ID   ENTB_ECOLI              Reviewed;         285 AA.
AC   P0ADI4; P15048; Q2MBK6;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   02-SEP-2026, entry version 146.
DE   RecName: Full=Enterobactin synthase component B {ECO:0000303|PubMed:2531000};
DE            EC=6.3.2.14 {ECO:0000269|PubMed:16632253, ECO:0000269|PubMed:2139796, ECO:0000269|PubMed:9214294, ECO:0000269|PubMed:9485415};
DE   AltName: Full=Enterobactin biosynthesis bifunctional protein EntB {ECO:0000303|PubMed:9214294};
DE   AltName: Full=Enterochelin synthase B {ECO:0000303|PubMed:2531000};
DE   Includes:
DE     RecName: Full=Isochorismatase {ECO:0000303|PubMed:2139796};
DE              EC=3.3.2.1 {ECO:0000269|PubMed:16632253, ECO:0000269|PubMed:2139796, ECO:0000269|PubMed:9214294, ECO:0000269|PubMed:9485415};
DE     AltName: Full=2,3-dihydro-2,3-dihydroxybenzoate synthase {ECO:0000303|PubMed:2139796};
DE     AltName: Full=Isochorismate lyase {ECO:0000303|PubMed:2139796};
DE   Includes:
DE     RecName: Full=Aryl carrier protein {ECO:0000303|PubMed:9214294};
DE              Short=ArCP {ECO:0000303|PubMed:9214294};
GN   Name=entB {ECO:0000303|PubMed:2521621};
GN   Synonyms=entG {ECO:0000303|PubMed:2172214};
GN   OrderedLocusNames=b0595, JW0587;
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], AND 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   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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   [3]
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   [4]
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   [5]
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   [6]
RP   PROTEIN SEQUENCE OF 2-13, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, ACTIVITY REGULATION, AND SUBUNIT.
RX   PubMed=2139796; DOI=10.1021/bi00458a013;
RA   Rusnak F., Liu J., Quinn N., Berchtold G.A., Walsh C.T.;
RT   "Subcloning of the enterobactin biosynthetic gene entB: expression,
RT   purification, characterization, and substrate specificity of
RT   isochorismatase.";
RL   Biochemistry 29:1425-1435(1990).
RN   [7]
RP   FUNCTION.
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   [8]
RP   FUNCTION.
RX   PubMed=2172214; DOI=10.1128/jb.172.11.6403-6410.1990;
RA   Staab J.F., Earhart C.F.;
RT   "EntG activity of Escherichia coli enterobactin synthetase.";
RL   J. Bacteriol. 172:6403-6410(1990).
RN   [9]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
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   [10]
RP   FUNCTION, CATALYTIC ACTIVITY, 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   [11]
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   [12]
RP   MUTAGENESIS OF GLY-242 AND ASP-244.
RX   PubMed=16925399; DOI=10.1021/ja063238h;
RA   Lai J.R., Fischbach M.A., Liu D.R., Walsh C.T.;
RT   "Localized protein interaction surfaces on the EntB carrier protein
RT   revealed by combinatorial mutagenesis and selection.";
RL   J. Am. Chem. Soc. 128:11002-11003(2006).
RN   [13]
RP   FUNCTION, AND MUTAGENESIS OF MET-249; PHE-264; ALA-268 AND LYS-269.
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   [14]
RP   FUNCTION.
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   [15]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=22096151; DOI=10.1099/mic.0.054361-0;
RA   Orchard S.S., Rostron J.E., Segall A.M.;
RT   "Escherichia coli enterobactin synthesis and uptake mutants are
RT   hypersensitive to an antimicrobial peptide that limits the availability of
RT   iron in addition to blocking Holliday junction resolution.";
RL   Microbiology 158:547-559(2012).
RN   [16]
RP   INTERACTION WITH ENTC.
RX   PubMed=35952947; DOI=10.1016/j.biochi.2022.07.018;
RA   Ouellette S., Pakarian P., Bin X., Pawelek P.D.;
RT   "Evidence of an intracellular interaction between the Escherichia coli
RT   enzymes EntC and EntB and identification of a potential electrostatic
RT   channeling surface.";
RL   Biochimie 202:159-165(2022).
RN   [17] {ECO:0007744|PDB:2FQ1}
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH MAGNESIUM ION,
RP   FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-240; ASP-263 AND PHE-264,
RP   COFACTOR, AND SUBUNIT.
