ID   ENTE_ECOLI              Reviewed;         536 AA.
AC   P10378; P15049; P77773; Q2MBK7;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 3.
DT   02-SEP-2026, entry version 195.
DE   RecName: Full=Enterobactin synthase component E {ECO:0000303|PubMed:9485415};
DE            EC=6.3.2.14 {ECO:0000269|PubMed:10688898, ECO:0000269|PubMed:16567620, ECO:0000269|PubMed:19852513, ECO:0000269|PubMed:20359185, ECO:0000269|PubMed:20845982, ECO:0000269|PubMed:2531000, ECO:0000269|PubMed:9214294};
DE   AltName: Full=2,3-dihydroxybenzoate-AMP ligase {ECO:0000303|PubMed:2531000};
DE            Short=DHB-AMP ligase {ECO:0000303|PubMed:2531000};
DE   AltName: Full=2,3-dihydroxybenzoate-AMP synthase {ECO:0000305};
DE            EC=6.2.1.71 {ECO:0000269|PubMed:10688898, ECO:0000269|PubMed:16567620, ECO:0000269|PubMed:19852513, ECO:0000269|PubMed:20359185, ECO:0000269|PubMed:20845982, ECO:0000269|PubMed:2531000};
DE   AltName: Full=Dihydroxybenzoic acid-activating enzyme {ECO:0000303|PubMed:2531000};
DE   AltName: Full=Enterochelin synthase E {ECO:0000303|PubMed:9485415};
GN   Name=entE {ECO:0000303|PubMed:2525505};
GN   OrderedLocusNames=b0594, JW0586;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=2525505; DOI=10.1016/0378-1097(89)90450-3;
RA   Staab J.F., Elkins M.F., Earhart C.F.;
RT   "Nucleotide sequence of the Escherichia coli entE gene.";
RL   FEMS Microbiol. Lett. 50:15-19(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RA   Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA   Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA   Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT   "Sequence of minutes 4-25 of Escherichia coli.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
RC   STRAIN=K12;
RX   PubMed=2110093; DOI=10.1111/j.1574-6968.1990.tb04118.x;
RA   Elkins M.F., Earhart C.F.;
RT   "Opacity factor from group A streptococci is an apoproteinase.";
RL   FEMS Microbiol. Lett. 56:35-39(1990).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 393-536.
RX   PubMed=2521622; DOI=10.1128/jb.171.2.791-798.1989;
RA   Liu J., Duncan K., Walsh C.T.;
RT   "Nucleotide sequence of a cluster of Escherichia coli enterobactin
RT   biosynthesis genes: identification of entA and purification of its product
RT   2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase.";
RL   J. Bacteriol. 171:791-798(1989).
RN   [7]
RP   INDUCTION.
RX   PubMed=6227609; DOI=10.1128/jb.156.3.1171-1177.1983;
RA   Fleming T.P., Nahlik M.S., McIntosh M.A.;
RT   "Regulation of enterobactin iron transport in Escherichia coli:
RT   characterization of ent::Mu d(Apr lac) operon fusions.";
RL   J. Bacteriol. 156:1171-1177(1983).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP   SUBSTRATE SPECIFICITY.
RX   PubMed=2531000; DOI=10.1021/bi00443a008;
RA   Rusnak F., Faraci W.S., Walsh C.T.;
RT   "Subcloning, expression, and purification of the enterobactin biosynthetic
RT   enzyme 2,3-dihydroxybenzoate-AMP ligase: demonstration of enzyme-bound
RT   (2,3-dihydroxybenzoyl)adenylate product.";
RL   Biochemistry 28:6827-6835(1989).
RN   [9]
RP   INDUCTION.
RX   PubMed=2521621; DOI=10.1128/jb.171.2.784-790.1989;
RA   Nahlik M.S., Brickman T.J., Ozenberger B.A., McIntosh M.A.;
RT   "Nucleotide sequence and transcriptional organization of the Escherichia
RT   coli enterobactin biosynthesis cistrons entB and entA.";
RL   J. Bacteriol. 171:784-790(1989).
RN   [10]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
RP   SPECIFICITY.
RX   PubMed=9214294; DOI=10.1021/bi970453p;
RA   Gehring A.M., Bradley K.A., Walsh C.T.;
RT   "Enterobactin biosynthesis in Escherichia coli: isochorismate lyase (EntB)
RT   is a bifunctional enzyme that is phosphopantetheinylated by EntD and then
RT   acylated by EntE using ATP and 2,3-dihydroxybenzoate.";
RL   Biochemistry 36:8495-8503(1997).
RN   [11]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=9485415; DOI=10.1021/bi9726584;
RA   Gehring A.M., Mori I., Walsh C.T.;
RT   "Reconstitution and characterization of the Escherichia coli enterobactin
RT   synthetase from EntB, EntE, and EntF.";
RL   Biochemistry 37:2648-2659(1998).
RN   [12]
RP   SUBCELLULAR LOCATION.
RX   PubMed=10692387; DOI=10.1128/jb.182.6.1768-1773.2000;
RA   Hantash F.M., Earhart C.F.;
RT   "Membrane association of the Escherichia coli enterobactin synthase
RT   proteins EntB/G, EntE, and EntF.";
RL   J. Bacteriol. 182:1768-1773(2000).
RN   [13]
RP   FUNCTION, CATALYTIC ACTIVITY, AND REACTION MECHANISM.
RX   PubMed=10688898; DOI=10.1073/pnas.040572897;
RA   Ehmann D.E., Shaw-Reid C.A., Losey H.C., Walsh C.T.;
RT   "The EntF and EntE adenylation domains of Escherichia coli enterobactin
RT   synthetase: sequestration and selectivity in acyl-AMP transfers to
RT   thiolation domain cosubstrates.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:2509-2514(2000).
RN   [14]
RP   FUNCTION, MUTAGENESIS OF ARG-437; LYS-473 AND ARG-494, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND REACTION MECHANISM.
RX   PubMed=16632253; DOI=10.1016/j.chembiol.2006.02.005;
RA   Drake E.J., Nicolai D.A., Gulick A.M.;
RT   "Structure of the EntB multidomain nonribosomal peptide synthetase and
RT   functional analysis of its interaction with the EntE adenylation domain.";
RL   Chem. Biol. 13:409-419(2006).
RN   [15]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=16567620; DOI=10.1073/pnas.0601038103;
RA   Lai J.R., Fischbach M.A., Liu D.R., Walsh C.T.;
RT   "A protein interaction surface in nonribosomal peptide synthesis mapped by
RT   combinatorial mutagenesis and selection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5314-5319(2006).
RN   [16]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   MISCELLANEOUS.
RX   PubMed=19852513; DOI=10.1021/bi901680m;
RA   Sikora A.L., Cahill S.M., Blanchard J.S.;
RT   "Enterobactin synthetase-catalyzed formation of P(1),P(3)-diadenosine-5'-
RT   tetraphosphate.";
RL   Biochemistry 48:10827-10829(2009).
RN   [17]
RP   FUNCTION, AND SUBSTRATE SPECIFICITY.
RX   PubMed=19699210; DOI=10.1016/j.jmb.2009.08.036;
RA   Khalil S., Pawelek P.D.;
RT   "Ligand-induced conformational rearrangements promote interaction between
RT   the Escherichia coli enterobactin biosynthetic proteins EntE and EntB.";
RL   J. Mol. Biol. 393:658-671(2009).
RN   [18]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP   REGULATION, AND REACTION MECHANISM.
RX   PubMed=20359185; DOI=10.1021/bi100350c;
RA   Sikora A.L., Wilson D.J., Aldrich C.C., Blanchard J.S.;
RT   "Kinetic and inhibition studies of dihydroxybenzoate-AMP ligase from
RT   Escherichia coli.";
RL   Biochemistry 49:3648-3657(2010).
RN   [19]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=20845982; DOI=10.1021/bi1012854;
RA   Felnagle E.A., Barkei J.J., Park H., Podevels A.M., McMahon M.D.,
RA   Drott D.W., Thomas M.G.;
RT   "MbtH-like proteins as integral components of bacterial nonribosomal
RT   peptide synthetases.";
RL   Biochemistry 49:8815-8817(2010).
RN   [20]
RP   FUNCTION, SUBUNIT, AND ACTIVITY REGULATION.
