TATC_ECOLI
ID TATC_ECOLI Reviewed; 258 AA.
AC P69423; P27857; P27858; P76765; P76766; Q2M8E3;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Sec-independent protein translocase protein TatC {ECO:0000255|HAMAP-Rule:MF_00902};
GN Name=tatC {ECO:0000255|HAMAP-Rule:MF_00902}; Synonyms=mttB, yigU, yigV;
GN OrderedLocusNames=b3839, JW3815;
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 CHARACTERIZATION.
RC STRAIN=K12;
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 2-6, AND INTERACTION WITH TATA AND TATB.
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9660752; DOI=10.1074/jbc.273.29.18003;
RA Bogsch E.G., Sargent F., Stanley N.R., Berks B.C., Robinson C., Palmer T.;
RT "An essential component of a novel bacterial protein export system with
RT homologues in plastids and mitochondria.";
RL J. Biol. Chem. 273:18003-18006(1998).
RN [8]
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 [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 MUTAGENESIS OF ARG-17; LEU-20 AND 20-LEU--ASN-22.
RX PubMed=11781311; DOI=10.1074/jbc.m109135200;
RA Allen S.C., Barrett C.M., Ray N., Robinson C.;
RT "Essential cytoplasmic domains in the Escherichia coli TatC protein.";
RL J. Biol. Chem. 277:10362-10366(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 MUTAGENESIS OF PHE-94; GLU-103 AND ASP-211.
RX PubMed=11952898; DOI=10.1046/j.1365-2958.2002.02853.x;
RA Buchanan G., Leeuw E., Stanley N.R., Wexler M., Berks B.C., Sargent F.,
RA Palmer T.;
RT "Functional complexity of the twin-arginine translocase TatC component
RT revealed by site-directed mutagenesis.";
RL Mol. Microbiol. 43:1457-1470(2002).
RN [14]
RP TOPOLOGY.
RC STRAIN=K12 / JM109 / ATCC 53323;
RX PubMed=11867724; DOI=10.1073/pnas.052018199;
RA Drew D., Sjoestrand D., Nilsson J., Urbig T., Chin C.-N., de Gier J.-W.,
RA von Heijne G.;
RT "Rapid topology mapping of Escherichia coli inner-membrane proteins by
RT prediction and PhoA/GFP fusion analysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:2690-2695(2002).
RN [15]
RP FUNCTION.
RX PubMed=14580344; DOI=10.1016/s1097-2765(03)00398-8;
RA Alami M., Luke I., Deitermann S., Eisner G., Koch H.G., Brunner J.,
RA Muller M.;
RT "Differential interactions between a twin-arginine signal peptide and its
RT translocase in Escherichia coli.";
RL Mol. Cell 12:937-946(2003).
RN [16]
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 [17]
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 [18]
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 [19]
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 [20]
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 [21]
RP FUNCTION, AND SUBSTRATE-BINDING.
RX PubMed=19666509; DOI=10.1073/pnas.0901566106;
RA Tarry M.J., Schafer E., Chen S., Buchanan G., Greene N.P., Lea S.M.,
RA Palmer T., Saibil H.R., Berks B.C.;
RT "Structural analysis of substrate binding by the TatBC component of the
RT twin-arginine protein transport system.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:13284-13289(2009).
RN [22]
RP FUNCTION.
RX PubMed=20926683; DOI=10.1091/mbc.e10-07-0585;
RA Maurer C., Panahandeh S., Jungkamp A.C., Moser M., Muller M.;
RT "TatB functions as an oligomeric binding site for folded Tat precursor
RT proteins.";
RL Mol. Biol. Cell 21:4151-4161(2010).
RN [23]
RP SUBUNIT, INTERACTION WITH DMSA AND DMSD, AND SUBCELLULAR LOCATION.
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. Together with
CC TatB, TatC is part of a receptor directly interacting with Tat signal
CC peptides. {ECO:0000255|HAMAP-Rule:MF_00902,
CC ECO:0000269|PubMed:11922668, ECO:0000269|PubMed:14580344,
CC ECO:0000269|PubMed:19666509, ECO:0000269|PubMed:20926683,
CC ECO:0000269|PubMed:9660752}.
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 TatC can form a distinct, stable, multimeric complex independent of
CC TatA and TatB. Each of TatA, TatB and TatC are able to interact in
CC pairs without the third partner. Interacts with the signal sequence of
CC DmsA and DmsD. {ECO:0000255|HAMAP-Rule:MF_00902,
CC ECO:0000269|PubMed:11279240, ECO:0000269|PubMed:15225613,
CC ECO:0000269|PubMed:15571732, ECO:0000269|PubMed:15663945,
CC ECO:0000269|PubMed:17686475, ECO:0000269|PubMed:20169075}.
CC -!- INTERACTION:
CC P69423; P69428: tatA; NbExp=2; IntAct=EBI-4411641, EBI-4411542;
CC P69423; P69425: tatB; NbExp=9; IntAct=EBI-4411641, EBI-4411577;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00902, ECO:0000269|PubMed:11591389,
CC ECO:0000269|PubMed:15225613, ECO:0000269|PubMed:20169075}; Multi-pass
CC membrane protein {ECO:0000255|HAMAP-Rule:MF_00902,
CC ECO:0000269|PubMed:11591389, ECO:0000269|PubMed:15225613,
CC ECO:0000269|PubMed:20169075}. Note=Localizes at the cell poles.
CC -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:11160116}.
CC -!- DISRUPTION PHENOTYPE: Disruption blocks the export of at least five
CC twin-arginine-containing precursor proteins that are predicted to bind
CC redox cofactors, and hence fold prior to translocation. Disruption does
CC not affect the Sec pathway. {ECO:0000269|PubMed:9660752}.
CC -!- SIMILARITY: Belongs to the TatC family. {ECO:0000255|HAMAP-
CC Rule:MF_00902}.
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DR EMBL; AJ005830; CAA06726.1; -; Genomic_DNA.
DR EMBL; AF067848; AAC19242.1; -; Genomic_DNA.
DR EMBL; M87049; AAA67634.1; ALT_FRAME; Genomic_DNA.
DR EMBL; M87049; AAA67635.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAC76842.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77463.1; -; Genomic_DNA.
DR PIR; H65188; H65188.
DR PIR; S30728; S30728.
DR RefSeq; NP_418282.1; NC_000913.3.
DR RefSeq; WP_000109943.1; NZ_STEB01000021.1.
DR AlphaFoldDB; P69423; -.
DR SMR; P69423; -.
DR BioGRID; 4259567; 437.
DR ComplexPortal; CPX-3445; Twin-arginine translocation complex.
DR DIP; DIP-58537N; -.
DR IntAct; P69423; 7.
DR MINT; P69423; -.
DR STRING; 511145.b3839; -.
DR TCDB; 2.A.64.1.1; the twin arginine targeting (tat) family.
DR PaxDb; P69423; -.
DR PRIDE; P69423; -.
DR EnsemblBacteria; AAC76842; AAC76842; b3839.
DR EnsemblBacteria; BAE77463; BAE77463; BAE77463.
DR GeneID; 66672254; -.
DR GeneID; 948328; -.
DR KEGG; ecj:JW3815; -.
DR KEGG; eco:b3839; -.
DR PATRIC; fig|1411691.4.peg.2870; -.
DR EchoBASE; EB1445; -.
DR eggNOG; COG0805; Bacteria.
DR HOGENOM; CLU_031942_1_1_6; -.
DR InParanoid; P69423; -.
DR OMA; EMSFLDH; -.
DR PhylomeDB; P69423; -.
DR BioCyc; EcoCyc:EG11479-MON; -.
DR BioCyc; MetaCyc:EG11479-MON; -.
DR PRO; PR:P69423; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IDA:EcoliWiki.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
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; IMP: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 GO; GO:0009314; P:response to radiation; IMP:EcoCyc.
DR HAMAP; MF_00902; TatC; 1.
DR InterPro; IPR019820; Sec-indep_translocase_CS.
DR InterPro; IPR002033; TatC.
DR PANTHER; PTHR30371; PTHR30371; 1.
DR Pfam; PF00902; TatC; 1.
DR PRINTS; PR01840; TATCFAMILY.
DR TIGRFAMs; TIGR00945; tatC; 1.
DR PROSITE; PS01218; TATC; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Direct protein sequencing; Membrane;
KW Protein transport; Reference proteome; Translocation; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11279240"
FT CHAIN 2..258
FT /note="Sec-independent protein translocase protein TatC"
FT /id="PRO_0000098083"
FT TOPO_DOM 2..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT TOPO_DOM 45..75
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT TOPO_DOM 97..115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT TOPO_DOM 137..156
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT TOPO_DOM 178..192
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..210
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT TOPO_DOM 211
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT TOPO_DOM 233..258
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MUTAGEN 17
FT /note="R->A: No anaerobic growth and no TorA export."
FT /evidence="ECO:0000269|PubMed:11781311"
FT MUTAGEN 20..22
FT /note="Missing: No anaerobic growth and 75% decrease in
FT TorA export."
FT /evidence="ECO:0000269|PubMed:11781311"
FT MUTAGEN 20
FT /note="L->A: 25% decrease in anaerobic growth and 75%
FT decrease in TorA export."
FT /evidence="ECO:0000269|PubMed:11781311"
FT MUTAGEN 94
FT /note="F->A,L: Loss of function."
FT /evidence="ECO:0000269|PubMed:11952898"
FT MUTAGEN 94
FT /note="F->A: Export of TorA restored; when associated with
FT A-211."
FT /evidence="ECO:0000269|PubMed:11952898"
FT MUTAGEN 103
FT /note="E->A,D,R: Loss of function."
FT /evidence="ECO:0000269|PubMed:11952898"
FT MUTAGEN 103
FT /note="E->A: Export of TorA restored; when associated with
FT A-211."
FT /evidence="ECO:0000269|PubMed:11952898"
FT MUTAGEN 103
FT /note="E->Q: Severely retard but does not abolish
FT activity."
FT /evidence="ECO:0000269|PubMed:11952898"
FT MUTAGEN 211
FT /note="D->A: Export activity of TorA blocked. Export of
FT TorA restored; when associated with A-94 or A-103."
FT /evidence="ECO:0000269|PubMed:11952898"
FT MUTAGEN 211
FT /note="D->E,N: Decrease in TorA export activity."
FT /evidence="ECO:0000269|PubMed:11952898"
SQ SEQUENCE 258 AA; 28876 MW; D2383F85AF62A81C CRC64;
MSVEDTQPLI THLIELRKRL LNCIIAVIVI FLCLVYFAND IYHLVSAPLI KQLPQGSTMI
ATDVASPFFT PIKLTFMVSL ILSAPVILYQ VWAFIAPALY KHERRLVVPL LVSSSLLFYI
GMAFAYFVVF PLAFGFLANT APEGVQVSTD IASYLSFVMA LFMAFGVSFE VPVAIVLLCW
MGITSPEDLR KKRPYVLVGA FVVGMLLTPP DVFSQTLLAI PMYCLFEIGV FFSRFYVGKG
RNREEENDAE AESEKTEE