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   [18] {ECO:0007744|PDB:3RG2}
RP   X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 209-285 IN A CHIMERIC CONSTRUCT
RP   WITH ENTE IN COMPLEX WITH PHOSPHOPANTETHEINE, SUBUNIT, AND
RP   PHOSPHOPANTETHEINYLATION AT SER-245.
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).
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(3+) atoms. EntB is a
CC       bifunctional protein that serves as an isochorismate lyase and an aryl
CC       carrier protein (ArCP). Catalyzes the conversion of isochorismate to
CC       2,3-dihydro-2,3-dihydroxybenzoate (2,3-diDHB), the precursor of 2,3-
CC       dihydroxybenzoate (DHB). In the enterobactin assembly, EntB functions
CC       as an aryl carrier protein phosphopantetheinylated near the C terminus
CC       by EntD to yield holo-EntB, which is then acylated by EntE with 2,3-
CC       dihydroxybenzoyl-AMP to form DHB-holo-EntB. Then this product will
CC       serve in the formation of the amide bond between 2,3-dihydroxybenzoate
CC       (DHB) and L-serine. {ECO:0000269|PubMed:16567620,
CC       ECO:0000269|PubMed:16632253, ECO:0000269|PubMed:19699210,
CC       ECO:0000269|PubMed:2139796, ECO:0000269|PubMed:2172214,
CC       ECO:0000269|PubMed:2531000, ECO:0000269|PubMed:9214294,
CC       ECO:0000269|PubMed:9485415}.
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:16632253, ECO:0000269|PubMed:2139796,
CC         ECO:0000269|PubMed:9214294, ECO:0000269|PubMed:9485415};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=isochorismate + H2O = (2S,3S)-2,3-dihydroxy-2,3-
CC         dihydrobenzoate + pyruvate; Xref=Rhea:RHEA:11112, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:29780, ChEBI:CHEBI:58764; EC=3.3.2.1;
CC         Evidence={ECO:0000269|PubMed:16632253, ECO:0000269|PubMed:2139796,
CC         ECO:0000269|PubMed:9214294, ECO:0000269|PubMed:9485415};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:16632253};
CC   -!- ACTIVITY REGULATION: Inhibited by 3-[(carboxyethenyl)oxy]-6-hydroxy-1-
CC       benzoic acid and 3-[(carboxyethenyl)oxy]benzoic acid.
CC       {ECO:0000269|PubMed:2139796}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=14.7 uM for isochorismate (at pH 7 and 37 degrees Celsius)
CC         {ECO:0000269|PubMed:2139796};
CC         KM=23 uM for 4,5-dihydroisochorismate (at pH 7 and 37 degrees
CC         Celsius) {ECO:0000269|PubMed:2139796};
CC         KM=86 uM for 3-[(carboxyethenyl)oxy]-1-cyclohexene-1-carboxylic acid
CC         (at pH 7 and 37 degrees Celsius) {ECO:0000269|PubMed:2139796};
CC         KM=120 uM for
CC         3-[(1-carboxylatoethenyl)oxy]-cyclohepta-1,6-diene-1-carboxylate (at
CC         pH 7 and 37 degrees Celsius) {ECO:0000269|PubMed:2139796};
CC         KM=280 uM for cis-3-[(carboxyethenyl)oxy]-4-cyclohexene-1-carboxylic
CC         acid (at pH 7 and 37 degrees Celsius) {ECO:0000269|PubMed:2139796};
CC         Vmax=18.5 umol/min/mg enzyme (at pH 7 and 37 degrees Celsius)
CC         {ECO:0000269|PubMed:2139796};
CC         Note=kcat is 600 min(-1) for isochorismatase activity with
CC         isochorismate as substrate (at pH 7 and 37 degrees Celsius). kcat is
CC         540 min(-1) for isochorismatase activity with
CC         3-[(1-carboxylatoethenyl)oxy]-cyclohepta-1,6-diene-1-carboxylate as
CC         substrate (at pH 7 and 37 degrees Celsius). kcat is 310 min(-1) for
CC         isochorismatase activity with 4,5-dihydroisochorismate as substrate
CC         (at pH 7 and 37 degrees Celsius). {ECO:0000269|PubMed:2139796};
CC       pH dependence:
CC         Optimum pH is between 6.5 and 7.5. At pH 5.5, EntB retains 50% of
CC         isochorismatase activity. {ECO:0000269|PubMed:2139796};
CC   -!- PATHWAY: Siderophore biosynthesis; enterobactin biosynthesis.
