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Protein

Sec-independent protein translocase protein TatB

Gene

tatB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation.UniRule annotation5 Publications

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • proton motive force dependent protein transmembrane transporter activity Source: EcoCyc

GO - Biological processi

  • intracellular protein transmembrane transport Source: EcoCyc
  • protein secretion Source: InterPro
  • protein transport by the Tat complex Source: EcoCyc
Complete GO annotation...

Keywords - Biological processi

Protein transport, Translocation, Transport

Enzyme and pathway databases

BioCyciEcoCyc:G7808-MONOMER.
ECOL316407:JW5580-MONOMER.
MetaCyc:G7808-MONOMER.

Protein family/group databases

TCDBi2.A.64.1.1. the twin arginine targeting (tat) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Sec-independent protein translocase protein TatBUniRule annotation
Gene namesi
Name:tatBUniRule annotation
Synonyms:mttA2, ysgB
Ordered Locus Names:b3838, JW5580
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG14322. tatB.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei1 – 2121HelicalUniRule annotationAdd
BLAST

GO - Cellular componenti

  • integral component of plasma membrane Source: EcoCyc
  • intracellular Source: GOC
  • TAT protein transport complex Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Disruption blocks the export of seven endogenous Tat substrates.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 171171Sec-independent protein translocase protein TatBPRO_0000192653Add
BLAST

Proteomic databases

PaxDbiP69425.
PRIDEiP69425.

Expressioni

Inductioni

Constitutively expressed.1 Publication

Interactioni

Subunit structurei

The Tat system comprises two distinct complexes: a TatABC complex, containing multiple copies of TatA, TatB and TatC subunits, and a separate TatA complex, containing only TatA subunits. Substrates initially bind to the TatABC complex, which probably triggers association of the separate TatA complex to form the active translocon. A complex containing only TatA and TatB has also been identified. It could be either an assembly intermediate or a disassembly intermediate generated during translocation activity. Each of TatA, TatB and TatC are able to interact in pairs without the third partner; TatB also forms homooligomers. Interacts with the signal sequence of DmsA and DmsD.UniRule annotation7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-4411577,EBI-4411577
tatCP694233EBI-4411577,EBI-4411641

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4262617. 325 interactions.
DIPiDIP-58536N.
IntActiP69425. 4 interactions.
MINTiMINT-8082940.
STRINGi511145.b3838.

Structurei

3D structure databases

ProteinModelPortaliP69425.
SMRiP69425. Positions 1-101.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The membrane-extrinsic domain forms parallel contacts with at least one other TatB protein.1 Publication

Sequence similaritiesi

Belongs to the TatB family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105X8U. Bacteria.
COG1826. LUCA.
HOGENOMiHOG000245368.
InParanoidiP69425.
KOiK03117.
OMAiNEAQHEG.
OrthoDBiEOG6WQD34.

Family and domain databases

HAMAPiMF_00237. TatB.
InterProiIPR018448. TatB.
IPR003998. TatB-like.
[Graphical view]
PRINTSiPR01506. TATBPROTEIN.
TIGRFAMsiTIGR01410. tatB. 1 hit.

Sequencei

Sequence statusi: Complete.

P69425-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFDIGFSELL LVFIIGLVVL GPQRLPVAVK TVAGWIRALR SLATTVQNEL
60 70 80 90 100
TQELKLQEFQ DSLKKVEKAS LTNLTPELKA SMDELRQAAE SMKRSYVAND
110 120 130 140 150
PEKASDEAHT IHNPVVKDNE AAHEGVTPAA AQTQASSPEQ KPETTPEPVV
160 170
KPAADAEPKT AAPSPSSSDK P
Length:171
Mass (Da):18,421
Last modified:March 1, 2005 - v1
Checksum:i31F1405404F5DABF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ005830 Genomic DNA. Translation: CAA06725.1.
AF067848 Genomic DNA. Translation: AAC19241.1.
M87049 Genomic DNA. Translation: AAA67633.1. Sequence problems.
U00096 Genomic DNA. Translation: AAT48228.1.
AP009048 Genomic DNA. Translation: BAE77464.1.
PIRiG91224.
RefSeqiWP_000459594.1. NZ_LN832404.1.
YP_026270.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAT48228; AAT48228; b3838.
BAE77464; BAE77464; BAE77464.
GeneIDi948319.
KEGGiecj:JW5580.
eco:b3838.
PATRICi32123175. VBIEscCol129921_3953.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ005830 Genomic DNA. Translation: CAA06725.1.
AF067848 Genomic DNA. Translation: AAC19241.1.
M87049 Genomic DNA. Translation: AAA67633.1. Sequence problems.
U00096 Genomic DNA. Translation: AAT48228.1.
AP009048 Genomic DNA. Translation: BAE77464.1.
PIRiG91224.
RefSeqiWP_000459594.1. NZ_LN832404.1.
YP_026270.1. NC_000913.3.

3D structure databases

ProteinModelPortaliP69425.
SMRiP69425. Positions 1-101.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262617. 325 interactions.
DIPiDIP-58536N.
IntActiP69425. 4 interactions.
MINTiMINT-8082940.
STRINGi511145.b3838.

Protein family/group databases

TCDBi2.A.64.1.1. the twin arginine targeting (tat) family.

Proteomic databases

PaxDbiP69425.
PRIDEiP69425.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAT48228; AAT48228; b3838.
BAE77464; BAE77464; BAE77464.
GeneIDi948319.
KEGGiecj:JW5580.
eco:b3838.
PATRICi32123175. VBIEscCol129921_3953.

Organism-specific databases

EchoBASEiEB4068.
EcoGeneiEG14322. tatB.

Phylogenomic databases

eggNOGiENOG4105X8U. Bacteria.
COG1826. LUCA.
HOGENOMiHOG000245368.
InParanoidiP69425.
KOiK03117.
OMAiNEAQHEG.
OrthoDBiEOG6WQD34.

Enzyme and pathway databases

BioCyciEcoCyc:G7808-MONOMER.
ECOL316407:JW5580-MONOMER.
MetaCyc:G7808-MONOMER.

Miscellaneous databases

PROiP69425.

Family and domain databases

HAMAPiMF_00237. TatB.
InterProiIPR018448. TatB.
IPR003998. TatB-like.
[Graphical view]
PRINTSiPR01506. TATBPROTEIN.
TIGRFAMsiTIGR01410. tatB. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Overlapping functions of components of a bacterial Sec-independent protein export pathway."
    Sargent F., Bogsch E.G., Stanley N.R., Wexler M., Robinson C., Berks B.C., Palmer T.
    EMBO J. 17:3640-3650(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  2. "A novel and ubiquitous system for membrane targeting and secretion of cofactor-containing proteins."
    Weiner J.H., Bilous P.T., Shaw G.M., Lubitz S.P., Frost L., Thomas G.H., Cole J.A., Turner R.J.
    Cell 93:93-101(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 33694 / HB101.
  3. "Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes."
    Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.
    Science 257:771-778(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION.
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "TatB and TatC form a functional and structural unit of the twin-arginine translocase from Escherichia coli."
    Bolhuis A., Mathers J.E., Thomas J.D., Barrett C.M., Robinson C.
    J. Biol. Chem. 276:20213-20219(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-5, INTERACTION WITH TATA AND TATC.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  7. "Sec-independent protein translocation in Escherichia coli. A distinct and pivotal role for the TatB protein."
    Sargent F., Stanley N.R., Berks B.C., Palmer T.
    J. Biol. Chem. 274:36073-36082(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  8. Cited for: REVIEW.
  9. "Purified components of the Escherichia coli Tat protein transport system form a double-layered ring structure."
    Sargent F., Gohlke U., De Leeuw E., Stanley N.R., Palmer T., Saibil H.R., Berks B.C.
    Eur. J. Biochem. 268:3361-3367(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, COMPLEX BETWEEN TATA AND TATB.
  10. "Membrane interactions and self-association of the TatA and TatB components of the twin-arginine translocation pathway."
    De Leeuw E., Porcelli I., Sargent F., Palmer T., Berks B.C.
    FEBS Lett. 506:143-148(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  11. "Constitutive expression of Escherichia coli tat genes indicates an important role for the twin-arginine translocase during aerobic and anaerobic growth."
    Jack R.L., Sargent F., Berks B.C., Sawers G., Palmer T.
    J. Bacteriol. 183:1801-1804(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  12. "In vivo dissection of the Tat translocation pathway in Escherichia coli."
    Ize B., Gerard F., Zhang M., Chanal A., Voulhoux R., Palmer T., Filloux A., Wu L.F.
    J. Mol. Biol. 317:327-335(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  13. "Differential interactions between a twin-arginine signal peptide and its translocase in Escherichia coli."
    Alami M., Luke I., Deitermann S., Eisner G., Koch H.G., Brunner J., Muller M.
    Mol. Cell 12:937-946(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Localization of the Tat translocon components in Escherichia coli."
    Berthelmann F., Bruser T.
    FEBS Lett. 569:82-88(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, SUBCELLULAR LOCATION.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  15. "The Escherichia coli twin-arginine translocation apparatus incorporates a distinct form of TatABC complex, spectrum of modular TatA complexes and minor TatAB complex."
    Oates J., Barrett C.M., Barnett J.P., Byrne K.G., Bolhuis A., Robinson C.
    J. Mol. Biol. 346:295-305(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  16. "The core TatABC complex of the twin-arginine translocase in Escherichia coli: TatC drives assembly whereas TatA is essential for stability."
    Mangels D., Mathers J.E., Bolhuis A., Robinson C.
    J. Mol. Biol. 345:415-423(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  17. "TatBC, TatB, and TatC form structurally autonomous units within the twin arginine protein transport system of Escherichia coli."
    Orriss G.L., Tarry M.J., Ize B., Sargent F., Lea S.M., Palmer T., Berks B.C.
    FEBS Lett. 581:4091-4097(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  18. "Structural analysis of substrate binding by the TatBC component of the twin-arginine protein transport system."
    Tarry M.J., Schafer E., Chen S., Buchanan G., Greene N.P., Lea S.M., Palmer T., Saibil H.R., Berks B.C.
    Proc. Natl. Acad. Sci. U.S.A. 106:13284-13289(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBSTRATE BINDING.
  19. "TatB functions as an oligomeric binding site for folded Tat precursor proteins."
    Maurer C., Panahandeh S., Jungkamp A.C., Moser M., Muller M.
    Mol. Biol. Cell 21:4151-4161(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBSTRATE BINDING.
  20. "Visualizing interactions along the Escherichia coli twin-arginine translocation pathway using protein fragment complementation."
    Kostecki J.S., Li H., Turner R.J., DeLisa M.P.
    PLoS ONE 5:E9225-E9225(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, INTERACTION WITH DMSA AND DMSD, SUBCELLULAR LOCATION.
  21. "Characterisation of the membrane-extrinsic domain of the TatB component of the twin arginine protein translocase."
    Maldonado B., Kneuper H., Buchanan G., Hatzixanthis K., Sargent F., Berks B.C., Palmer T.
    FEBS Lett. 585:478-484(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN.

Entry informationi

Entry nameiTATB_ECOLI
AccessioniPrimary (citable) accession number: P69425
Secondary accession number(s): O69415
, O87926, P27856, Q2M8E2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2005
Last modified: July 6, 2016
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.