[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION. PubMed=9401025 [NCBI, ExPASy, EBI, Israel, Japan] Peist R., Koch A., Bolek P., Sewitz S., Kolbus T., Boos W.; "Characterization of the aes gene of Escherichia coli encoding an enzyme with esterase activity."; J. Bacteriol. 179:7679-7686(1997).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=K12; DOI=10.1016/0022-2836(91)90180-E; PubMed=2051480 [NCBI, ExPASy, EBI, Israel, Japan] Miyamoto K., Nakahigashi K., Nishimura K., Inokuchi H.; "Isolation and characterization of visible light-sensitive mutants of Escherichia coli K12."; J. Mol. Biol. 219:393-398(1991).
[3]	SEQUENCE REVISION. Miyamoto K.; Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; 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.; "Sequence of minutes 4-25 of Escherichia coli."; Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[6]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).
[7]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-103. STRAIN=K12; PubMed=7721718 [NCBI, ExPASy, EBI, Israel, Japan] Harlow K.W., Nygaard P., Hove-Jensen B.; "Cloning and characterization of the gsk gene encoding guanosine kinase of Escherichia coli."; J. Bacteriol. 177:2236-2240(1995).
[8]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21. STRAIN=K12; Mori H., Iida A., Teshiba S., Fujio T.; Submitted (DEC-1990) to the EMBL/GenBank/DDBJ databases.
[9]	PROTEIN SEQUENCE OF 1-10, AND BIOPHYSICOCHEMICAL PROPERTIES. PubMed=9576853 [NCBI, ExPASy, EBI, Israel, Japan] Kanaya S., Koyanagi T., Kanaya E.; "An esterase from Escherichia coli with a sequence similarity to hormone-sensitive lipase."; Biochem. J. 332:75-80(1998).
[10]	MUTAGENESIS OF HIS-103; GLU-128; GLY-163; ASP-164; SER-165; GLY-167; ASP-262; ASP-266 AND HIS-292. DOI=10.1016/S0014-5793(99)00813-3; PubMed=10431819 [NCBI, ExPASy, EBI, Israel, Japan] Haruki M., Oohashi Y., Mizuguchi S., Matsuo Y., Morikawa M., Kanaya S.; "Identification of catalytically essential residues in Escherichia coli esterase by site-directed mutagenesis."; FEBS Lett. 454:262-266(1999).
[11]	FUNCTION, AND INTERACTION WITH MALT. DOI=10.1074/jbc.M200991200; PubMed=11867639 [NCBI, ExPASy, EBI, Israel, Japan] Joly N., Danot O., Schlegel A., Boos W., Richet E.; "The Aes protein directly controls the activity of MalT, the central transcriptional activator of the Escherichia coli maltose regulon."; J. Biol. Chem. 277:16606-16613(2002).
[12]	FUNCTION, DIMERIZATION, AND INTERACTION WITH MELA. DOI=10.1074/jbc.M207398200; PubMed=12374803 [NCBI, ExPASy, EBI, Israel, Japan] Mandrich L., Caputo E., Martin B.M., Rossi M., Manco G.; "The Aes protein and the monomeric alpha-galactosidase from Escherichia coli form a non-covalent complex. Implications for the regulation of carbohydrate metabolism."; J. Biol. Chem. 277:48241-48247(2002).

Comments

FUNCTION: Displays esterase activity towards short chain fatty esters (acyl chain length of up to 8 carbons). Able to hydrolyze triacetylglycerol (triacetin) and tributyrylglycerol (tributyrin), but not trioleylglycerol (triolein) or cholesterol oleate. Negatively regulates malT activity by antagonizing maltotriose binding. Inhibits melA galactosidase activity.

BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters:	K_M=1.5 mM for p-nitrophenylacetate (at pH 7.1 and 25 degrees Celsius);
	K_M=0.7 mM for p-nitrophenylpropionate (at pH 7.1 and 25 degrees Celsius);
	K_M=0.5 mM for p-nitrophenylbutyrate (at pH 7.1 and 25 degrees Celsius);
	K_M=0.26 mM for p-nitrophenylvalerate (at pH 7.1 and 25 degrees Celsius);
	K_M=0.22 mM for p-nitrophenylhexanoate (at pH 7.1 and 25 degrees Celsius);
	K_M=0.16 mM for p-nitrophenyloctanoate (at pH 7.1 and 25 degrees Celsius);
	V_max=34.2 µmol/min/mg enzyme toward p-nitrophenylbutyrate (at pH 5.6 and 30 degrees Celsius);
	V_max=3.67 µmol/min/mg enzyme toward tributyrylglycerol (at pH 5.6 and 30 degrees Celsius);
	V_max=0.22 µmol/min/mg enzyme toward trioleylglycerol (at pH 5.6 and 30 degrees Celsius);
pH dependence:	Optimum pH is 9.0;

SUBUNIT: Homodimer. Interacts with malT and melA.
SUBCELLULAR LOCATION: Cytoplasm.
MISCELLANEOUS: Not essential for cell growth.
SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
SEQUENCE CAUTION:
- Sequence=L35149; Type=Frameshift; Positions=37;

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

D90259; BAA14305.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U82664; AAB40230.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC73578.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE76255.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D00798; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
L35149; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]

PIR

C64778; C64778.

RefSeq

AP_001125.1; -.
NP_415009.1; -.

3D structure databases

ModBase

P23872.

Protein-protein interaction databases

DIP

DIP:9062N; -.

Enzyme and pathway databases

BioCyc

EcoCyc:EG11101-MON; -.
MetaCyc:EG11101-MON; -.

Organism-specific databases

EchoBASE

EB1093; -.

EcoGene

EG11101; aes.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004091;	Molecular function: carboxylesterase activity (inferred from electronic annotation from HAMAP).
GO:0008152;	Biological process: metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

HAMAP

MF_01958; -; 1.
PBIL [Tree]

InterPro

IPR013094; AB_hydrolase_3.
IPR002168; Lipase_GDXG_AS.
Graphical view of domain structure.

Pfam

PF07859; Abhydrolase_3; 1.
Pfam graphical view of domain structure.

PROSITE

PS01173; LIPASE_GDXG_HIS; 1.
PS01174; LIPASE_GDXG_SER; 1.

ProtoNet

P23872.

Genome annotation databases

GeneID

947514; -.

GenomeReviews

U00096_GR; b0476.
AP009048_GR; JW0465.

KEGG

ecj:JW0465; -.
eco:b0476; -.

Phylogenomic databases

HOGENOM

P23872; -.

Genome annotation databases

CMR

P23872; b0476.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase; Serine esterase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 319`	`319`	`Acetyl esterase.`	`PRO_0000071555`
`ACT_SITE`	`165 165`		`Probable.`
`ACT_SITE`	`262 262`		`Probable.`
`ACT_SITE`	`292 292`		`Probable.`
`MUTAGEN`	`103 103`		`H->A: Reduces enzymatic efficiency.`
`MUTAGEN`	`128 128`		`E->A: Reduces enzymatic efficiency.`
`MUTAGEN`	`163 163`		`G->A: Diminishes catalytic efficiency.`
`MUTAGEN`	`164 164`		`D->A: Strongly reduces enzymatic activity.`
`MUTAGEN`	`165 165`		`S->A: Abolishes enzymatic activity.`
`MUTAGEN`	`167 167`		`G->A: Diminishes substrate affinity.`
`MUTAGEN`	`262 262`		`D->A: Strongly reduces enzymatic activity.`
`MUTAGEN`	`266 266`		`D->A: Reduces enzymatic efficiency.`
`MUTAGEN`	`292 292`		`H->A: Abolishes enzymatic activity.`
`CONFLICT`	`18 18`		`K -> N (in Ref. 8).`
`CONFLICT`	`275 319`		`LAAHQQPCEFKLYPGTLHAFLHYSRMMKTADEALRDGAQF` `FTAQL -> VSCASAAL (in Ref. 2).`

Sequence information

Length: 319 AA [This is the length of the unprocessed precursor]

Molecular weight: 36034 Da [This is the MW of the unprocessed precursor]

CRC64: 4F9E234E23CCE7D0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKPENKLPVL DLISAEMKTV VNTLQPDLPP WPATGTIAEQ RQYYTLERRF WNAGAPEMAT 

        70         80         90        100        110        120 
RAYMVPTKYG QVETRLFCPQ PDSPATLFYL HGGGFILGNL DTHDRIMRLL ASYSQCTVIG 

       130        140        150        160        170        180 
IDYTLSPEAR FPQAIEEIVA ACCYFHQQAE DYQINMSRIG FAGDSAGAML ALASALWLRD 

       190        200        210        220        230        240 
KQIDCGKVAG VLLWYGLYGL RDSVTRRLLG GVWDGLTQQD LQMYEEAYLS NDADRESPYY 

       250        260        270        280        290        300 
CLFNNDLTRE VPPCFIAGAE FDPLLDDSRL LYQTLAAHQQ PCEFKLYPGT LHAFLHYSRM 

       310 
MKTADEALRD GAQFFTAQL

P23872 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools