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Protein

tRNA threonylcarbamoyladenosine biosynthesis protein TsaB

Gene

tsaB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t6A37) in tRNAs that read codons beginning with adenine. Is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaD and TsaE. TsaB seems to play an indirect role in the t6A biosynthesis pathway, possibly in regulating the core enzymatic function of TsaD. In fact, can act as a protease that specifically degrades TsaD in vitro; therefore TsaB may post-translationally regulate cellular pools of TsaD via proteolytic degradation. Does not show sialoglycoprotease activity against glycophorin A.2 Publications

GO - Molecular functioni

  • identical protein binding Source: EcoCyc
  • metallopeptidase activity Source: EcoCyc

GO - Biological processi

  • tRNA threonylcarbamoyladenosine modification Source: EcoCyc
Complete GO annotation...

Keywords - Biological processi

tRNA processing

Enzyme and pathway databases

BioCyciEcoCyc:G6991-MONOMER.
ECOL316407:JW1796-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA threonylcarbamoyladenosine biosynthesis protein TsaB
Alternative name(s):
t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaB
Gene namesi
Name:tsaB
Synonyms:yeaZ
Ordered Locus Names:b1807, JW1796
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13512. tsaB.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Appears essential for growth, since no null mutants can be obtained. Conditional depletion of this gene leads to enlarged cells, which display highly condensed nucleoids. The TsaB depletion phenotype is suppressed by overexpressing the response regulator RstA.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 231231tRNA threonylcarbamoyladenosine biosynthesis protein TsaBPRO_0000096990Add
BLAST

Proteomic databases

EPDiP76256.
PaxDbiP76256.
PRIDEiP76256.

Interactioni

Subunit structurei

Homodimer. Interacts with TsaD and TsaE in a mutually exclusive manner; TsaD is the preferred partner. Also interacts with TsaC.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
tsaDP058526EBI-560669,EBI-561994

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4260340. 15 interactions.
DIPiDIP-11804N.
IntActiP76256. 12 interactions.
MINTiMINT-1255819.
STRINGi511145.b1807.

Structurei

Secondary structure

1
231
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 76Combined sources
Beta strandi9 – 1911Combined sources
Beta strandi22 – 298Combined sources
Turni31 – 333Combined sources
Turni34 – 374Combined sources
Helixi38 – 4811Combined sources
Helixi53 – 553Combined sources
Beta strandi58 – 669Combined sources
Helixi68 – 8417Combined sources
Beta strandi89 – 935Combined sources
Helixi94 – 10512Combined sources
Beta strandi109 – 1168Combined sources
Beta strandi118 – 1203Combined sources
Beta strandi122 – 1298Combined sources
Helixi138 – 1403Combined sources
Beta strandi142 – 1443Combined sources
Helixi146 – 1538Combined sources
Beta strandi158 – 1647Combined sources
Helixi165 – 1695Combined sources
Turni171 – 1766Combined sources
Beta strandi178 – 1836Combined sources
Helixi191 – 1933Combined sources
Helixi194 – 20411Combined sources
Helixi210 – 2123Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OKJX-ray2.28A/B/C/D2-231[»]
4WQ4X-ray2.33C/D1-231[»]
4WQ5X-ray2.33C/D1-231[»]
4YDUX-ray2.33C/D1-231[»]
ProteinModelPortaliP76256.
SMRiP76256. Positions 1-218.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP76256.

Family & Domainsi

Sequence similaritiesi

Belongs to the KAE1 / TsaD family. TsaB subfamily.Curated

Phylogenomic databases

eggNOGiENOG41072GX. Bacteria.
COG1214. LUCA.
HOGENOMiHOG000052125.
InParanoidiP76256.
KOiK14742.
OMAiEPIYLRN.
OrthoDBiEOG6D8B8B.
PhylomeDBiP76256.

Family and domain databases

InterProiIPR000905. Gcp-like_dom.
IPR022496. T6A_YeaZ.
[Graphical view]
PfamiPF00814. Peptidase_M22. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03725. T6A_YeaZ. 1 hit.

Sequencei

Sequence statusi: Complete.