RX   PubMed=21166461; DOI=10.1021/bi101558v;
RA   Khalil S., Pawelek P.D.;
RT   "Enzymatic adenylation of 2,3-dihydroxybenzoate is enhanced by a protein-
RT   protein interaction between Escherichia coli 2,3-dihydro-2,3-
RT   dihydroxybenzoate dehydrogenase (EntA) and 2,3-dihydroxybenzoate-AMP ligase
RT   (EntE).";
RL   Biochemistry 50:533-545(2011).
RN   [21]
RP   X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG AND
RP   PHOSPHOPANTETHEINE, AND SUBUNIT.
RX   PubMed=22365602; DOI=10.1016/j.chembiol.2011.11.013;
RA   Sundlov J.A., Shi C., Wilson D.J., Aldrich C.C., Gulick A.M.;
RT   "Structural and functional investigation of the intermolecular interaction
RT   between NRPS adenylation and carrier protein domains.";
RL   Chem. Biol. 19:188-198(2012).
RN   [22]
RP   X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF CHIMERIC ENTE-ENTB CONSTRUCT IN
RP   COMPLEX WITH SUBSTRATE ANALOG AND PHOSPHOPANTETHEINE, AND SUBUNIT.
RX   PubMed=23897471; DOI=10.1107/s0907444913009372;
RA   Sundlov J.A., Gulick A.M.;
RT   "Structure determination of the functional domain interaction of a chimeric
RT   nonribosomal peptide synthetase from a challenging crystal with
RT   noncrystallographic translational symmetry.";
RL   Acta Crystallogr. D 69:1482-1492(2013).
CC   -!- FUNCTION: Involved in the biosynthesis of the siderophore enterobactin
CC       (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-
CC       dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding
CC       for the three catechol functionalities that provide hexadentate
CC       coordination for the tightly ligated iron(2+) atoms. EntE processes via
CC       a two-step adenylation-ligation reaction (bi-uni-uni-bi ping-pong
CC       mechanism). First, it catalyzes the activation of the carboxylate group
CC       of 2,3-dihydroxy-benzoate (DHB), via a reversible ATP-dependent
CC       pyrophosphate exchange reactions to yield the acyladenylate
CC       intermediate 2,3-dihydroxybenzoyl-AMP. It can also transfer AMP to
CC       salicylate, 2,4-dihydroxybenzoate, gentisate and 2,3,4-
CC       trihydroxybenzoate. In the second step, DHB is transferred from 2,3-
CC       dihydroxybenzoyl-AMP onto the phosphopantetheinylated EntB (holo-EntB)
CC       to form DHB-holo-EntB. Then this product will serve in the formation of
CC       the amide bond between 2,3-dihydroxybenzoate (DHB) and L-serine. It can
CC       also transfer adenylated salicylate to holo-EntB.
CC       {ECO:0000269|PubMed:10688898, ECO:0000269|PubMed:16567620,
CC       ECO:0000269|PubMed:16632253, ECO:0000269|PubMed:19699210,
CC       ECO:0000269|PubMed:19852513, ECO:0000269|PubMed:20359185,
CC       ECO:0000269|PubMed:20845982, ECO:0000269|PubMed:21166461,
CC       ECO:0000269|PubMed:2531000, ECO:0000269|PubMed:9214294}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3 2,3-dihydroxybenzoate + 3 L-serine + 6 ATP = enterobactin +
CC         6 AMP + 6 diphosphate + 4 H(+); Xref=Rhea:RHEA:30571,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:33384, ChEBI:CHEBI:36654, ChEBI:CHEBI:77805,
CC         ChEBI:CHEBI:456215; EC=6.3.2.14;
CC         Evidence={ECO:0000269|PubMed:10688898, ECO:0000269|PubMed:16567620,
CC         ECO:0000269|PubMed:19852513, ECO:0000269|PubMed:20359185,
CC         ECO:0000269|PubMed:20845982, ECO:0000269|PubMed:2531000,
CC         ECO:0000269|PubMed:9214294};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2,3-dihydroxybenzoate + holo-[ACP] + ATP = 2,3-
CC         dihydroxybenzoyl-[ACP] + AMP + diphosphate; Xref=Rhea:RHEA:61652,
CC         Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:19024, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:36654, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:90610, ChEBI:CHEBI:456215; EC=6.2.1.71;
CC         Evidence={ECO:0000269|PubMed:10688898, ECO:0000269|PubMed:16567620,
CC         ECO:0000269|PubMed:19852513, ECO:0000269|PubMed:20359185,
CC         ECO:0000269|PubMed:20845982, ECO:0000269|PubMed:2531000};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2,3-dihydroxybenzoyl-5'-AMP + holo-[ACP] = 2,3-
CC         dihydroxybenzoyl-[ACP] + AMP + H(+); Xref=Rhea:RHEA:48604, Rhea:RHEA-
CC         COMP:9685, Rhea:RHEA-COMP:19024, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57417, ChEBI:CHEBI:64479, ChEBI:CHEBI:90610,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:10688898,
CC         ECO:0000269|PubMed:16567620, ECO:0000269|PubMed:19852513,
CC         ECO:0000269|PubMed:20359185, ECO:0000269|PubMed:20845982,
CC         ECO:0000269|PubMed:9214294, ECO:0000269|PubMed:9485415};
CC   -!- ACTIVITY REGULATION: Inhibited by the adenylate analogs, 5'-O-[N-
CC       (salicyl)sulfamoyl]adenosine (Sal-AMS) and 5'-O-[N-(2,3-
CC       dihydroxybenzoyl)sulfamoyl]adenosine (DHB-AMS). Adenylation of 2,3-
CC       dihydroxybenzoate (DHB) is enhanced by a protein-protein interaction
CC       between the EntA and EntE. {ECO:0000269|PubMed:20359185,
CC       ECO:0000269|PubMed:21166461}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.4 uM for holo-EntB (at pH 8.8 and 37 degrees Celsius)
CC         {ECO:0000269|PubMed:9214294};
CC         KM=0.5 uM for holo-EntB {ECO:0000269|PubMed:16567620};
CC         KM=2.5 uM for DHB (at pH 7.8 and 25 degrees Celsius)
CC         {ECO:0000269|PubMed:20359185};
CC         KM=2.7 uM for DHB {ECO:0000269|PubMed:2531000};
CC         KM=2.9 uM for DHB {ECO:0000269|PubMed:20845982};
CC         KM=2.9 uM for holo-EntB (at pH 7.8 and 25 degrees Celsius)
CC         {ECO:0000269|PubMed:20359185};
CC         KM=23.3 uM for holo-EntB (at pH 7.5 and 37 degrees Celsius)
CC         {ECO:0000269|PubMed:16632253};
CC         KM=70 uM for 3-hydroxybenzoate (at pH 7.8 and 25 degrees Celsius)
CC         {ECO:0000269|PubMed:20359185};
CC         KM=70 uM for salicylate (at pH 7.8 and 25 degrees Celsius)
CC         {ECO:0000269|PubMed:20359185};
CC         KM=400 uM for 5,5-diadenosine tetraphosphate
CC         {ECO:0000269|PubMed:19852513};
CC         KM=430 uM for ATP (at pH 7.8 and 25 degrees Celsius)
CC         {ECO:0000269|PubMed:20359185};
CC         KM=1200 uM for ATP {ECO:0000269|PubMed:2531000};
CC         KM=3100 uM for 4-aminosalicylate (at pH 7.8 and 25 degrees Celsius)
CC         {ECO:0000269|PubMed:20359185};
CC         KM=34.2 mM for D-pantetheine (at pH 7.8 and 25 degrees Celsius)
CC         {ECO:0000269|PubMed:20359185};
CC         Vmax=3168.2 pmol/min/mg enzyme {ECO:0000269|PubMed:20845982};
CC         Note=kcat is 0.3 sec(-1) for 2,3-dihydroxybenzoate-AMP ligase
CC         activity with 3-hydroxybenzoate as substrate (at pH 7.8 and 25
CC         degrees Celsius). kcat is 0.8 sec(-1) for 2,3-dihydroxybenzoate-AMP
CC         ligase activity with salicylate as substrate (at pH 7.8 and 25
CC         degrees Celsius). kcat is 0.9 sec(-1) for
CC         S-dihydroxybenzoyltransferase activity with D-pantetheine as
CC         substrate (at pH 7.8 and 25 degrees Celsius). kcat is 2.8 sec(-1) for
CC         2,3-dihydroxybenzoate-AMP ligase activity with ATP and DHB as
CC         substrates (at pH 7.8 and 25 degrees Celsius). kcat is 2.8 sec(-1)
CC         for S-dihydroxybenzoyltransferase activity with holo-EntB as
CC         substrate (at pH 7.8 and 25 degrees Celsius). kcat is 4.4 sec(-1) for
CC         2,3-dihydroxybenzoate-AMP ligase activity with 4-aminosalicylate as
CC         substrate (at pH 7.8 and 25 degrees Celsius). kcat is 5.94 sec(-1)
CC         for S-dihydroxybenzoyltransferase activity with holo-EntB as
CC         substrate (at pH 7.8 and 25 degrees Celsius). kcat is 100 min(-1) for
CC         S-dihydroxybenzoyltransferase activity with holo-EntB as substrate
CC         (at pH 8.8 and 37 degrees Celsius). kcat is 140 min(-1) for
CC         S-dihydroxybenzoyltransferase activity with holo-EntB as substrate.
CC         {ECO:0000269|PubMed:16567620, ECO:0000269|PubMed:16632253,
CC         ECO:0000269|PubMed:20359185, ECO:0000269|PubMed:9214294};
CC   -!- PATHWAY: Siderophore biosynthesis; enterobactin biosynthesis.
CC       {ECO:0000305|PubMed:9485415}.
CC   -!- SUBUNIT: Proteins EntB, EntD, EntE, and EntF form a multienzyme complex
CC       called enterobactin synthase. Monomer. EntA and EntE interact together.
CC       {ECO:0000269|PubMed:21166461, ECO:0000269|PubMed:22365602,
CC       ECO:0000269|PubMed:23897471, ECO:0000269|PubMed:2531000,
CC       ECO:0000269|PubMed:9485415}.
CC   -!- INTERACTION:
CC       P10378; P15047: entA; NbExp=5; IntAct=EBI-550322, EBI-1118936;
CC       P10378; P0ADI4: entB; NbExp=3; IntAct=EBI-550322, EBI-547993;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10692387}.
CC   -!- INDUCTION: Under conditions of iron deficiency and by the fur protein.
CC       {ECO:0000269|PubMed:2521621, ECO:0000269|PubMed:6227609}.
CC   -!- MISCELLANEOUS: In the absence of holo-EntB, EntE can transfer the
CC       adenylate moiety of the 2,3-dihydroxybenzoyl-AMP intermediate to ATP,
CC       generating the stress signaling molecule Ap4A involved in the
CC       regulation of cell division during oxidative stress, and releasing 2,3-
CC       dihydroxybenzoate. It seems that the expression of EntE during iron
CC       starvation produces Ap(4)A to slow growth until intracellular iron
CC       stores can be restored. {ECO:0000269|PubMed:19852513}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       EntE subfamily. {ECO:0000305}.
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DR   EMBL; X15058; CAA33158.1; -; Genomic_DNA.
DR   EMBL; U82598; AAB40794.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73695.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76349.1; -; Genomic_DNA.
DR   EMBL; M24148; AAA16101.1; -; Unassigned_DNA.
DR   EMBL; M36700; AAA18492.1; -; Genomic_DNA.
DR   PIR; H64792; SYECEB.
DR   RefSeq; NP_415126.1; NC_000913.3.
DR   RefSeq; WP_000026812.1; NZ_CP009789.1.
DR   PDB; 3RG2; X-ray; 3.10 A; A/B/C/D/E/F/G/H/I/J=1-536.
DR   PDB; 4IZ6; X-ray; 2.40 A; A/B=1-536.
DR   PDB; 6IYK; X-ray; 2.45 A; A/B=1-536.
DR   PDB; 6IYL; X-ray; 2.56 A; A/B=1-536.
DR   PDB; 8K5S; X-ray; 2.65 A; A/B=1-536.
DR   PDB; 8K5T; X-ray; 2.80 A; A/B=1-536.
DR   AlphaFoldDB; P10378; -.
DR   SMR; P10378; -.
DR   BioGRID; 4259905; 326.
DR   BioGRID; 851747; 5.
DR   ComplexPortal; CPX-5747; entAE 2,3-dihydroxybenzoate-AMP ligase complex.
DR   ComplexPortal; CPX-5748; entBE aryl carrier complex.
DR   DIP; DIP-9515N; -.
DR   FunCoup; P10378; 50.
