TOLA_ECOLI
ID TOLA_ECOLI Reviewed; 421 AA.
AC P19934;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Tol-Pal system protein TolA {ECO:0000305};
GN Name=tolA {ECO:0000303|PubMed:2687247}; Synonyms=cim, excC, lky;
GN OrderedLocusNames=b0739, JW0729;
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, AND TOPOLOGY.
RC STRAIN=K12 / JM105 / ATCC 47016;
RX PubMed=2687247; DOI=10.1128/jb.171.12.6600-6609.1989;
RA Levengood S.K., Webster R.E.;
RT "Nucleotide sequences of the tolA and tolB genes and localization of their
RT products, components of a multistep translocation system in Escherichia
RT coli.";
RL J. Bacteriol. 171:6600-6609(1989).
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 DOMAINS.
RX PubMed=2068069; DOI=10.1073/pnas.88.14.5939;
RA Levengood S.K., Beyer W.F. Jr., Webster R.E.;
RT "TolA: a membrane protein involved in colicin uptake contains an extended
RT helical region.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:5939-5943(1991).
RN [7]
RP FUNCTION.
RX PubMed=8416897; DOI=10.1128/jb.175.1.222-228.1993;
RA Levengood-Freyermuth S.K., Click E.M., Webster R.E.;
RT "Role of the carboxyl-terminal domain of TolA in protein import and
RT integrity of the outer membrane.";
RL J. Bacteriol. 175:222-228(1993).
RN [8]
RP INTERACTION WITH TOLQ AND TOLR.
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 PORINS.
RX PubMed=8978668; DOI=10.1002/j.1460-2075.1996.tb01032.x;
RA Derouiche R., Gavioli M., Benedetti H., Prilipov A., Lazdunski C.,
RA Lloubes R.;
RT "TolA central domain interacts with Escherichia coli porins.";
RL EMBO J. 15:6408-6415(1996).
RN [10]
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 [11]
RP FUNCTION, INTERACTION WITH PAL, AND DOMAIN.
RX PubMed=11115123; DOI=10.1046/j.1365-2958.2000.02190.x;
RA Cascales E., Gavioli M., Sturgis J.N., Lloubes R.;
RT "Proton motive force drives the interaction of the inner membrane TolA and
RT outer membrane pal proteins in Escherichia coli.";
RL Mol. Microbiol. 38:904-915(2000).
RN [12]
RP INTERACTION WITH PAL.
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 [13]
RP FUNCTION, INTERACTION WITH TOLB AND CPOB, AND DOMAIN.
RX PubMed=11994151; DOI=10.1046/j.1365-2958.2002.02895.x;
RA Walburger A., Lazdunski C., Corda Y.;
RT "The Tol/Pal system function requires an interaction between the C-terminal
RT domain of TolA and the N-terminal domain of TolB.";
RL Mol. Microbiol. 44:695-708(2002).
RN [14]
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 [15]
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 [16]
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 [17] {ECO:0007744|PDB:1TOL}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 294-421.
RX PubMed=10404600; DOI=10.1016/s0969-2126(99)80092-6;
RA Lubkowski J., Hennecke F., Plueckthun A., Wlodawer A.;
RT "Filamentous phage infection: crystal structure of g3p in complex with its
RT coreceptor, the C-terminal domain of TolA.";
RL Structure 7:711-722(1999).
RN [18] {ECO:0007744|PDB:1S62}
RP STRUCTURE BY NMR OF 325-421, AND DOMAIN.
RX PubMed=15701516; DOI=10.1016/j.jmb.2004.12.028;
RA Deprez C., Lloubes R., Gavioli M., Marion D., Guerlesquin F., Blanchard L.;
RT "Solution structure of the E.coli TolA C-terminal domain reveals
RT conformational changes upon binding to the phage g3p N-terminal domain.";
RL J. Mol. Biol. 346:1047-1057(2005).
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:8416897,
CC PubMed:11115123, PubMed:11994151, PubMed:17233825). The Tol-Pal system
CC is also required for polar localization of chemoreceptors clusters
CC (PubMed:24720726). The system also appears to be required for the
CC 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). {ECO:0000269|PubMed:11115123,
CC ECO:0000269|PubMed:11994151, ECO:0000269|PubMed:1683466,
CC ECO:0000269|PubMed:17233825, ECO:0000269|PubMed:24720726,
CC ECO:0000269|PubMed:32152098, ECO:0000269|PubMed:8416897,
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). TolA interacts with TolQ and TolR via its N-terminal
CC domain (PubMed:7744737, PubMed:10419942). Interacts with CpoB, and with
CC the trimeric porins OmpC, OmpF, PhoE and LamB via its central domain
CC (PubMed:8978668, PubMed:11994151). Interacts with TolB via its C-
CC terminal domain (PubMed:11994151). Also interacts with Pal via its C-
CC terminal domain. This interaction is proton motive force dependent and
CC requires TolQ and TolR (PubMed:11115123, PubMed:11722743).
CC {ECO:0000269|PubMed:10419942, ECO:0000269|PubMed:11115123,
CC ECO:0000269|PubMed:11722743, ECO:0000269|PubMed:11994151,
CC ECO:0000269|PubMed:7744737, ECO:0000269|PubMed:8978668,
CC ECO:0000305|PubMed:17233825}.
CC -!- INTERACTION:
CC P19934; P0A855: tolB; NbExp=5; IntAct=EBI-1120026, EBI-7180728;
CC P19934; P04480: caa; Xeno; NbExp=6; IntAct=EBI-1120026, EBI-6559916;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:2068069,
CC ECO:0000269|PubMed:2687247}; Single-pass membrane protein
CC {ECO:0000269|PubMed:2687247}. Note=Accumulates at cell constriction
CC sites. Recruitment to the division site is dependent on FtsN activity.
CC {ECO:0000269|PubMed:17233825}.
CC -!- DOMAIN: Contains an N-terminal domain that anchors the protein to the
CC inner membrane, a central domain (domain II), and a C-terminal domain
CC (domain III), which is the functional portion of the protein
CC (PubMed:2068069). The C-terminal domain is involved in interaction with
CC TolB and Pal, and is also involved in direct interaction with colicins
CC and phages. It adapts its conformation upon binding to various partners
CC (PubMed:11115123, PubMed:11994151, PubMed:15701516).
CC {ECO:0000269|PubMed:11115123, ECO:0000269|PubMed:11994151,
CC ECO:0000269|PubMed:15701516, ECO:0000269|PubMed:2068069}.
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 TolA family. {ECO:0000305}.
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DR EMBL; M28232; AAA24683.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73833.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35405.1; -; Genomic_DNA.
DR PIR; JV0057; JV0057.
DR RefSeq; NP_415267.1; NC_000913.3.
DR RefSeq; WP_000030637.1; NZ_STEB01000035.1.
DR PDB; 1S62; NMR; -; A=325-421.
DR PDB; 1TOL; X-ray; 1.85 A; A=295-421.
DR PDB; 3QDP; X-ray; 2.15 A; A=302-421.
DR PDB; 3QDR; X-ray; 2.65 A; A=302-421.
DR PDBsum; 1S62; -.
DR PDBsum; 1TOL; -.
DR PDBsum; 3QDP; -.
DR PDBsum; 3QDR; -.
DR AlphaFoldDB; P19934; -.
DR SMR; P19934; -.
DR BioGRID; 4261827; 179.
DR ComplexPortal; CPX-5782; Tol-Pal cell envelope complex.
DR DIP; DIP-11005N; -.
DR IntAct; P19934; 10.
DR MINT; P19934; -.
DR STRING; 511145.b0739; -.
DR TCDB; 2.C.1.2.1; the tonb-exbb-exbd/tola-tolq-tolr outer membrane receptor energizers and stabilizers (tonb/tola) family.
DR jPOST; P19934; -.
DR PaxDb; P19934; -.
DR PRIDE; P19934; -.
DR EnsemblBacteria; AAC73833; AAC73833; b0739.
DR EnsemblBacteria; BAA35405; BAA35405; BAA35405.
DR GeneID; 66670991; -.
DR GeneID; 946625; -.
DR KEGG; ecj:JW0729; -.
DR KEGG; eco:b0739; -.
DR PATRIC; fig|511145.12.peg.771; -.
DR EchoBASE; EB1000; -.
DR eggNOG; COG3064; Bacteria.
DR HOGENOM; CLU_035992_0_0_6; -.
DR OMA; FNLFRDI; -.
DR PhylomeDB; P19934; -.
DR BioCyc; EcoCyc:EG11007-MON; -.
DR EvolutionaryTrace; P19934; -.
DR PRO; PR:P19934; -.
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:0097718; F:disordered domain specific binding; IPI:CAFA.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0019534; F:toxin transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046790; F:virion binding; IDA:CAFA.
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; IDA:EcoCyc.
DR GO; GO:0071237; P:cellular response to bacteriocin; IMP:EcoCyc.
DR GO; GO:0017038; P:protein import; IMP:EcoliWiki.
DR GO; GO:0015031; P:protein transport; IBA:GO_Central.
DR GO; GO:1905153; P:regulation of membrane invagination; IC:ComplexPortal.
DR GO; GO:0046718; P:viral entry into host cell; IDA:EcoCyc.
DR InterPro; IPR014161; Tol-Pal_TolA.
DR Pfam; PF06519; TolA; 1.
DR TIGRFAMs; TIGR02794; tolA_full; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cell inner membrane;
KW Cell membrane; Disulfide bond; Membrane; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..421
FT /note="Tol-Pal system protein TolA"
FT /id="PRO_0000072622"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:2687247"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..421
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:2687247"
FT REPEAT 224..229
FT /note="1"
FT REPEAT 230..234
FT /note="2"
FT REPEAT 235..240
FT /note="3"
FT REPEAT 241..245
FT /note="4"
FT REPEAT 246..250
FT /note="5"
FT REPEAT 251..255
FT /note="6"
FT REPEAT 256..260
FT /note="7"
FT REPEAT 261..266
FT /note="8"
FT REPEAT 267..271
FT /note="9"
FT REPEAT 272..277
FT /note="10"
FT REPEAT 278..282
FT /note="11"
FT REPEAT 283..287
FT /note="12"
FT REPEAT 288..292
FT /note="13"
FT REGION 48..310
FT /note="Domain II (alpha-helical)"
FT REGION 65..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..292
FT /note="13 X tandem repeats of [EDA]-K(1,2)-A(2,4)"
FT REGION 300..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..421
FT /note="Domain III (functional)"
FT COMPBIAS 69..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 363..388
FT /evidence="ECO:0007744|PDB:1S62, ECO:0007744|PDB:3QDP,
FT ECO:0007744|PDB:3QDR"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:1S62"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:1S62"
FT HELIX 335..349
FT /evidence="ECO:0007829|PDB:1TOL"
FT TURN 350..352
FT /evidence="ECO:0007829|PDB:1S62"
FT HELIX 355..358
FT /evidence="ECO:0007829|PDB:1TOL"
FT STRAND 363..369
FT /evidence="ECO:0007829|PDB:1TOL"
FT TURN 371..373
FT /evidence="ECO:0007829|PDB:1S62"
FT STRAND 375..383
FT /evidence="ECO:0007829|PDB:1TOL"
FT HELIX 385..397
FT /evidence="ECO:0007829|PDB:1TOL"
FT HELIX 406..412
FT /evidence="ECO:0007829|PDB:1TOL"
FT STRAND 416..420
FT /evidence="ECO:0007829|PDB:1TOL"
SQ SEQUENCE 421 AA; 43157 MW; 8B2F52B4B97C655E CRC64;
MSKATEQNDK LKRAIIISAV LHVILFAALI WSSFDENIEA SAGGGGGSSI DAVMVDSGAV
VEQYKRMQSQ ESSAKRSDEQ RKMKEQQAAE ELREKQAAEQ ERLKQLEKER LAAQEQKKQA
EEAAKQAELK QKQAEEAAAK AAADAKAKAE ADAKAAEEAA KKAAADAKKK AEAEAAKAAA
EAQKKAEAAA AALKKKAEAA EAAAAEARKK AATEAAEKAK AEAEKKAAAE KAAADKKAAA
EKAAADKKAA EKAAAEKAAA DKKAAAEKAA ADKKAAAAKA AAEKAAAAKA AAEADDIFGE
LSSGKNAPKT GGGAKGNNAS PAGSGNTKNN GASGADINNY AGQIKSAIES KFYDASSYAG
KTCTLRIKLA PDGMLLDIKP EGGDPALCQA ALAAAKLAKI PKPPSQAVYE VFKNAPLDFK
P
