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Protein

Sec-independent protein translocase protein TatC

Gene

tatC

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 TatB, TatC is part of a receptor directly interacting with Tat signal peptides.UniRule annotation5 Publications

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Biological processi

Protein transport, Translocation, Transport

Enzyme and pathway databases

BioCyciEcoCyc:EG11479-MONOMER.
ECOL316407:JW3815-MONOMER.
MetaCyc:EG11479-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 TatCUniRule annotation
Gene namesi
Name:tatCUniRule annotation
Synonyms:mttB, yigU, yigV
Ordered Locus Names:b3839, JW3815
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11479. tatC.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 2322CytoplasmicSequence analysisAdd
BLAST
Transmembranei24 – 4421HelicalUniRule annotationAdd
BLAST
Topological domaini45 – 7531PeriplasmicSequence analysisAdd
BLAST
Transmembranei76 – 9621HelicalUniRule annotationAdd
BLAST
Topological domaini97 – 11519CytoplasmicSequence analysisAdd
BLAST
Transmembranei116 – 13621HelicalUniRule annotationAdd
BLAST
Topological domaini137 – 15620PeriplasmicSequence analysisAdd
BLAST
Transmembranei157 – 17721HelicalUniRule annotationAdd
BLAST
Topological domaini178 – 19215CytoplasmicSequence analysisAdd
BLAST
Transmembranei193 – 21018HelicalUniRule annotationAdd
BLAST
Topological domaini211 – 2111PeriplasmicSequence analysis
Transmembranei212 – 23221HelicalUniRule annotationAdd
BLAST
Topological domaini233 – 25826CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of plasma membrane Source: EcoCyc
  • intracellular Source: GOC
  • membrane Source: EcoliWiki
  • plasma membrane Source: EcoCyc
  • 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 at least five twin-arginine-containing precursor proteins that are predicted to bind redox cofactors, and hence fold prior to translocation. Disruption does not affect the Sec pathway.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi17 – 171R → A: No anaerobic growth and no TorA export. 1 Publication
Mutagenesisi20 – 223Missing : No anaerobic growth and 75% decrease in TorA export. 1 Publication
Mutagenesisi20 – 201L → A: 25% decrease in anaerobic growth and 75% decrease in TorA export. 1 Publication
Mutagenesisi94 – 941F → A or L: Loss of function. 1 Publication
Mutagenesisi94 – 941F → A: Export of TorA restored; when associated with A-211. 1 Publication
Mutagenesisi103 – 1031E → A, D or R: Loss of function. 1 Publication
Mutagenesisi103 – 1031E → A: Export of TorA restored; when associated with A-211. 1 Publication
Mutagenesisi103 – 1031E → Q: Severely retard but does not abolish activity. 1 Publication
Mutagenesisi211 – 2111D → A: Export activity of TorA blocked. Export of TorA restored; when associated with A-94 or A-103. 1 Publication
Mutagenesisi211 – 2111D → E or N: Decrease in TorA export activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 258257Sec-independent protein translocase protein TatCPRO_0000098083Add
BLAST

Proteomic databases

PaxDbiP69423.

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. TatC can form a distinct, stable, multimeric complex independent of TatA and TatB. Each of TatA, TatB and TatC are able to interact in pairs without the third partner. Interacts with the signal sequence of DmsA and DmsD.UniRule annotation6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
tatBP694253EBI-4411641,EBI-4411577

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4259567. 343 interactions.
DIPiDIP-58537N.
IntActiP69423. 4 interactions.
MINTiMINT-8083961.
STRINGi511145.b3839.

Structurei

3D structure databases

ProteinModelPortaliP69423.
SMRiP69423. Positions 12-235.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TatC family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105DCX. Bacteria.
COG0805. LUCA.
HOGENOMiHOG000245379.
InParanoidiP69423.
KOiK03118.
OMAiATQIYKF.
OrthoDBiEOG60SCQS.
PhylomeDBiP69423.

Family and domain databases

HAMAPiMF_00902. TatC.
InterProiIPR019820. Sec-indep_translocase_CS.
IPR002033. TatC.
[Graphical view]
PANTHERiPTHR30371:SF0. PTHR30371:SF0. 1 hit.
PfamiPF00902. TatC. 1 hit.
[Graphical view]
PRINTSiPR01840. TATCFAMILY.
TIGRFAMsiTIGR00945. tatC. 1 hit.
PROSITEiPS01218. TATC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P69423-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVEDTQPLI THLIELRKRL LNCIIAVIVI FLCLVYFAND IYHLVSAPLI
60 70 80 90 100
KQLPQGSTMI ATDVASPFFT PIKLTFMVSL ILSAPVILYQ VWAFIAPALY
110 120 130 140 150
KHERRLVVPL LVSSSLLFYI GMAFAYFVVF PLAFGFLANT APEGVQVSTD
160 170 180 190 200
IASYLSFVMA LFMAFGVSFE VPVAIVLLCW MGITSPEDLR KKRPYVLVGA
210 220 230 240 250
FVVGMLLTPP DVFSQTLLAI PMYCLFEIGV FFSRFYVGKG RNREEENDAE

AESEKTEE
Length:258
Mass (Da):28,876
Last modified:January 23, 2007 - v2
Checksum:iD2383F85AF62A81C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ005830 Genomic DNA. Translation: CAA06726.1.
AF067848 Genomic DNA. Translation: AAC19242.1.
M87049 Genomic DNA. Translation: AAA67634.1. Frameshift.
M87049 Genomic DNA. Translation: AAA67635.1. Frameshift.
U00096 Genomic DNA. Translation: AAC76842.1.
AP009048 Genomic DNA. Translation: BAE77463.1.
PIRiH65188.
S30728.
RefSeqiNP_418282.1. NC_000913.3.
WP_000109943.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76842; AAC76842; b3839.
BAE77463; BAE77463; BAE77463.
GeneIDi948328.
KEGGiecj:JW3815.
eco:b3839.
PATRICi32123177. VBIEscCol129921_3954.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ005830 Genomic DNA. Translation: CAA06726.1.
AF067848 Genomic DNA. Translation: AAC19242.1.
M87049 Genomic DNA. Translation: AAA67634.1. Frameshift.
M87049 Genomic DNA. Translation: AAA67635.1. Frameshift.
U00096 Genomic DNA. Translation: AAC76842.1.
AP009048 Genomic DNA. Translation: BAE77463.1.
PIRiH65188.
S30728.
RefSeqiNP_418282.1. NC_000913.3.
WP_000109943.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP69423.
SMRiP69423. Positions 12-235.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259567. 343 interactions.
DIPiDIP-58537N.
IntActiP69423. 4 interactions.
MINTiMINT-8083961.
STRINGi511145.b3839.

Protein family/group databases

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

Proteomic databases

PaxDbiP69423.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76842; AAC76842; b3839.
BAE77463; BAE77463; BAE77463.
GeneIDi948328.
KEGGiecj:JW3815.
eco:b3839.
PATRICi32123177. VBIEscCol129921_3954.

Organism-specific databases

EchoBASEiEB1445.
EcoGeneiEG11479. tatC.

Phylogenomic databases

eggNOGiENOG4105DCX. Bacteria.
COG0805. LUCA.
HOGENOMiHOG000245379.
InParanoidiP69423.
KOiK03118.
OMAiATQIYKF.
OrthoDBiEOG60SCQS.
PhylomeDBiP69423.

Enzyme and pathway databases

BioCyciEcoCyc:EG11479-MONOMER.
ECOL316407:JW3815-MONOMER.
MetaCyc:EG11479-MONOMER.

Miscellaneous databases

PROiP69423.

Family and domain databases

HAMAPiMF_00902. TatC.
InterProiIPR019820. Sec-indep_translocase_CS.
IPR002033. TatC.
[Graphical view]
PANTHERiPTHR30371:SF0. PTHR30371:SF0. 1 hit.
PfamiPF00902. TatC. 1 hit.
[Graphical view]
PRINTSiPR01840. TATCFAMILY.
TIGRFAMsiTIGR00945. tatC. 1 hit.
PROSITEiPS01218. TATC. 1 hit.
[Graphical view]
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], CHARACTERIZATION.
    Strain: K12.
  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 2-6, INTERACTION WITH TATA AND TATB.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  7. "An essential component of a novel bacterial protein export system with homologues in plastids and mitochondria."
    Bogsch E.G., Sargent F., Stanley N.R., Berks B.C., Robinson C., Palmer T.
    J. Biol. Chem. 273:18003-18006(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  8. Cited for: REVIEW.
  9. "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.
  10. "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.
  11. "Essential cytoplasmic domains in the Escherichia coli TatC protein."
    Allen S.C., Barrett C.M., Ray N., Robinson C.
    J. Biol. Chem. 277:10362-10366(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ARG-17; LEU-20 AND 20-LEU--ASN-22.
  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. "Functional complexity of the twin-arginine translocase TatC component revealed by site-directed mutagenesis."
    Buchanan G., Leeuw E., Stanley N.R., Wexler M., Berks B.C., Sargent F., Palmer T.
    Mol. Microbiol. 43:1457-1470(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF PHE-94; GLU-103 AND ASP-211.
  14. "Rapid topology mapping of Escherichia coli inner-membrane proteins by prediction and PhoA/GFP fusion analysis."
    Drew D., Sjoestrand D., Nilsson J., Urbig T., Chin C.-N., de Gier J.-W., von Heijne G.
    Proc. Natl. Acad. Sci. U.S.A. 99:2690-2695(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY.
    Strain: K12 / JM109 / ATCC 53323.
  15. "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.
  16. "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.
  17. "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.
  18. "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.
  19. "Global topology analysis of the Escherichia coli inner membrane proteome."
    Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
    Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: K12 / MG1655 / ATCC 47076.
  20. "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.
  21. "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.
  22. "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.
  23. "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.

Entry informationi

Entry nameiTATC_ECOLI
AccessioniPrimary (citable) accession number: P69423
Secondary accession number(s): P27857
, P27858, P76765, P76766, Q2M8E3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: January 23, 2007
Last modified: April 13, 2016
This is version 93 of the entry and version 2 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.