CC       {ECO:0000305|PubMed:9214294}.
CC   -!- SUBUNIT: Proteins EntB, EntD, EntE, and EntF form a multienzyme complex
CC       called enterobactin synthase. Homodimer (PubMed:16632253). Also forms a
CC       specific pairwise interaction with EntC; this interaction likely
CC       facilitates substrate channeling to connect the EntB and EntC active
CC       sites (PubMed:35952947). {ECO:0000269|PubMed:16632253,
CC       ECO:0000269|PubMed:2139796, ECO:0000269|PubMed:22365602,
CC       ECO:0000269|PubMed:35952947, ECO:0000269|PubMed:9485415}.
CC   -!- INTERACTION:
CC       P0ADI4; P0ADI4: entB; NbExp=3; IntAct=EBI-547993, EBI-547993;
CC       P0ADI4; P10378: entE; NbExp=3; IntAct=EBI-547993, EBI-550322;
CC       P0ADI4; P0A8Y8: entH; NbExp=3; IntAct=EBI-547993, EBI-1118982;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10692387}.
CC   -!- INDUCTION: Under conditions of iron deficiency and by the fur protein.
CC       {ECO:0000269|PubMed:2521621}.
CC   -!- PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine
CC       of apo-EntB by EntD. Holo-EntB so formed is then acylated with 2,3-
CC       dihydroxybenzoate in a reaction catalyzed by EntE.
CC       {ECO:0000269|PubMed:22365602}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are hypersensitive to the
CC       antimicrobial peptide wrwycr. {ECO:0000269|PubMed:22096151}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the isochorismatase
CC       family. {ECO:0000305}.
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DR   EMBL; M24148; AAA16102.1; -; Unassigned_DNA.
DR   EMBL; M24143; AAA76835.1; -; Genomic_DNA.
DR   EMBL; U82598; AAB40795.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73696.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76350.1; -; Genomic_DNA.
DR   PIR; C91904; YXECIC.
DR   RefSeq; NP_415127.1; NC_000913.3.
DR   RefSeq; WP_001007138.1; NZ_CP009789.1.
DR   PDB; 2FQ1; X-ray; 2.30 A; A/B=1-285.
DR   PDB; 3RG2; X-ray; 3.10 A; A/B/C/D/E/F/G/H/I/J=209-285.
DR   PDB; 4IZ6; X-ray; 2.40 A; A/B=211-285.
DR   AlphaFoldDB; P0ADI4; -.
DR   SMR; P0ADI4; -.
DR   BioGRID; 4260905; 218.
DR   BioGRID; 850538; 5.
DR   ComplexPortal; CPX-5748; entBE aryl carrier complex.
DR   DIP; DIP-9512N; -.
DR   FunCoup; P0ADI4; 410.
DR   IntAct; P0ADI4; 29.
DR   STRING; 511145.b0595; -.
DR   jPOST; P0ADI4; -.
DR   PaxDb; 511145-b0595; -.
DR   EnsemblBacteria; AAC73696; AAC73696; b0595.
DR   GeneID; 946178; -.
DR   KEGG; ecj:JW0587; -.
DR   KEGG; eco:b0595; -.
DR   KEGG; ecoc:C3026_02970; -.
DR   PATRIC; fig|1411691.4.peg.1674; -.
DR   EchoBASE; EB0256; -.
DR   eggNOG; COG1535; Bacteria.
DR   eggNOG; COG3433; Bacteria.
DR   HOGENOM; CLU_068979_2_0_6; -.
DR   InParanoid; P0ADI4; -.
DR   OMA; RDIKPFF; -.
DR   OrthoDB; 5794853at2; -.
DR   PhylomeDB; P0ADI4; -.
DR   BioCyc; EcoCyc:ENTB-MONOMER; -.
DR   BioCyc; MetaCyc:ENTB-MONOMER; -.
DR   BRENDA; 3.3.2.1; 2026.
DR   BRENDA; 6.3.2.14; 2026.
DR   SABIO-RK; P0ADI4; -.
DR   UniPathway; UPA00017; -.
DR   EvolutionaryTrace; P0ADI4; -.
DR   PRO; PR:P0ADI4; -.
DR   Proteomes; UP000000625; Chromosome.
DR   AbasyAtlas; P0ADI4; -.
DR   GO; GO:0005737; C:cytoplasm; EXP:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR   GO; GO:0047527; F:2,3-dihydroxybenzoate-serine ligase activity; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0008908; F:isochorismatase activity; IDA:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR   GO; GO:0031177; F:phosphopantetheine binding; IDA:UniProtKB.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IMP:EcoliWiki.