DR   IntAct; P10378; 14.
DR   STRING; 511145.b0594; -.
DR   BindingDB; P10378; -.
DR   ChEMBL; CHEMBL4856; -.
DR   jPOST; P10378; -.
DR   PaxDb; 511145-b0594; -.
DR   EnsemblBacteria; AAC73695; AAC73695; b0594.
DR   GeneID; 947426; -.
DR   KEGG; ecj:JW0586; -.
DR   KEGG; eco:b0594; -.
DR   KEGG; ecoc:C3026_02965; -.
DR   PATRIC; fig|1411691.4.peg.1675; -.
DR   EchoBASE; EB0259; -.
DR   eggNOG; COG1021; Bacteria.
DR   HOGENOM; CLU_000022_59_7_6; -.
DR   InParanoid; P10378; -.
DR   OMA; TFRGYYR; -.
DR   OrthoDB; 9803968at2; -.
DR   PhylomeDB; P10378; -.
DR   BioCyc; EcoCyc:ENTE-MONOMER; -.
DR   BioCyc; MetaCyc:ENTE-MONOMER; -.
DR   BRENDA; 6.2.1.71; 2026.
DR   BRENDA; 6.3.2.14; 2026.
DR   UniPathway; UPA00017; -.
DR   PRO; PR:P10378; -.
DR   Proteomes; UP000000625; Chromosome.
DR   AbasyAtlas; P10378; -.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0016020; C:membrane; EXP:UniProtKB.
DR   GO; GO:0008668; F:2,3-dihydroxybenzoate--[aryl-carrier protein] ligase activity; IDA:EcoCyc.
DR   GO; GO:0047527; F:2,3-dihydroxybenzoate-serine ligase activity; IDA:UniProtKB.
DR   GO; GO:0009239; P:enterobactin biosynthetic process; IDA:ComplexPortal.
DR   CDD; cd05920; 23DHB-AMP_lg; 1.
DR   FunFam; 3.30.300.30:FF:000021; Enterobactin synthase component E; 1.
DR   FunFam; 3.40.50.12780:FF:000031; Enterobactin synthase component E; 1.
DR   FunFam; 2.30.38.10:FF:000003; Vibriobactin-specific 2,3-dihydroxybenzoate-AMP ligase; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR045851; AMP-b_sf.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_synth/lig_dom.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR050237; ATP-dep_AMP-bd_enzyme.
DR   InterPro; IPR011963; DHB_AMP_lig.
DR   NCBIfam; TIGR02275; DHB_AMP_lig; 1.
DR   NCBIfam; NF008192; PRK10946.1; 1.
DR   PANTHER; PTHR43767; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR   PANTHER; PTHR43767:SF1; NONRIBOSOMAL PEPTIDE SYNTHASE PES1 (EUROFUNG)-RELATED; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PDBsum; 3RG2; -.
DR   PDBsum; 4IZ6; -.
DR   PDBsum; 6IYK; -.
DR   PDBsum; 6IYL; -.
DR   PDBsum; 8K5S; -.
DR   PDBsum; 8K5T; -.
PE   1: Evidence at protein level;
KW   3D-structure; Acyltransferase; ATP-binding; Enterobactin biosynthesis;
KW   Ligase; Membrane; Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..536
FT                   /note="Enterobactin synthase component E"
FT                   /id="PRO_0000193075"
FT   REGION          438..439
FT                   /note="Phosphopantetheine binding"
FT                   /evidence="ECO:0000269|PubMed:22365602,
FT                   ECO:0000269|PubMed:23897471"
FT   BINDING         235
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:22365602"
FT   BINDING         240
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:23897471"
FT   BINDING         309
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:22365602,
FT                   ECO:0000269|PubMed:23897471"
FT   BINDING         331
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:22365602,
FT                   ECO:0000269|PubMed:23897471"
FT   BINDING         335
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:22365602"
FT   BINDING         415
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:22365602,
FT                   ECO:0000269|PubMed:23897471"
FT   BINDING         432
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:23897471"
FT   BINDING         441
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:23897471"
FT   MUTAGEN         437
FT                   /note="R->D: Catalyzes the adenylation reaction with 10%
FT                   reduction of activity compared to the wild-type. 3%
FT                   reduction of activity compared to the wild-type; when
FT                   associated with D-473."
FT                   /evidence="ECO:0000269|PubMed:16632253"
FT   MUTAGEN         473
FT                   /note="K->D: Catalyzes the adenylation reaction with same
FT                   activity as the wild-type. 3% reduction of activity
FT                   compared to the wild-type; when associated with D-437."
FT                   /evidence="ECO:0000269|PubMed:16632253"
FT   MUTAGEN         494
FT                   /note="R->D: Catalyzes the adenylation reaction with same
FT                   activity as the wild-type."
FT                   /evidence="ECO:0000269|PubMed:16632253"
FT   CONFLICT        369..378
FT                   /note="DAEGNPLPQG -> ECRRKSTAAR (in Ref. 1; CAA33158)"
FT                   /evidence="ECO:0000305"
FT   HELIX           7..9
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   HELIX           10..18
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   HELIX           29..32
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   TURN            33..36
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   STRAND          39..44
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   STRAND          47..50
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   HELIX           51..67
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   STRAND          75..79
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   HELIX           84..96
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   STRAND          99..103
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   HELIX           109..119
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   STRAND          122..127
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   HELIX           131..133
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   STRAND          134..136
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   HELIX           137..145
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   TURN            146..148
FT                   /evidence="ECO:0007829|PDB:8K5T"
FT   STRAND          151..155
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   HELIX           163..168
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   HELIX           178..180
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   STRAND          183..189
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   STRAND          193..196
FT                   /evidence="ECO:0007829|PDB:6IYK"
FT   STRAND          199..203
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   HELIX           204..218
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   STRAND          225..228
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   HELIX           235..239
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   HELIX           242..249
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   STRAND          252..255
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   HELIX           261..271
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   STRAND          275..278
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   HELIX           280..291
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   HELIX           296..299
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   STRAND          304..310
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   HELIX           311..313
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   HELIX           314..323
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   STRAND          326..334
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   STRAND          337..341
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   HELIX           348..353
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   STRAND          357..360
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   STRAND          364..368
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   STRAND          370..372
FT                   /evidence="ECO:0007829|PDB:8K5T"
FT   STRAND          380..386
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   STRAND          388..390
FT                   /evidence="ECO:0007829|PDB:8K5T"
FT   HELIX           398..404
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   STRAND          411..419
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   STRAND          425..430
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   STRAND          432..437
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   STRAND          440..443
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   HELIX           444..451
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   STRAND          457..467
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   TURN            468..470
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   STRAND          471..482
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   HELIX           486..494
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   TURN            495..497
FT                   /evidence="ECO:0007829|PDB:3RG2"
FT   HELIX           500..502
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   STRAND          505..509
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   STRAND          519..521
FT                   /evidence="ECO:0007829|PDB:4IZ6"
FT   HELIX           523..531
FT                   /evidence="ECO:0007829|PDB:4IZ6"
SQ   SEQUENCE   536 AA;  59112 MW;  F818942DFDD8DC99 CRC64;
     MSIPFTRWPE EFARRYREKG YWQDLPLTDI LTRHAASDSI AVIDGERQLS YRELNQAADN
     LACSLRRQGI KPGETALVQL GNVAELYITF FALLKLGVAP VLALFSHQRS ELNAYASQIE
     PALLIADRQH ALFSGDDFLN TFVTEHSSIR VVQLLNDSGE HNLQDAINHP AEDFTATPSP
     ADEVAYFQLS GGTTGTPKLI PRTHNDYYYS VRRSVEICQF TQQTRYLCAI PAAHNYAMSS
     PGSLGVFLAG GTVVLAADPS ATLCFPLIEK HQVNVTALVP PAVSLWLQAL IEGESRAQLA
     SLKLLQVGGA RLSATLAARI PAEIGCQLQQ VFGMAEGLVN YTRLDDSAEK IIHTQGYPMC
     PDDEVWVADA EGNPLPQGEV GRLMTRGPYT FRGYYKSPQH NASAFDANGF YCSGDLISID
     PEGYITVQGR EKDQINRGGE KIAAEEIENL LLRHPAVIYA ALVSMEDELM GEKSCAYLVV
     KEPLRAVQVR RFLREQGIAE FKLPDRVECV DSLPLTAVGK VDKKQLRQWL ASRASA
//