P76256-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRILAIDTAT EACSVALWND GTVNAHFELC PREHTQRILP MVQDILTTSG
60 70 80 90 100
TSLTDINALA YGRGPGSFTG VRIGIGIAQG LALGAELPMI GVSTLMTMAQ
110 120 130 140 150
GAWRKNGATR VLAAIDARMG EVYWAEYQRD ENGIWHGEET EAVLKPEIVH
160 170 180 190 200
ERMQQLSGEW VTVGTGWQAW PDLGKESGLV LRDGEVLLPA AEDMLPIACQ
210 220 230
MFAEGKTVAV EHAEPVYLRN NVAWKKLPGK E
Length:231
Mass (Da):25,181
Last modified:February 1, 1997 - v1
Checksum:i5163E6A5342DC276
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74877.1.
AP009048 Genomic DNA. Translation: BAA15611.1.
PIRiG64941.
RefSeqiNP_416321.1. NC_000913.3.
WP_001220966.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74877; AAC74877; b1807.
BAA15611; BAA15611; BAA15611.
GeneIDi946304.
KEGGiecj:JW1796.
eco:b1807.
PATRICi32118931. VBIEscCol129921_1883.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74877.1.
AP009048 Genomic DNA. Translation: BAA15611.1.
PIRiG64941.
RefSeqiNP_416321.1. NC_000913.3.
WP_001220966.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OKJX-ray2.28A/B/C/D2-231[»]
4WQ4X-ray2.33C/D1-231[»]
4WQ5X-ray2.33C/D1-231[»]
4YDUX-ray2.33C/D1-231[»]
ProteinModelPortaliP76256.
SMRiP76256. Positions 1-218.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260340. 15 interactions.
DIPiDIP-11804N.
IntActiP76256. 12 interactions.
MINTiMINT-1255819.
STRINGi511145.b1807.

Proteomic databases

EPDiP76256.
PaxDbiP76256.
PRIDEiP76256.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74877; AAC74877; b1807.
BAA15611; BAA15611; BAA15611.
GeneIDi946304.
KEGGiecj:JW1796.
eco:b1807.
PATRICi32118931. VBIEscCol129921_1883.

Organism-specific databases

EchoBASEiEB3285.
EcoGeneiEG13512. tsaB.

Phylogenomic databases

eggNOGiENOG41072GX. Bacteria.
COG1214. LUCA.
HOGENOMiHOG000052125.
InParanoidiP76256.
KOiK14742.
OMAiEPIYLRN.
OrthoDBiEOG6D8B8B.
PhylomeDBiP76256.

Enzyme and pathway databases

BioCyciEcoCyc:G6991-MONOMER.
ECOL316407:JW1796-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP76256.
PROiP76256.

Family and domain databases

InterProiIPR000905. Gcp-like_dom.
IPR022496. T6A_YeaZ.
[Graphical view]
PfamiPF00814. Peptidase_M22. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03725. T6A_YeaZ. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "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.
  4. "Conserved network of proteins essential for bacterial viability."
    Handford J.I., Ize B., Buchanan G., Butland G.P., Greenblatt J., Emili A., Palmer T.
    J. Bacteriol. 191:4732-4749(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEASE ACTIVITY, FUNCTION, DISRUPTION PHENOTYPE, SUBUNIT, INTERACTION WITH TSAD AND TSAE, LACK OF GLYCOPROTEASE ACTIVITY, SUBCELLULAR LOCATION.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  5. Cited for: INTERACTION WITH TSAD AND TSAE.
    Strain: K12.
  6. "Biosynthesis of threonylcarbamoyl adenosine (t6A), a universal tRNA nucleoside."
    Deutsch C., El Yacoubi B., de Crecy-Lagard V., Iwata-Reuyl D.
    J. Biol. Chem. 287:13666-13673(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN T(6)A37 FORMATION, GENE NAME, INTERACTION WITH TSAE; TSAD AND TSAC.
    Strain: K12.
  7. "Preliminary crystallographic analysis of the Escherichia coli YeaZ protein using the anomalous signal of a gadolinium derivative."
    Jeudy S., Stelter M., Coutard B., Kahn R., Abergel C.
    Acta Crystallogr. F 61:848-851(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 2-231, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiTSAB_ECOLI
AccessioniPrimary (citable) accession number: P76256
Secondary accession number(s): O08476, O08477
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: July 6, 2016
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

TsaBCDE are necessary and sufficient for tRNA(NNU) t6A37 threonylcarbamoyladenosine modification in vitro in E.coli.1 Publication

Caution

The well-known t6A modification appears to be a hydrolyzed artifact of natural cyclic t6A (ct6A) that occurs during the preparation and handling of tRNA in E.coli and many other species (PubMed:23242255). In these species, the t6A modification is processed further by dehydration into ct6A, a reaction catalyzed by TcdA.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  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.