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Protein

Enterobactin synthase component E

Gene

entE

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

Functioni

Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provide hexadentate coordination for the tightly ligated iron2+ atoms. EntE proccesses via a two-step adenylation-ligation reaction (bi-uni-uni-bi ping-pong mechanism). First, it catalyzes the activation of the carboxylate group of 2,3-dihydroxy-benzoate (DHB), via a reversible ATP-dependent pyrophosphate exchange reactions to yield the acyladenylate intermediate 2,3-dihydroxybenzoyl-AMP. It can also transfer AMP to salicylate, 2,4-dihydroxybenzoate, gentisate and 2,3,4-trihydroxybenzoate. In the second step, DHB is transferred from 2,3-dihydroxybenzoyl-AMP onto the phosphopantetheinylated EntB (holo-EntB) to form DHB-holo-EntB. Then this product will serve in the formation of the amide bond between 2,3-dihydroxybenzoate (DHB) and L-serine. It can also transfer adenylated salicylate to holo-EntB.10 Publications

Catalytic activityi

6 ATP + 3 2,3-dihydroxybenzoate + 3 L-serine = enterobactin + 6 AMP + 6 diphosphate.7 Publications
ATP + 2,3-dihydroxybenzoate = diphosphate + (2,3-dihydroxybenzoyl)adenylate.6 Publications
(2,3-dihydroxybenzoyl)adenylate + holo-entB = adenosine 5'-monophosphate + aryl-holo-entB.7 Publications

Enzyme regulationi

Inhibited by the adenylate analogs, 5'-O-[N-(salicyl)sulfamoyl]adenosine (Sal-AMS) and 5'-O-[N-(2,3-dihydroxybenzoyl)sulfamoyl]adenosine (DHB-AMS). Adenylation of 2,3-dihydroxybenzoate (DHB) is enhanced by a protein-protein interaction between the EntA and EntE.2 Publications

Kineticsi

Kcat is 0.3 sec(-1) for 2,3-dihydroxybenzoate-AMP ligase activity with 3-hydroxybenzoate as substrate (at pH 7.8 and 25 degrees Celsius). Kcat is 0.8 sec(-1) for 2,3-dihydroxybenzoate-AMP ligase activity with salicylate as substrate (at pH 7.8 and 25 degrees Celsius). Kcat is 0.9 sec(-1) for S-dihydroxybenzoyltransferase activity with D-pantetheine as substrate (at pH 7.8 and 25 degrees Celsius). Kcat is 2.8 sec(-1) for 2,3-dihydroxybenzoate-AMP ligase activity with ATP and DHB as substrates (at pH 7.8 and 25 degrees Celsius). Kcat is 2.8 sec(-1) for S-dihydroxybenzoyltransferase activity with holo-EntB as substrate (at pH 7.8 and 25 degrees Celsius). Kcat is 4.4 sec(-1) for 2,3-dihydroxybenzoate-AMP ligase activity with 4-aminosalicylate as substrate (at pH 7.8 and 25 degrees Celsius). Kcat is 5.94 sec(-1) for S-dihydroxybenzoyltransferase activity with holo-EntB as substrate (at pH 7.8 and 25 degrees Celsius). Kcat is 100 min(-1) for S-dihydroxybenzoyltransferase activity with holo-EntB as substrate (at pH 8.8 and 37 degrees Celsius). Kcat is 140 min(-1) for S-dihydroxybenzoyltransferase activity with holo-EntB as substrate.4 Publications

  1. KM=0.4 µM for holo-EntB (at pH 8.8 and 37 degrees Celsius)1 Publication
  2. KM=0.5 µM for holo-EntB1 Publication
  3. KM=2.5 µM for DHB (at pH 7.8 and 25 degrees Celsius)1 Publication
  4. KM=2.7 µM for DHB1 Publication
  5. KM=2.9 µM for DHB1 Publication
  6. KM=2.9 µM for holo-EntB (at pH 7.8 and 25 degrees Celsius)1 Publication
  7. KM=23.3 µM for holo-EntB (at pH 7.5 and 37 degrees Celsius)1 Publication
  8. KM=70 µM for 3-hydroxybenzoate (at pH 7.8 and 25 degrees Celsius)1 Publication
  9. KM=70 µM for salicylate (at pH 7.8 and 25 degrees Celsius)1 Publication
  10. KM=400 µM for 5,5-diadenosine tetraphosphate1 Publication
  11. KM=430 µM for ATP (at pH 7.8 and 25 degrees Celsius)1 Publication
  12. KM=1200 µM for ATP1 Publication
  13. KM=3100 µM for 4-aminosalicylate (at pH 7.8 and 25 degrees Celsius)1 Publication
  14. KM=34.2 mM for D-pantetheine (at pH 7.8 and 25 degrees Celsius)1 Publication
  1. Vmax=3168.2 pmol/min/mg enzyme1 Publication

Pathwayi: enterobactin biosynthesis

This protein is involved in the pathway enterobactin biosynthesis, which is part of Siderophore biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway enterobactin biosynthesis and in Siderophore biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei235 – 2351Substrate1 Publication
Binding sitei240 – 2401Substrate1 Publication
Binding sitei309 – 3091Substrate; via amide nitrogen2 Publications
Binding sitei331 – 3311Substrate; via carbonyl oxygen2 Publications
Binding sitei335 – 3351Substrate; via amide nitrogen1 Publication
Binding sitei415 – 4151Substrate2 Publications
Binding sitei432 – 4321Substrate1 Publication
Binding sitei441 – 4411Substrate1 Publication

GO - Molecular functioni

  • (2,3-dihydroxybenzoyl)adenylate synthase activity Source: EcoCyc
  • 2,3-dihydroxybenzoate-serine ligase activity Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • transferase activity, transferring acyl groups Source: UniProtKB-KW

GO - Biological processi

  • enterobactin biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Ligase, Transferase

Keywords - Biological processi

Enterobactin biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:ENTE-MONOMER.
ECOL316407:JW0586-MONOMER.
MetaCyc:ENTE-MONOMER.
BRENDAi6.3.2.14. 2026.
UniPathwayiUPA00017.

Names & Taxonomyi

Protein namesi
Recommended name:
Enterobactin synthase component E1 Publication (EC:6.3.2.147 Publications)
Alternative name(s):
2,3-dihydroxybenzoate-AMP ligase1 Publication
Short name:
DHB-AMP ligase1 Publication
2,3-dihydroxybenzoate-AMP synthaseCurated (EC:2.7.7.586 Publications)
Dihydroxybenzoic acid-activating enzyme1 Publication
Enterochelin synthase E1 Publication
S-dihydroxybenzoyltransferase1 Publication (EC:2.5.1.-6 Publications)
Gene namesi
Name:entE1 Publication
Ordered Locus Names:b0594, JW0586
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10263. entE.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi437 – 4371R → D: Catalyzes the adenylation reaction with 10% reduction of activity compared to the wild-type. 3% reduction of activity compared to the wild-type; when associated with D-473. 1 Publication
Mutagenesisi473 – 4731K → D: Catalyzes the adenylation reaction with same activity as the wild-type. 3% reduction of activity compared to the wild-type; when associated with D-437. 1 Publication
Mutagenesisi494 – 4941R → D: Catalyzes the adenylation reaction with same activity as the wild-type. 1 Publication

Chemistry

ChEMBLiCHEMBL4856.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 536536Enterobactin synthase component EPRO_0000193075Add
BLAST

Proteomic databases

EPDiP10378.
PaxDbiP10378.
PRIDEiP10378.

Expressioni

Inductioni

Under conditions of iron deficiency and by the fur protein.2 Publications

Interactioni

Subunit structurei

Proteins EntB, EntD, EntE, and EntF form a multienzyme complex called enterobactin synthase. Monomer. EntA and EntE interact together.5 Publications

Protein-protein interaction databases

BioGridi4259905. 320 interactions.
DIPiDIP-9515N.
IntActiP10378. 13 interactions.
MINTiMINT-1228110.
STRINGi511145.b0594.

Chemistry

BindingDBiP10378.

Structurei

Secondary structure

1
536
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 189Combined sources
Helixi29 – 324Combined sources
Turni33 – 364Combined sources
Beta strandi39 – 446Combined sources
Beta strandi47 – 504Combined sources
Helixi51 – 6717Combined sources
Beta strandi75 – 795Combined sources
Helixi85 – 9612Combined sources
Beta strandi99 – 1035Combined sources
Helixi109 – 11911Combined sources
Beta strandi122 – 1276Combined sources
Helixi131 – 1333Combined sources
Beta strandi134 – 1363Combined sources
Helixi137 – 1459Combined sources
Beta strandi151 – 1555Combined sources
Helixi163 – 1686Combined sources
Beta strandi183 – 1897Combined sources
Beta strandi193 – 1964Combined sources
Beta strandi199 – 2035Combined sources
Helixi204 – 21815Combined sources
Beta strandi225 – 2284Combined sources
Helixi235 – 2395Combined sources
Helixi242 – 2498Combined sources
Beta strandi252 – 2554Combined sources
Helixi261 – 27111Combined sources
Beta strandi275 – 2784Combined sources
Helixi280 – 29112Combined sources
Helixi296 – 2994Combined sources
Beta strandi304 – 3107Combined sources
Helixi314 – 32310Combined sources
Beta strandi326 – 3349Combined sources
Beta strandi337 – 3415Combined sources
Helixi348 – 3536Combined sources
Beta strandi357 – 3604Combined sources
Beta strandi364 – 3685Combined sources
Beta strandi380 – 3867Combined sources
Beta strandi388 – 3903Combined sources
Helixi398 – 4047Combined sources
Beta strandi411 – 4199Combined sources
Beta strandi425 – 4306Combined sources
Beta strandi432 – 4376Combined sources
Beta strandi440 – 4434Combined sources
Helixi444 – 4518Combined sources
Beta strandi457 – 46711Combined sources
Turni468 – 4703Combined sources
Beta strandi471 – 48212Combined sources
Helixi486 – 4949Combined sources
Turni495 – 4973Combined sources
Helixi500 – 5023Combined sources
Beta strandi505 – 5095Combined sources
Beta strandi519 – 5213Combined sources
Helixi523 – 5319Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3RG2X-ray3.10A/B/C/D/E/F/G/H/I/J1-536[»]
4IZ6X-ray2.40A/B1-536[»]
ProteinModelPortaliP10378.
SMRiP10378. Positions 1-536.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni438 – 4392Phosphopantetheine binding2 Publications

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108IQC. Bacteria.
COG1021. LUCA.
HOGENOMiHOG000230011.
InParanoidiP10378.
KOiK02363.
OMAiRSNEICH.
OrthoDBiEOG600DJW.
PhylomeDBiP10378.

Family and domain databases

InterProiIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR011963. DHB_AMP_lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02275. DHB_AMP_lig. 1 hit.
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P10378-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIPFTRWPE EFARRYREKG YWQDLPLTDI LTRHAASDSI AVIDGERQLS
60 70 80 90 100
YRELNQAADN LACSLRRQGI KPGETALVQL GNVAELYITF FALLKLGVAP
110 120 130 140 150
VLALFSHQRS ELNAYASQIE PALLIADRQH ALFSGDDFLN TFVTEHSSIR
160 170 180 190 200
VVQLLNDSGE HNLQDAINHP AEDFTATPSP ADEVAYFQLS GGTTGTPKLI
210 220 230 240 250
PRTHNDYYYS VRRSVEICQF TQQTRYLCAI PAAHNYAMSS PGSLGVFLAG
260 270 280 290 300
GTVVLAADPS ATLCFPLIEK HQVNVTALVP PAVSLWLQAL IEGESRAQLA
310 320 330 340 350
SLKLLQVGGA RLSATLAARI PAEIGCQLQQ VFGMAEGLVN YTRLDDSAEK
360 370 380 390 400
IIHTQGYPMC PDDEVWVADA EGNPLPQGEV GRLMTRGPYT FRGYYKSPQH
410 420 430 440 450
NASAFDANGF YCSGDLISID PEGYITVQGR EKDQINRGGE KIAAEEIENL
460 470 480 490 500
LLRHPAVIYA ALVSMEDELM GEKSCAYLVV KEPLRAVQVR RFLREQGIAE
510 520 530
FKLPDRVECV DSLPLTAVGK VDKKQLRQWL ASRASA
Length:536
Mass (Da):59,112
Last modified:November 1, 1997 - v3
Checksum:iF818942DFDD8DC99
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti369 – 37810DAEGNPLPQG → ECRRKSTAAR in CAA33158 (PubMed:2525505).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15058 Genomic DNA. Translation: CAA33158.1.
U82598 Genomic DNA. Translation: AAB40794.1.
U00096 Genomic DNA. Translation: AAC73695.1.
AP009048 Genomic DNA. Translation: BAE76349.1.
M24148 Unassigned DNA. Translation: AAA16101.1.
M36700 Genomic DNA. Translation: AAA18492.1.
PIRiH64792. SYECEB.
RefSeqiNP_415126.1. NC_000913.3.
WP_000026812.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73695; AAC73695; b0594.
BAE76349; BAE76349; BAE76349.
GeneIDi947426.
KEGGiecj:JW0586.
eco:b0594.
PATRICi32116364. VBIEscCol129921_0622.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15058 Genomic DNA. Translation: CAA33158.1.
U82598 Genomic DNA. Translation: AAB40794.1.
U00096 Genomic DNA. Translation: AAC73695.1.
AP009048 Genomic DNA. Translation: BAE76349.1.
M24148 Unassigned DNA. Translation: AAA16101.1.
M36700 Genomic DNA. Translation: AAA18492.1.
PIRiH64792. SYECEB.
RefSeqiNP_415126.1. NC_000913.3.
WP_000026812.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3RG2X-ray3.10A/B/C/D/E/F/G/H/I/J1-536[»]
4IZ6X-ray2.40A/B1-536[»]
ProteinModelPortaliP10378.
SMRiP10378. Positions 1-536.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259905. 320 interactions.
DIPiDIP-9515N.
IntActiP10378. 13 interactions.
MINTiMINT-1228110.
STRINGi511145.b0594.

Chemistry

BindingDBiP10378.
ChEMBLiCHEMBL4856.

Proteomic databases

EPDiP10378.
PaxDbiP10378.
PRIDEiP10378.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73695; AAC73695; b0594.
BAE76349; BAE76349; BAE76349.
GeneIDi947426.
KEGGiecj:JW0586.
eco:b0594.
PATRICi32116364. VBIEscCol129921_0622.

Organism-specific databases

EchoBASEiEB0259.
EcoGeneiEG10263. entE.

Phylogenomic databases

eggNOGiENOG4108IQC. Bacteria.
COG1021. LUCA.
HOGENOMiHOG000230011.
InParanoidiP10378.
KOiK02363.
OMAiRSNEICH.
OrthoDBiEOG600DJW.
PhylomeDBiP10378.

Enzyme and pathway databases

UniPathwayiUPA00017.
BioCyciEcoCyc:ENTE-MONOMER.
ECOL316407:JW0586-MONOMER.
MetaCyc:ENTE-MONOMER.
BRENDAi6.3.2.14. 2026.

Miscellaneous databases

PROiP10378.

Family and domain databases

InterProiIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR011963. DHB_AMP_lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02275. DHB_AMP_lig. 1 hit.
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the Escherichia coli entE gene."
    Staab J.F., Elkins M.F., Earhart C.F.
    FEMS Microbiol. Lett. 50:15-19(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "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.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "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.
  5. "Opacity factor from group A streptococci is an apoproteinase."
    Elkins M.F., Earhart C.F.
    FEMS Microbiol. Lett. 56:35-39(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
    Strain: K12.
  6. "Nucleotide sequence of a cluster of Escherichia coli enterobactin biosynthesis genes: identification of entA and purification of its product 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase."
    Liu J., Duncan K., Walsh C.T.
    J. Bacteriol. 171:791-798(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 393-536.
  7. "Regulation of enterobactin iron transport in Escherichia coli: characterization of ent::Mu d(Apr lac) operon fusions."
    Fleming T.P., Nahlik M.S., McIntosh M.A.
    J. Bacteriol. 156:1171-1177(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  8. "Subcloning, expression, and purification of the enterobactin biosynthetic enzyme 2,3-dihydroxybenzoate-AMP ligase: demonstration of enzyme-bound (2,3-dihydroxybenzoyl)adenylate product."
    Rusnak F., Faraci W.S., Walsh C.T.
    Biochemistry 28:6827-6835(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBSTRATE SPECIFICITY.
  9. "Nucleotide sequence and transcriptional organization of the Escherichia coli enterobactin biosynthesis cistrons entB and entA."
    Nahlik M.S., Brickman T.J., Ozenberger B.A., McIntosh M.A.
    J. Bacteriol. 171:784-790(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  10. "Enterobactin biosynthesis in Escherichia coli: isochorismate lyase (EntB) is a bifunctional enzyme that is phosphopantetheinylated by EntD and then acylated by EntE using ATP and 2,3-dihydroxybenzoate."
    Gehring A.M., Bradley K.A., Walsh C.T.
    Biochemistry 36:8495-8503(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY.
  11. "Reconstitution and characterization of the Escherichia coli enterobactin synthetase from EntB, EntE, and EntF."
    Gehring A.M., Mori I., Walsh C.T.
    Biochemistry 37:2648-2659(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  12. "Membrane association of the Escherichia coli enterobactin synthase proteins EntB/G, EntE, and EntF."
    Hantash F.M., Earhart C.F.
    J. Bacteriol. 182:1768-1773(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  13. "The EntF and EntE adenylation domains of Escherichia coli enterobactin synthetase: sequestration and selectivity in acyl-AMP transfers to thiolation domain cosubstrates."
    Ehmann D.E., Shaw-Reid C.A., Losey H.C., Walsh C.T.
    Proc. Natl. Acad. Sci. U.S.A. 97:2509-2514(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM.
  14. "Structure of the EntB multidomain nonribosomal peptide synthetase and functional analysis of its interaction with the EntE adenylation domain."
    Drake E.J., Nicolai D.A., Gulick A.M.
    Chem. Biol. 13:409-419(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ARG-437; LYS-473 AND ARG-494, BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM.
  15. "A protein interaction surface in nonribosomal peptide synthesis mapped by combinatorial mutagenesis and selection."
    Lai J.R., Fischbach M.A., Liu D.R., Walsh C.T.
    Proc. Natl. Acad. Sci. U.S.A. 103:5314-5319(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
  16. "Enterobactin synthetase-catalyzed formation of P(1),P(3)-diadenosine-5'-tetraphosphate."
    Sikora A.L., Cahill S.M., Blanchard J.S.
    Biochemistry 48:10827-10829(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MISCELLANEOUS.
  17. "Ligand-induced conformational rearrangements promote interaction between the Escherichia coli enterobactin biosynthetic proteins EntE and EntB."
    Khalil S., Pawelek P.D.
    J. Mol. Biol. 393:658-671(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBSTRATE SPECIFICITY.
  18. "Kinetic and inhibition studies of dihydroxybenzoate-AMP ligase from Escherichia coli."
    Sikora A.L., Wilson D.J., Aldrich C.C., Blanchard J.S.
    Biochemistry 49:3648-3657(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, REACTION MECHANISM.
  19. "MbtH-like proteins as integral components of bacterial nonribosomal peptide synthetases."
    Felnagle E.A., Barkei J.J., Park H., Podevels A.M., McMahon M.D., Drott D.W., Thomas M.G.
    Biochemistry 49:8815-8817(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
  20. "Enzymatic adenylation of 2,3-dihydroxybenzoate is enhanced by a protein-protein interaction between Escherichia coli 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase (EntA) and 2,3-dihydroxybenzoate-AMP ligase (EntE)."
    Khalil S., Pawelek P.D.
    Biochemistry 50:533-545(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, ENZYME REGULATION.
  21. "Structural and functional investigation of the intermolecular interaction between NRPS adenylation and carrier protein domains."
    Sundlov J.A., Shi C., Wilson D.J., Aldrich C.C., Gulick A.M.
    Chem. Biol. 19:188-198(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG AND PHOSPHOPANTETHEINE, SUBUNIT.
  22. "Structure determination of the functional domain interaction of a chimeric nonribosomal peptide synthetase from a challenging crystal with noncrystallographic translational symmetry."
    Sundlov J.A., Gulick A.M.
    Acta Crystallogr. D 69:1482-1492(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF CHIMERIC ENTE-ENTB CONSTRUCT IN COMPLEX WITH SUBSTRATE ANALOG AND PHOSPHOPANTETHEINE, SUBUNIT.

Entry informationi

Entry nameiENTE_ECOLI
AccessioniPrimary (citable) accession number: P10378
Secondary accession number(s): P15049, P77773, Q2MBK7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 1, 1997
Last modified: March 16, 2016
This is version 146 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

In the absence of holo-EntB, EntE can transfer the adenylate moiety of the 2,3-dihydroxybenzoyl-AMP intermediate to ATP, generating the stress signaling molecule Ap4A involved in the regulation of cell division during oxidative stress, and releasing 2,3-dihydroxybenzoate. It seems that the expression of EntE during iron starvation produces Ap4A to slow growth until intracellular iron stores can be restored.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.