TATA_ECOLI
ID TATA_ECOLI Reviewed; 89 AA.
AC P69428; O65938; P27856; Q2M8E1;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Sec-independent protein translocase protein TatA {ECO:0000255|HAMAP-Rule:MF_00236};
GN Name=tatA {ECO:0000255|HAMAP-Rule:MF_00236}; Synonyms=mttA1, yigT;
GN OrderedLocusNames=b3836, JW3813;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=9649434; DOI=10.1093/emboj/17.13.3640;
RA Sargent F., Bogsch E.G., Stanley N.R., Wexler M., Robinson C., Berks B.C.,
RA Palmer T.;
RT "Overlapping functions of components of a bacterial Sec-independent protein
RT export pathway.";
RL EMBO J. 17:3640-3650(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33694 / HB101;
RX PubMed=9546395; DOI=10.1016/s0092-8674(00)81149-6;
RA Weiner J.H., Bilous P.T., Shaw G.M., Lubitz S.P., Frost L., Thomas G.H.,
RA Cole J.A., Turner R.J.;
RT "A novel and ubiquitous system for membrane targeting and secretion of
RT cofactor-containing proteins.";
RL Cell 93:93-101(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=1379743; DOI=10.1126/science.1379743;
RA Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
RT "Analysis of the Escherichia coli genome: DNA sequence of the region from
RT 84.5 to 86.5 minutes.";
RL Science 257:771-778(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
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].
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 PROTEIN SEQUENCE OF 1-6, AND INTERACTION WITH TATB AND TATC.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=11279240; DOI=10.1074/jbc.m100682200;
RA Bolhuis A., Mathers J.E., Thomas J.D., Barrett C.M., Robinson C.;
RT "TatB and TatC form a functional and structural unit of the twin-arginine
RT translocase from Escherichia coli.";
RL J. Biol. Chem. 276:20213-20219(2001).
RN [7]
RP REVIEW.
RX PubMed=10652088; DOI=10.1046/j.1365-2958.2000.01719.x;
RA Berks B.C., Sargent F., Palmer T.;
RT "The Tat protein export pathway.";
RL Mol. Microbiol. 35:260-274(2000).
RN [8]
RP COMPLEX BETWEEN TATA AND TATB.
RX PubMed=11422364; DOI=10.1046/j.1432-1327.2001.02263.x;
RA Sargent F., Gohlke U., De Leeuw E., Stanley N.R., Palmer T., Saibil H.R.,
RA Berks B.C.;
RT "Purified components of the Escherichia coli Tat protein transport system
RT form a double-layered ring structure.";
RL Eur. J. Biochem. 268:3361-3367(2001).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=11591389; DOI=10.1016/s0014-5793(01)02904-0;
RA De Leeuw E., Porcelli I., Sargent F., Palmer T., Berks B.C.;
RT "Membrane interactions and self-association of the TatA and TatB components
RT of the twin-arginine translocation pathway.";
RL FEBS Lett. 506:143-148(2001).
RN [10]
RP INDUCTION.
RX PubMed=11160116; DOI=10.1128/jb.183.5.1801-1804.2001;
RA Jack R.L., Sargent F., Berks B.C., Sawers G., Palmer T.;
RT "Constitutive expression of Escherichia coli tat genes indicates an
RT important role for the twin-arginine translocase during aerobic and
RT anaerobic growth.";
RL J. Bacteriol. 183:1801-1804(2001).
RN [11]
RP TOPOLOGY, AND TATA HOMOOLIGOMERIC COMPLEXES.
RX PubMed=12427031; DOI=10.1021/bi026142i;
RA Porcelli I., de Leeuw E., Wallis R., van den Brink-van der Laan E.,
RA de Kruijff B., Wallace B.A., Palmer T., Berks B.C.;
RT "Characterization and membrane assembly of the TatA component of the
RT Escherichia coli twin-arginine protein transport system.";
RL Biochemistry 41:13690-13697(2002).
RN [12]
RP FUNCTION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=11922668; DOI=10.1006/jmbi.2002.5431;
RA Ize B., Gerard F., Zhang M., Chanal A., Voulhoux R., Palmer T., Filloux A.,
RA Wu L.F.;
RT "In vivo dissection of the Tat translocation pathway in Escherichia coli.";
RL J. Mol. Biol. 317:327-335(2002).
RN [13]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=15225613; DOI=10.1016/j.febslet.2004.05.054;
RA Berthelmann F., Bruser T.;
RT "Localization of the Tat translocon components in Escherichia coli.";
RL FEBS Lett. 569:82-88(2004).
RN [14]
RP SUBUNIT.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=15663945; DOI=10.1016/j.jmb.2004.11.047;
RA Oates J., Barrett C.M., Barnett J.P., Byrne K.G., Bolhuis A., Robinson C.;
RT "The Escherichia coli twin-arginine translocation apparatus incorporates a
RT distinct form of TatABC complex, spectrum of modular TatA complexes and
RT minor TatAB complex.";
RL J. Mol. Biol. 346:295-305(2005).
RN [15]
RP SUBUNIT.
RX PubMed=15571732; DOI=10.1016/j.jmb.2004.10.043;
RA Mangels D., Mathers J.E., Bolhuis A., Robinson C.;
RT "The core TatABC complex of the twin-arginine translocase in Escherichia
RT coli: TatC drives assembly whereas TatA is essential for stability.";
RL J. Mol. Biol. 345:415-423(2005).
RN [16]
RP ARCHITECTURE OF THE TATA COMPLEX BY ELECTRON MICROSCOPY.
RX PubMed=16027357; DOI=10.1073/pnas.0503558102;
RA Gohlke U., Pullan L., McDevitt C.A., Porcelli I., de Leeuw E., Palmer T.,
RA Saibil H.R., Berks B.C.;
RT "The TatA component of the twin-arginine protein transport system forms
RT channel complexes of variable diameter.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:10482-10486(2005).
RN [17]
RP SUBUNIT.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=17686475; DOI=10.1016/j.febslet.2007.07.044;
RA Orriss G.L., Tarry M.J., Ize B., Sargent F., Lea S.M., Palmer T.,
RA Berks B.C.;
RT "TatBC, TatB, and TatC form structurally autonomous units within the twin
RT arginine protein transport system of Escherichia coli.";
RL FEBS Lett. 581:4091-4097(2007).
RN [18]
RP SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PHE-39.
RX PubMed=20169075; DOI=10.1371/journal.pone.0009225;
RA Kostecki J.S., Li H., Turner R.J., DeLisa M.P.;
RT "Visualizing interactions along the Escherichia coli twin-arginine
RT translocation pathway using protein fragment complementation.";
RL PLoS ONE 5:E9225-E9225(2010).
CC -!- FUNCTION: Part of the twin-arginine translocation (Tat) system that
CC transports large folded proteins containing a characteristic twin-
CC arginine motif in their signal peptide across membranes. TatA could
CC form the protein-conducting channel of the Tat system.
CC {ECO:0000255|HAMAP-Rule:MF_00236, ECO:0000269|PubMed:11922668,
CC ECO:0000269|PubMed:9649434}.
CC -!- SUBUNIT: The Tat system comprises two distinct complexes: a TatABC
CC complex, containing multiple copies of TatA, TatB and TatC subunits,
CC and a separate TatA complex, containing only TatA subunits. Substrates
CC initially bind to the TatABC complex, which probably triggers
CC association of the separate TatA complex to form the active translocon.
CC A complex containing only TatA and TatB has also been identified. It
CC could be either an assembly intermediate or a disassembly intermediate
CC generated during translocation activity. Each of TatA, TatB and TatC
CC are able to interact in pairs without the third partner; TatA also
CC forms homooligomers. {ECO:0000255|HAMAP-Rule:MF_00236,
CC ECO:0000269|PubMed:15225613, ECO:0000269|PubMed:15571732,
CC ECO:0000269|PubMed:15663945, ECO:0000269|PubMed:17686475,
CC ECO:0000269|PubMed:20169075}.
CC -!- INTERACTION:
CC P69428; P69423: tatC; NbExp=2; IntAct=EBI-4411542, EBI-4411641;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00236, ECO:0000269|PubMed:11591389,
CC ECO:0000269|PubMed:15225613, ECO:0000269|PubMed:20169075}; Single-pass
CC membrane protein {ECO:0000255|HAMAP-Rule:MF_00236,
CC ECO:0000269|PubMed:11591389, ECO:0000269|PubMed:15225613,
CC ECO:0000269|PubMed:20169075}; Cytoplasmic side
CC {ECO:0000269|PubMed:11591389, ECO:0000269|PubMed:15225613,
CC ECO:0000269|PubMed:20169075}. Note=Abundant all over the membrane, but
CC is more concentrated at the cell poles.
CC -!- INDUCTION: Constitutively expressed. TatA is the most highly expressed
CC of the tat genes. {ECO:0000269|PubMed:11160116}.
CC -!- DISRUPTION PHENOTYPE: Disruption of tatA affects the correct
CC localization of multiple enzymes whose precursors bear twin arginine
CC transfer peptides. Export is completely blocked when both tatA and tatE
CC are inactivated. {ECO:0000269|PubMed:9649434}.
CC -!- MISCELLANEOUS: TatA forms a transmembrane channel with a lid structure
CC on the cytoplasmic side. The number of TatA protomers can vary so that
CC the channel can adopt different diameters to accommodate substrates of
CC various sizes. This enables TatA to pack tightly around substrate and
CC prevents ion leakage during transport.
CC -!- MISCELLANEOUS: Absence of TatA from the TatBC complex leads to the
CC instability of the complex and the specific breakdown of TatB.
CC -!- SIMILARITY: Belongs to the TatA/E family. {ECO:0000255|HAMAP-
CC Rule:MF_00236}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA67633.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAC19240.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ005830; CAA06724.1; -; Genomic_DNA.
DR EMBL; AF067848; AAC19240.1; ALT_INIT; Genomic_DNA.
DR EMBL; M87049; AAA67633.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAC76839.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77465.1; -; Genomic_DNA.
DR PIR; E65188; E65188.
DR PIR; S30727; S30727.
DR RefSeq; NP_418280.4; NC_000913.3.
DR RefSeq; WP_001295260.1; NZ_STEB01000021.1.
DR PDB; 2LZR; NMR; -; A=1-49.
DR PDB; 2LZS; NMR; -; A/B/C/D/E/F/G/H/I=1-49.
DR PDB; 2MN6; NMR; -; A/B=1-89.
DR PDB; 2MN7; NMR; -; A=1-89.
DR PDBsum; 2LZR; -.
DR PDBsum; 2LZS; -.
DR PDBsum; 2MN6; -.
DR PDBsum; 2MN7; -.
DR AlphaFoldDB; P69428; -.
DR BMRB; P69428; -.
DR SMR; P69428; -.
DR BioGRID; 4263055; 402.
DR ComplexPortal; CPX-3445; Twin-arginine translocation complex.
DR DIP; DIP-10958N; -.
DR IntAct; P69428; 3.
DR MINT; P69428; -.
DR STRING; 511145.b3836; -.
DR TCDB; 2.A.64.1.1; the twin arginine targeting (tat) family.
DR jPOST; P69428; -.
DR PaxDb; P69428; -.
DR PRIDE; P69428; -.
DR EnsemblBacteria; AAC76839; AAC76839; b3836.
DR EnsemblBacteria; BAE77465; BAE77465; BAE77465.
DR GeneID; 67414378; -.
DR GeneID; 948321; -.
DR KEGG; ecj:JW3813; -.
DR KEGG; eco:b3836; -.
DR PATRIC; fig|511145.12.peg.3952; -.
DR eggNOG; COG1826; Bacteria.
DR HOGENOM; CLU_086034_5_1_6; -.
DR InParanoid; P69428; -.
DR OMA; GGISIWN; -.
DR PhylomeDB; P69428; -.
DR BioCyc; EcoCyc:TATA; -.
DR BioCyc; MetaCyc:TATA; -.
DR PRO; PR:P69428; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; 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:0005886; C:plasma membrane; IC:ComplexPortal.
DR GO; GO:0033281; C:TAT protein transport complex; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IGI:EcoliWiki.
DR GO; GO:0009977; F:proton motive force dependent protein transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0065002; P:intracellular protein transmembrane transport; IDA:EcoCyc.
DR GO; GO:0043953; P:protein transport by the Tat complex; IDA:EcoCyc.
DR DisProt; DP00834; -.
DR HAMAP; MF_00236; TatA_E; 1.
DR InterPro; IPR003369; TatA/B/E.
DR InterPro; IPR006312; TatA/E.
DR Pfam; PF02416; TatA_B_E; 1.
DR TIGRFAMs; TIGR01411; tatAE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane;
KW Direct protein sequencing; Membrane; Protein transport; Reference proteome;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..89
FT /note="Sec-independent protein translocase protein TatA"
FT /id="PRO_0000097934"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00236"
FT REGION 65..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 39
FT /note="F->A: Homooligomerizes more efficiently than wt,
FT blocks translocation."
FT /evidence="ECO:0000269|PubMed:20169075"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:2LZS"
FT HELIX 6..32
FT /evidence="ECO:0007829|PDB:2LZR"
FT HELIX 34..42
FT /evidence="ECO:0007829|PDB:2LZR"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:2LZS"
SQ SEQUENCE 89 AA; 9664 MW; 4874F393EFFADC1B CRC64;
MGGISIWQLL IIAVIVVLLF GTKKLGSIGS DLGASIKGFK KAMSDDEPKQ DKTSQDADFT
AKTIADKQAD TNQEQAKTED AKRHDKEQV