DR   GO; GO:0009239; P:enterobactin biosynthetic process; IDA:UniProtKB.
DR   CDD; cd01013; isochorismatase; 1.
DR   FunFam; 1.10.1200.10:FF:000009; Isochorismatase; 1.
DR   FunFam; 3.40.50.850:FF:000002; Vibriobactin-specific isochorismatase; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.50.850; Isochorismatase-like; 1.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR016291; Isochorismatase.
DR   InterPro; IPR000868; Isochorismatase-like_dom.
DR   InterPro; IPR050272; Isochorismatase-like_hydrls.
DR   InterPro; IPR036380; Isochorismatase-like_sf.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   PANTHER; PTHR43540:SF3; ENTEROBACTIN SYNTHASE COMPONENT B; 1.
DR   PANTHER; PTHR43540; PEROXYUREIDOACRYLATE/UREIDOACRYLATE AMIDOHYDROLASE-RELATED; 1.
DR   Pfam; PF00857; Isochorismatase; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   PIRSF; PIRSF001111; Isochorismatase; 1.
DR   PRINTS; PR01398; ISCHRISMTASE.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52499; Isochorismatase-like hydrolases; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PDBsum; 2FQ1; -.
DR   PDBsum; 3RG2; -.
DR   PDBsum; 4IZ6; -.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing;
KW   Enterobactin biosynthesis; Hydrolase; Ligase; Magnesium; Metal-binding;
KW   Multifunctional enzyme; Phosphopantetheine; Phosphoprotein;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2139796"
FT   CHAIN           2..285
FT                   /note="Enterobactin synthase component B"
FT                   /id="PRO_0000201822"
FT   DOMAIN          209..284
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          2..213
FT                   /note="Isochorismatase"
FT                   /evidence="ECO:0000303|PubMed:9214294"
FT   BINDING         227
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|PubMed:16632253,
FT                   ECO:0007744|PDB:2FQ1"
FT   BINDING         242
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|PubMed:16632253,
FT                   ECO:0007744|PDB:2FQ1"
FT   BINDING         244
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|PubMed:16632253,
FT                   ECO:0007744|PDB:2FQ1"
FT   MOD_RES         245
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000269|PubMed:22365602,
FT                   ECO:0007744|PDB:3RG2"
FT   MUTAGEN         240
FT                   /note="D->R: The catalytic efficiency slightly increases,
FT                   but a 8-fold decrease of the affinity for the
FT                   S-dihydroxybenzoyltransferase EntE is observed."
FT                   /evidence="ECO:0000269|PubMed:16632253"
FT   MUTAGEN         242
FT                   /note="G->A: Not efficiently phosphopantetheinylated by
FT                   EntD."
FT                   /evidence="ECO:0000269|PubMed:16925399"
FT   MUTAGEN         244
FT                   /note="D->A: Efficiently phosphopantetheinylated by EntD."
FT                   /evidence="ECO:0000269|PubMed:16925399"
FT   MUTAGEN         244
FT                   /note="D->R: Not efficiently phosphopantetheinylated by
FT                   EntD."
FT                   /evidence="ECO:0000269|PubMed:16925399"
FT   MUTAGEN         249
FT                   /note="M->A: Unable to recognize EntE and EntF. Exhibits a
FT                   decrease in the enterobactin production compared to the
FT                   wild-type. Still able to be phosphopantetheinylated."
FT                   /evidence="ECO:0000269|PubMed:16567620"
FT   MUTAGEN         263
FT                   /note="D->R: The catalytic efficiency is the same as the
FT                   wild-type, but a 3-fold decrease of the affinity for the
FT                   S-dihydroxybenzoyltransferase EntE is observed."
FT                   /evidence="ECO:0000269|PubMed:16632253"
FT   MUTAGEN         264
FT                   /note="F->E: The affinity for EntE and catalytic efficiency
FT                   of the S-dihydroxybenzoyltransferase EntE are below that of
FT                   the wild-type."
FT                   /evidence="ECO:0000269|PubMed:16567620,
FT                   ECO:0000269|PubMed:16632253"
FT   MUTAGEN         268
FT                   /note="A->Q: Unable to recognize EntE and EntF. Exhibits a
FT                   decrease in the enterobactin production compared to the
FT                   wild-type. Still able to be phosphopantetheinylated."
FT                   /evidence="ECO:0000269|PubMed:16567620"
FT   MUTAGEN         269
FT                   /note="K->A: Behaves similarly to the wild-type."
FT                   /evidence="ECO:0000269|PubMed:16567620"
FT   HELIX           10..12
FT                   /evidence="ECO:0007829|PDB:2FQ1"
FT   HELIX           14..16
FT                   /evidence="ECO:0007829|PDB:2FQ1"
FT   HELIX           18..20
FT                   /evidence="ECO:0007829|PDB:2FQ1"
FT   HELIX           28..30
FT                   /evidence="ECO:0007829|PDB:2FQ1"
FT   STRAND          31..36
FT                   /evidence="ECO:0007829|PDB:2FQ1"
FT   HELIX           40..43
FT                   /evidence="ECO:0007829|PDB:2FQ1"
FT   HELIX           51..69
FT                   /evidence="ECO:0007829|PDB:2FQ1"
FT   STRAND          74..78
FT                   /evidence="ECO:0007829|PDB:2FQ1"
FT   HELIX           85..88
FT                   /evidence="ECO:0007829|PDB:2FQ1"
FT   HELIX           91..95
FT                   /evidence="ECO:0007829|PDB:2FQ1"
FT   HELIX           98..101
FT                   /evidence="ECO:0007829|PDB:2FQ1"
FT   HELIX           103..105
FT                   /evidence="ECO:0007829|PDB:2FQ1"
FT   HELIX           110..112
FT                   /evidence="ECO:0007829|PDB:2FQ1"
FT   STRAND          118..122
FT                   /evidence="ECO:0007829|PDB:2FQ1"
FT   STRAND          125..127
FT                   /evidence="ECO:0007829|PDB:2FQ1"
FT   TURN            128..131
FT                   /evidence="ECO:0007829|PDB:2FQ1"
FT   HELIX           134..140
FT                   /evidence="ECO:0007829|PDB:2FQ1"
FT   STRAND          145..151
FT                   /evidence="ECO:0007829|PDB:2FQ1"
FT   HELIX           153..157
FT                   /evidence="ECO:0007829|PDB:2FQ1"
FT   HELIX           158..166
FT                   /evidence="ECO:0007829|PDB:2FQ1"
FT   STRAND          170..179
FT                   /evidence="ECO:0007829|PDB:2FQ1"
FT   HELIX           183..196
FT                   /evidence="ECO:0007829|PDB:2FQ1"
FT   STRAND          199..201
FT                   /evidence="ECO:0007829|PDB:2FQ1"
FT   HELIX           203..206
FT                   /evidence="ECO:0007829|PDB:2FQ1"
FT   STRAND          207..209
FT                   /evidence="ECO:0007829|PDB:2FQ1"
FT   HELIX           210..212
FT                   /evidence="ECO:0007829|PDB:2FQ1"
FT   HELIX           215..222
FT                   /evidence="ECO:0007829|PDB:2FQ1"
FT   HELIX           223..225
FT                   /evidence="ECO:0007829|PDB:2FQ1"
FT   HELIX           231..233
FT                   /evidence="ECO:0007829|PDB:2FQ1"
FT   HELIX           239..241
FT                   /evidence="ECO:0007829|PDB:2FQ1"
FT   HELIX           247..255
FT                   /evidence="ECO:0007829|PDB:2FQ1"
FT   TURN            256..258
FT                   /evidence="ECO:0007829|PDB:2FQ1"
FT   HELIX           264..268
FT                   /evidence="ECO:0007829|PDB:2FQ1"
FT   HELIX           273..281
FT                   /evidence="ECO:0007829|PDB:2FQ1"
SQ   SEQUENCE   285 AA;  32554 MW;  E98C62D5ED23BAB1 CRC64;
     MAIPKLQAYA LPESHDIPQN KVDWAFEPQR AALLIHDMQD YFVSFWGENC PMMEQVIANI
     AALRDYCKQH NIPVYYTAQP KEQSDEDRAL LNDMWGPGLT RSPEQQKVVD RLTPDADDTV
     LVKWRYSAFH RSPLEQMLKE SGRNQLIITG VYAHIGCMTT ATDAFMRDIK PFMVADALAD
     FSRDEHLMSL KYVAGRSGRV VMTEELLPAP IPASKAALRE VILPLLDESD EPFDDDNLID
     YGLDSVRMMA LAARWRKVHG DIDFVMLAKN PTIDAWWKLL SREVK
//