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Protein

Acyl-CoA thioesterase 2

Gene

tesB

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

Functioni

Can hydrolyze a broad range of acyl-CoA thioesters. Its physiological function is not known.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei58 – 581
Active sitei204 – 2041

GO - Molecular functioni

  • acyl-CoA hydrolase activity Source: EcoCyc

GO - Biological processi

  • acyl-CoA metabolic process Source: InterPro
  • fatty acid catabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciEcoCyc:THIOESTERII-MONOMER.
ECOL316407:JW0442-MONOMER.
MetaCyc:THIOESTERII-MONOMER.
RETL1328306-WGS:GSTH-4063-MONOMER.
BRENDAi3.1.2.2. 2026.
3.1.2.20. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-CoA thioesterase 2 (EC:3.1.2.-)
Alternative name(s):
Acyl-CoA thioesterase II
Short name:
TEII
Gene namesi
Name:tesB
Ordered Locus Names:b0452, JW0442
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10995. tesB.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 286285Acyl-CoA thioesterase 2PRO_0000202144Add
BLAST

Proteomic databases

PaxDbiP0AGG2.
PRIDEiP0AGG2.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

BioGridi4259857. 16 interactions.
DIPiDIP-10980N.
IntActiP0AGG2. 5 interactions.
STRINGi511145.b0452.

Structurei

Secondary structure

1
286
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1210Combined sources
Beta strandi15 – 184Combined sources
Beta strandi21 – 244Combined sources
Helixi36 – 4914Combined sources
Beta strandi56 – 649Combined sources
Beta strandi74 – 8310Combined sources
Beta strandi85 – 9612Combined sources
Beta strandi99 – 10911Combined sources
Helixi133 – 1408Combined sources
Helixi146 – 1494Combined sources
Beta strandi157 – 1648Combined sources
Turni168 – 1703Combined sources
Beta strandi176 – 18611Combined sources
Helixi192 – 20211Combined sources
Beta strandi205 – 2073Combined sources
Helixi208 – 2158Combined sources
Beta strandi224 – 23512Combined sources
Beta strandi245 – 25511Combined sources
Beta strandi258 – 26710Combined sources
Beta strandi272 – 28413Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C8UX-ray1.90A/B2-286[»]
ProteinModelPortaliP0AGG2.
SMRiP0AGG2. Positions 2-286.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AGG2.

Family & Domainsi

Sequence similaritiesi

Belongs to the C/M/P thioester hydrolase family.Curated

Phylogenomic databases

eggNOGiENOG4105C29. Bacteria.
COG1946. LUCA.
HOGENOMiHOG000246495.
InParanoidiP0AGG2.
KOiK10805.
OMAiIYDVEIL.
PhylomeDBiP0AGG2.

Family and domain databases

Gene3Di3.10.129.10. 2 hits.
InterProiIPR003703. Acyl_CoA_thio.
IPR029069. HotDog_dom.
[Graphical view]
PANTHERiPTHR11066. PTHR11066. 1 hit.
SUPFAMiSSF54637. SSF54637. 2 hits.
TIGRFAMsiTIGR00189. tesB. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P0AGG2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQALKNLLT LLNLEKIEEG LFRGQSEDLG LRQVFGGQVV GQALYAAKET
60 70 80 90 100
VPEERLVHSF HSYFLRPGDS KKPIIYDVET LRDGNSFSAR RVAAIQNGKP
110 120 130 140 150
IFYMTASFQA PEAGFEHQKT MPSAPAPDGL PSETQIAQSL AHLLPPVLKD
160 170 180 190 200
KFICDRPLEV RPVEFHNPLK GHVAEPHRQV WIRANGSVPD DLRVHQYLLG
210 220 230 240 250
YASDLNFLPV ALQPHGIGFL EPGIQIATID HSMWFHRPFN LNEWLLYSVE
260 270 280
STSASSARGF VRGEFYTQDG VLVASTVQEG VMRNHN
Length:286
Mass (Da):31,966
Last modified:January 23, 2007 - v2
Checksum:i8E7C4A4BCF73CA4B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63308 Genomic DNA. Translation: AAA24665.1.
U82664 Genomic DNA. Translation: AAB40208.1.
U00096 Genomic DNA. Translation: AAC73555.1.
AP009048 Genomic DNA. Translation: BAE76232.1.
PIRiD64775.
RefSeqiNP_414986.1. NC_000913.3.
WP_000075876.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73555; AAC73555; b0452.
BAE76232; BAE76232; BAE76232.
GeneIDi945074.
KEGGiecj:JW0442.
eco:b0452.
PATRICi32116059. VBIEscCol129921_0471.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63308 Genomic DNA. Translation: AAA24665.1.
U82664 Genomic DNA. Translation: AAB40208.1.
U00096 Genomic DNA. Translation: AAC73555.1.
AP009048 Genomic DNA. Translation: BAE76232.1.
PIRiD64775.
RefSeqiNP_414986.1. NC_000913.3.
WP_000075876.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C8UX-ray1.90A/B2-286[»]
ProteinModelPortaliP0AGG2.
SMRiP0AGG2. Positions 2-286.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259857. 16 interactions.
DIPiDIP-10980N.
IntActiP0AGG2. 5 interactions.
STRINGi511145.b0452.

Proteomic databases

PaxDbiP0AGG2.
PRIDEiP0AGG2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73555; AAC73555; b0452.
BAE76232; BAE76232; BAE76232.
GeneIDi945074.
KEGGiecj:JW0442.
eco:b0452.
PATRICi32116059. VBIEscCol129921_0471.

Organism-specific databases

EchoBASEiEB0988.
EcoGeneiEG10995. tesB.

Phylogenomic databases

eggNOGiENOG4105C29. Bacteria.
COG1946. LUCA.
HOGENOMiHOG000246495.
InParanoidiP0AGG2.
KOiK10805.
OMAiIYDVEIL.
PhylomeDBiP0AGG2.

Enzyme and pathway databases

BioCyciEcoCyc:THIOESTERII-MONOMER.
ECOL316407:JW0442-MONOMER.
MetaCyc:THIOESTERII-MONOMER.
RETL1328306-WGS:GSTH-4063-MONOMER.
BRENDAi3.1.2.2. 2026.
3.1.2.20. 2026.

Miscellaneous databases

EvolutionaryTraceiP0AGG2.
PROiP0AGG2.

Family and domain databases

Gene3Di3.10.129.10. 2 hits.
InterProiIPR003703. Acyl_CoA_thio.
IPR029069. HotDog_dom.
[Graphical view]
PANTHERiPTHR11066. PTHR11066. 1 hit.
SUPFAMiSSF54637. SSF54637. 2 hits.
TIGRFAMsiTIGR00189. tesB. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiTESB_ECOLI
AccessioniPrimary (citable) accession number: P0AGG2
Secondary accession number(s): P23911, Q2MBX4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 89 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

3D-structure, Complete proteome, Direct protein sequencing, 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.