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Protein

Sec-independent protein translocase protein TatAd

Gene

tatAd

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 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. TatA could form the protein-conducting channel of the Tat system. Required for PhoD secretion. The cytosolic fraction of TatAd binds the precursor of PhoD.UniRule annotation1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Translocation, Transport

Enzyme and pathway databases

BioCyciBSUB:BSU02630-MONOMER.

Protein family/group databases

TCDBi2.A.64.3.1. the twin arginine targeting (tat) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Sec-independent protein translocase protein TatAdUniRule annotation
Gene namesi
Name:tatAdUniRule annotation
Synonyms:yczB
Ordered Locus Names:BSU02630
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

Topology

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7070Sec-independent protein translocase protein TatAdPRO_0000097981Add
BLAST

Proteomic databases

PaxDbiO31467.

Expressioni

Inductioni

Expressed under conditions of phosphate starvation.

Interactioni

Subunit structurei

Forms a complex with TatCd. Two types of complexes exist: one composed of TatAd and TatCd, and another composed only of TatAd. Soluble TatAd forms homomultimers bigger than 100 kDa. Soluble TatAd associates in homomultimeric micelle-like particles with a size of about 12 or 25 nm in diameter as well as in elongated particles of 12 nm in diameter.UniRule annotation2 Publications

Protein-protein interaction databases

IntActiO31467. 20 interactions.
STRINGi224308.Bsubs1_010100001463.

Structurei

Secondary structure

1
70
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53Combined sources
Helixi7 – 2014Combined sources
Turni23 – 253Combined sources
Helixi26 – 4924Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L16NMR-A1-70[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TatA/E family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG41067S4. Bacteria.
ENOG410XUF0. LUCA.
HOGENOMiHOG000245365.
InParanoidiO31467.
KOiK03116.
OMAiKKATREP.
OrthoDBiEOG6WQD34.
PhylomeDBiO31467.

Family and domain databases

HAMAPiMF_00236. TatA_E.
InterProiIPR003369. TatA/B/E.
IPR006312. TatA/E.
IPR003998. TatB-like.
[Graphical view]
PfamiPF02416. MttA_Hcf106. 1 hit.
[Graphical view]
PRINTSiPR01506. TATBPROTEIN.
TIGRFAMsiTIGR01411. tatAE. 1 hit.

Sequencei

Sequence statusi: Complete.

O31467-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFSNIGIPGL ILIFVIALII FGPSKLPEIG RAAGRTLLEF KSATKSLVSG
60 70
DEKEEKSAEL TAVKQDKNAG
Length:70
Mass (Da):7,431
Last modified:November 3, 2009 - v2
Checksum:i3D6B356BC425D111
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB12057.2.
PIRiA69767.
RefSeqiNP_388145.2. NC_000964.3.
WP_003223835.1. NZ_JNCM01000030.1.

Genome annotation databases

EnsemblBacteriaiCAB12057; CAB12057; BSU02630.
GeneIDi11238161.
938398.
KEGGibsu:BSU02630.
PATRICi18972085. VBIBacSub10457_0271.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB12057.2.
PIRiA69767.
RefSeqiNP_388145.2. NC_000964.3.
WP_003223835.1. NZ_JNCM01000030.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L16NMR-A1-70[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO31467. 20 interactions.
STRINGi224308.Bsubs1_010100001463.

Protein family/group databases

TCDBi2.A.64.3.1. the twin arginine targeting (tat) family.

Proteomic databases

PaxDbiO31467.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12057; CAB12057; BSU02630.
GeneIDi11238161.
938398.
KEGGibsu:BSU02630.
PATRICi18972085. VBIBacSub10457_0271.

Phylogenomic databases

eggNOGiENOG41067S4. Bacteria.
ENOG410XUF0. LUCA.
HOGENOMiHOG000245365.
InParanoidiO31467.
KOiK03116.
OMAiKKATREP.
OrthoDBiEOG6WQD34.
PhylomeDBiO31467.

Enzyme and pathway databases

BioCyciBSUB:BSU02630-MONOMER.

Family and domain databases

HAMAPiMF_00236. TatA_E.
InterProiIPR003369. TatA/B/E.
IPR006312. TatA/E.
IPR003998. TatB-like.
[Graphical view]
PfamiPF02416. MttA_Hcf106. 1 hit.
[Graphical view]
PRINTSiPR01506. TATBPROTEIN.
TIGRFAMsiTIGR01411. tatAE. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  2. "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
    Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
    Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO 18 AND 34.
  3. "TatC is a specificity determinant for protein secretion via the twin-arginine translocation pathway."
    Jongbloed J.D.H., Martin U., Antelmann H., Hecker M., Tjalsma H., Venema G., Bron S., van Dijl J.M., Mueller J.
    J. Biol. Chem. 275:41350-41357(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF THE TAT GENES.
  4. "Sequence-specific binding of prePhoD to soluble TatAd indicates protein-mediated targeting of the Tat export in Bacillus subtilis."
    Pop O.I., Westermann M., Volkmer-Engert R., Schulz D., Lemke C., Schreiber S., Gerlach R., Wetzker R., Mueller J.P.
    J. Biol. Chem. 278:38428-38436(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PHOD PRECURSOR.
  5. Cited for: CHARACTERIZATION OF THE TWO TAT TRANSLOCASE SYSTEMS.
  6. "The TatAd component of the Bacillus subtilis twin-arginine protein transport system forms homo-multimeric complexes in its cytosolic and membrane embedded localisation."
    Westermann M., Pop O.I., Gerlach R., Appel T.R., Schloermann W., Schreiber S., Mueller J.P.
    Biochim. Biophys. Acta 1758:443-451(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  7. "Affinity of TatCd for TatAd elucidates its receptor function in the Bacillus subtilis twin arginine translocation (Tat) translocase system."
    Schreiber S., Stengel R., Westermann M., Volkmer-Engert R., Pop O.I., Mueller J.P.
    J. Biol. Chem. 281:19977-19984(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TATCD.
  8. "A minimal Tat system from a gram-positive organism: a bifunctional TatA subunit participates in discrete TatAC and TatA complexes."
    Barnett J.P., Eijlander R.T., Kuipers O.P., Robinson C.
    J. Biol. Chem. 283:2534-2542(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
    Strain: 168.
  9. "Solution NMR structure of the TatA component of the twin-arginine protein transport system from gram-positive bacterium Bacillus subtilis."
    Hu Y., Zhao E., Li H., Xia B., Jin C.
    J. Am. Chem. Soc. 132:15942-15944(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiTATAD_BACSU
AccessioniPrimary (citable) accession number: O31467
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: November 3, 2009
Last modified: February 17, 2016
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

B.subtilis possesses two minimal, substrate-specific, Tat translocases: TatAd-TatCd and TatAy-TatCy, each one composed of a TatA and a TatC protein. TatA is bifunctional and performs the function of both the TatA and TatB proteins of Gram-negative organisms.
Membrane-localization and maintenance of TatAd is assisted by TatCd.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.