Acyl-CoA thioesterase I precursor - Escherichia coli (strain K12)

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P0ADA1 (TESA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 67. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Acyl-CoA thioesterase I
EC=3.1.2.-

Alternative name(s):
Lecithinase B
Lysophospholipase L1
EC=3.1.1.5
Protease I

Gene names

Name:	tesA
Synonyms:	apeA, pldC
Ordered Locus Names:	b0494, JW0483

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	208 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Hydrolyzes only long chain acyl thioesters (C12-C18). Specificity similar to chymotrypsin.
Catalytic activity	2-lysophosphatidylcholine + H₂O = glycerophosphocholine + a carboxylate.
Subunit structure	Monomer.
Subcellular location	Periplasm.
Sequence similarities	Belongs to the 'GDSL' lipolytic enzyme family.
Sequence caution	The sequence AAB40248.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Periplasm
Domain	Signal
Molecular function	Hydrolase Protease
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	lipid metabolic process Inferred from electronic annotation. Source: InterPro proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	outer membrane-bounded periplasmic space Inferred from direct assay Ref.2. Source: EcoCyc
Molecular_function	acyl-CoA hydrolase activity Inferred from direct assay PubMed 4554913. Source: EcoCyc lysophospholipase activity Inferred from direct assay Ref.6. Source: EcoCyc peptidase activity Inferred from direct assay Ref.2. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 26

Ref.2 Ref.6

Chain

27 – 208

182

Acyl-CoA thioesterase I

PRO_0000017848

Sites

Active site

Nucleophile By similarity

Active site

180

By similarity

Active site

183

Ref.8

Binding site

Substrate; via amide nitrogen

Binding site

Substrate

Experimental info

Mutagenesis

S → A: Reduces activity by over 99%. Ref.7

Mutagenesis

G → A: Reduces activity by over 75%. Ref.7

Mutagenesis

N → A: Reduces activity by over 60%. Ref.7

Mutagenesis

135

L → P: Lowers activity towards substrates with long acyl chains.

Mutagenesis

180

D → A: Reduces activity by over 70%. Ref.7

Mutagenesis

183

H → A: Reduces activity by over 99%. Ref.7

Secondary structure

208

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0ADA1 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: CD03F23EA39541F1
Show »

FASTA

208

23,622

        10         20         30         40         50         60 
MMNFNNVFRW HLPFLFLVLL TFRAAAADTL LILGDSLSAG YRMSASAAWP ALLNDKWQSK 

        70         80         90        100        110        120 
TSVVNASISG DTSQQGLARL PALLKQHQPR WVLVELGGND GLRGFQPQQT EQTLRQILQD 

       130        140        150        160        170        180 
VKAANAEPLL MQIRLPANYG RRYNEAFSAI YPKLAKEFDV PLLPFFMEEV YLKPQWMQDD 

       190        200 
GIHPNRDAQP FIADWMAKQL QPLVNHDS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Escherichia coli thioesterase I, molecular cloning and sequencing of the structural gene and identification as a periplasmic enzyme." Cho H., Cronan J.E. Jr. J. Biol. Chem. 268:9238-9245(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"Molecular cloning, sequencing, and mapping of the gene encoding protease I and characterization of proteinase and proteinase-defective Escherichia coli mutants." Ichihara S., Matsubara Y., Kato C., Akasaka K., Mizushima S. J. Bacteriol. 175:1032-1037(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 27-38. Strain: K12.
[3]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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]	"Lysophospholipase L1 from Escherichia coli K-12 overproducer." Karasawa K., Kudo I., Kobayashi T., Homma H., Chiba N., Mizushima H., Inoue K., Nojima S. J. Biochem. 109:288-293(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-43, CHARACTERIZATION AS LYSOPHOSPHOLIPASE. Strain: K12.
[7]	"Functional role of catalytic triad and oxyanion hole-forming residues on enzyme activity of Escherichia coli thioesterase I/protease I/phospholipase L1." Lee L.-C., Lee Y.-L., Leu R.-J., Shaw J.-F. Biochem. J. 397:69-76(2006) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF SER-36; GLY-70; ASN-99; ASP-180 AND HIS-183.
[8]	"Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: consensus sequence blocks constitute the catalytic center of SGNH-hydrolases through a conserved hydrogen bond network." Lo Y.-C., Lin S.-C., Shaw J.-F., Liaw Y.-C. J. Mol. Biol. 330:539-551(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 27-208 IN COMPLEX WITH SUBSTRATE ANALOG, ACTIVE SITE, MASS SPECTROMETRY.
[9]	"Substrate specificities of Escherichia coli thioesterase I/protease I/lysophospholipase L1 are governed by its switch loop movement." Lo Y.-C., Lin S.-C., Shaw J.-F., Liaw Y.-C. Biochemistry 44:1971-1979(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 27-208 OF WILD-TYPE AND MUTANT PRO-135 IN COMPLEX WITH SUBSTRATE ANALOG.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L06182 Genomic DNA. Translation: AAA24664.1.
D13180 Genomic DNA. Translation: BAA02475.1.
U82664 Genomic DNA. Translation: AAB40248.1. Different initiation.
U00096 Genomic DNA. Translation: AAC73596.1.
AP009048 Genomic DNA. Translation: BAE76273.1.

PIR

A49699.
PX0045.

RefSeq

NP_415027.1. NC_000913.2.
YP_488785.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IVN	X-ray	1.90	A	27-208	[»]
1J00	X-ray	2.00	A	27-208	[»]
1JRL	X-ray	1.95	A	27-208	[»]
1U8U	X-ray	2.08	A	27-208	[»]
1V2G	X-ray	2.00	A	27-208	[»]

ProteinModelPortal

P0ADA1.

SMR

P0ADA1. Positions 27-204.

ModBase

Search...

Protein-protein interaction databases

STRING

511145.b0494.

2D gel databases

SWISS-2DPAGE

P0ADA1.

Proteomic databases

PaxDb

P0ADA1.

PRIDE

P0ADA1.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73596; AAC73596; b0494.
BAE76273; BAE76273; BAE76273.

GeneID

12930860.
945127.

KEGG

ecj:Y75_p0481.
eco:b0494.

PATRIC

32116147. VBIEscCol129921_0515.

Organism-specific databases

EchoBASE

EB1504.

EcoGene

EG11542. tesA.

Phylogenomic databases

eggNOG

COG2755.

HOGENOM

HOG000261382.

K10804.

OMA

PPNYGPD.

ProtClustDB

PRK10528.

Enzyme and pathway databases

BioCyc

EcoCyc:THIOESTERI-MONOMER.
ECOL316407:JW0483-MONOMER.
MetaCyc:THIOESTERI-MONOMER.

SABIO-RK

P0ADA1.

Gene expression databases

Genevestigator

P0ADA1.

Family and domain databases

Gene3D

3.40.50.1110. 1 hit.

InterPro

IPR001087. Lipase_GDSL.
IPR008265. Lipase_GDSL_AS.
IPR013831. SGNH_hydro-type_esterase_dom.
[Graphical view]

Pfam

PF00657. Lipase_GDSL. 1 hit.
[Graphical view]

PROSITE

PS01098. LIPASE_GDSL_SER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0ADA1.

Entry information

Entry name

TESA_ECOLI

Accession

Primary (citable) accession number: P0ADA1
Secondary accession number(s): P29679

Q2MBT3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	December 6, 2005
Last modified:	May 1, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents