TATB_ECOLI
ID TATB_ECOLI Reviewed; 171 AA.
AC P69425; O69415; O87926; P27856; Q2M8E2;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Sec-independent protein translocase protein TatB {ECO:0000255|HAMAP-Rule:MF_00237};
GN Name=tatB {ECO:0000255|HAMAP-Rule:MF_00237}; Synonyms=mttA2, ysgB;
GN OrderedLocusNames=b3838, JW5580;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 1-5, AND INTERACTION WITH TATA 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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10593889; DOI=10.1074/jbc.274.51.36073;
RA Sargent F., Stanley N.R., Berks B.C., Palmer T.;
RT "Sec-independent protein translocation in Escherichia coli. A distinct and
RT pivotal role for the TatB protein.";
RL J. Biol. Chem. 274:36073-36082(1999).
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 SUBUNIT, AND 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 [10]
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 [11]
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 [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 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 [14]
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 [15]
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 [16]
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 [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 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 [19]
RP FUNCTION, AND SUBSTRATE BINDING.
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 [20]
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).
RN [21]
RP DOMAIN.
RX PubMed=21237157; DOI=10.1016/j.febslet.2011.01.016;
RA Maldonado B., Kneuper H., Buchanan G., Hatzixanthis K., Sargent F.,
RA Berks B.C., Palmer T.;
RT "Characterisation of the membrane-extrinsic domain of the TatB component of
RT the twin arginine protein translocase.";
RL FEBS Lett. 585:478-484(2011).
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 TatC, TatB is part of a receptor directly interacting with Tat signal
CC peptides. TatB may form an oligomeric binding site that transiently
CC accommodates folded Tat precursor proteins before their translocation.
CC {ECO:0000255|HAMAP-Rule:MF_00237, ECO:0000269|PubMed:10593889,
CC ECO:0000269|PubMed:11922668, ECO:0000269|PubMed:14580344,
CC ECO:0000269|PubMed:19666509, ECO:0000269|PubMed:20926683}.
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; TatB also
CC forms homooligomers. Interacts with the signal sequence of DmsA and
CC DmsD. {ECO:0000255|HAMAP-Rule:MF_00237, ECO:0000269|PubMed:11279240,
CC ECO:0000269|PubMed:11422364, 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 P69425; P69425: tatB; NbExp=3; IntAct=EBI-4411577, EBI-4411577;
CC P69425; P69423: tatC; NbExp=9; IntAct=EBI-4411577, EBI-4411641;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00237, ECO:0000269|PubMed:11591389,
CC ECO:0000269|PubMed:15225613, ECO:0000269|PubMed:20169075}; Single-pass
CC membrane protein {ECO:0000255|HAMAP-Rule:MF_00237,
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 -!- DOMAIN: The membrane-extrinsic domain forms parallel contacts with at
CC least one other TatB protein. {ECO:0000269|PubMed:21237157}.
CC -!- DISRUPTION PHENOTYPE: Disruption blocks the export of seven endogenous
CC Tat substrates. {ECO:0000269|PubMed:10593889}.
CC -!- SIMILARITY: Belongs to the TatB family. {ECO:0000255|HAMAP-
CC Rule:MF_00237}.
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DR EMBL; AJ005830; CAA06725.1; -; Genomic_DNA.
DR EMBL; AF067848; AAC19241.1; -; Genomic_DNA.
DR EMBL; M87049; AAA67633.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U00096; AAT48228.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77464.1; -; Genomic_DNA.
DR PIR; G91224; G91224.
DR RefSeq; WP_000459594.1; NZ_STEB01000021.1.
DR RefSeq; YP_026270.1; NC_000913.3.
DR AlphaFoldDB; P69425; -.
DR SMR; P69425; -.
DR BioGRID; 4262617; 402.
DR ComplexPortal; CPX-3445; Twin-arginine translocation complex.
DR DIP; DIP-58536N; -.
DR IntAct; P69425; 7.
DR MINT; P69425; -.
DR STRING; 511145.b3838; -.
DR TCDB; 2.A.64.1.1; the twin arginine targeting (tat) family.
DR jPOST; P69425; -.
DR PaxDb; P69425; -.
DR PRIDE; P69425; -.
DR EnsemblBacteria; AAT48228; AAT48228; b3838.
DR EnsemblBacteria; BAE77464; BAE77464; BAE77464.
DR GeneID; 66672255; -.
DR GeneID; 948319; -.
DR KEGG; ecj:JW5580; -.
DR KEGG; eco:b3838; -.
DR PATRIC; fig|1411691.4.peg.2871; -.
DR EchoBASE; EB4068; -.
DR eggNOG; COG1826; Bacteria.
DR HOGENOM; CLU_086034_1_0_6; -.
DR InParanoid; P69425; -.
DR OMA; GQFQEAM; -.
DR PhylomeDB; P69425; -.
DR BioCyc; EcoCyc:G7808-MON; -.
DR BioCyc; MetaCyc:G7808-MON; -.
DR PRO; PR:P69425; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
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: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 HAMAP; MF_00237; TatB; 1.
DR InterPro; IPR018448; TatB.
DR TIGRFAMs; TIGR01410; tatB; 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 CHAIN 1..171
FT /note="Sec-independent protein translocase protein TatB"
FT /id="PRO_0000192653"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00237"
FT REGION 117..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 171 AA; 18421 MW; 31F1405404F5DABF CRC64;
MFDIGFSELL LVFIIGLVVL GPQRLPVAVK TVAGWIRALR SLATTVQNEL TQELKLQEFQ
DSLKKVEKAS LTNLTPELKA SMDELRQAAE SMKRSYVAND PEKASDEAHT IHNPVVKDNE
AAHEGVTPAA AQTQASSPEQ KPETTPEPVV KPAADAEPKT AAPSPSSSDK P
