane transport energizer (mot/exb) superfamily.
DR jPOST; P0ABU9; -.
DR PaxDb; P0ABU9; -.
DR PRIDE; P0ABU9; -.
DR EnsemblBacteria; AAC73831; AAC73831; b0737.
DR EnsemblBacteria; BAA35403; BAA35403; BAA35403.
DR GeneID; 67413776; -.
DR GeneID; 948900; -.
DR KEGG; ecj:JW0727; -.
DR KEGG; eco:b0737; -.
DR PATRIC; fig|1411691.4.peg.1535; -.
DR EchoBASE; EB1003; -.
DR eggNOG; COG0811; Bacteria.
DR HOGENOM; CLU_053325_2_2_6; -.
DR InParanoid; P0ABU9; -.
DR OMA; SWTYIFR; -.
DR PhylomeDB; P0ABU9; -.
DR BioCyc; EcoCyc:EG11010-MON; -.
DR PRO; PR:P0ABU9; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0032153; C:cell division site; IDA:EcoCyc.
DR GO; GO:0030313; C:cell envelope; 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:EcoCyc.
DR GO; GO:0043213; P:bacteriocin transport; IMP:EcoCyc.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IC:ComplexPortal.
DR GO; GO:0017038; P:protein import; IMP:EcoliWiki.
DR GO; GO:1905153; P:regulation of membrane invagination; IC:ComplexPortal.
DR HAMAP; MF_02202; TolQ; 1.
DR InterPro; IPR002898; MotA_ExbB_proton_chnl.
DR InterPro; IPR014163; Tol-Pal_TolQ.
DR Pfam; PF01618; MotA_ExbB; 1.
DR TIGRFAMs; TIGR02796; tolQ; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..230
FT /note="Tol-Pal system protein TolQ"
FT /id="PRO_0000145822"
FT TOPO_DOM 1..15
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:8300535,
FT ECO:0000305|PubMed:8331075"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02202"
FT TOPO_DOM 37..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8300535,
FT ECO:0000305|PubMed:8331075"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02202"
FT TOPO_DOM 160..170
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:8300535,
FT ECO:0000305|PubMed:8331075"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02202"
FT TOPO_DOM 192..230
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996,
FT ECO:0000269|PubMed:8300535, ECO:0000305|PubMed:8331075"
FT MUTAGEN 177
FT /note="A->V: Significantly reduces TolA-Pal interaction."
FT /evidence="ECO:0000269|PubMed:11722743"
SQ SEQUENCE 230 AA; 25598 MW; F4356F6C5B0F753C CRC64;
MTDMNILDLF LKASLLVKLI MLILIGFSIA SWAIIIQRTR ILNAAAREAE AFEDKFWSGI
ELSRLYQESQ GKRDNLTGSE QIFYSGFKEF VRLHRANSHA PEAVVEGASR AMRISMNREL
ENLETHIPFL GTVGSISPYI GLFGTVWGIM HAFIALGAVK QATLQMVAPG IAEALIATAI
GLFAAIPAVM AYNRLNQRVN KLELNYDNFM EEFTAILHRQ AFTVSESNKG
