ENTB_ECOLI
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 03-AUG-2022, entry version 132.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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 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 [17]
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(2+) 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 + 6 ATP + 3 L-serine = 6 AMP + 6
CC diphosphate + enterobactin + 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=H2O + isochorismate = (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 3-[(1-carboxylatoethenyl)oxy]-cyclohepta-1,6-diene-1-
CC carboxylate (at pH 7 and 37 degrees Celsius)
CC {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 3-[(1-
CC 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. Dimer. {ECO:0000269|PubMed:16632253,
CC ECO:0000269|PubMed:2139796, ECO:0000269|PubMed:22365602,
CC 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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_SSUV01000008.1.
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 PDBsum; 2FQ1; -.
DR PDBsum; 3RG2; -.
DR PDBsum; 4IZ6; -.
DR AlphaFoldDB; P0ADI4; -.
DR SMR; P0ADI4; -.
DR BioGRID; 4260905; 201.
DR BioGRID; 850538; 5.
DR ComplexPortal; CPX-5748; entBE aryl carrier complex.
DR DIP; DIP-9512N; -.
DR IntAct; P0ADI4; 29.
DR STRING; 511145.b0595; -.
DR SWISS-2DPAGE; P0ADI4; -.
DR jPOST; P0ADI4; -.
DR PaxDb; P0ADI4; -.
DR PRIDE; P0ADI4; -.
DR EnsemblBacteria; AAC73696; AAC73696; b0595.
DR EnsemblBacteria; BAE76350; BAE76350; BAE76350.
DR GeneID; 946178; -.
DR KEGG; ecj:JW0587; -.
DR KEGG; eco:b0595; -.
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 PhylomeDB; P0ADI4; -.
DR BioCyc; EcoCyc:ENTB-MON; -.
DR BioCyc; MetaCyc:ENTB-MON; -.
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; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
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 Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.40.50.850; -; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR016291; Isochorismatase.
DR InterPro; IPR000868; Isochorismatase-like.
DR InterPro; IPR036380; Isochorismatase-like_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR Pfam; PF00857; Isochorismatase; 1.
DR Pfam; PF00550; PP-binding; 1.
DR PIRSF; PIRSF001111; Isochorismatase; 1.
DR PRINTS; PR01398; ISCHRISMTASE.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF52499; SSF52499; 1.
DR PROSITE; PS50075; CARRIER; 1.
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 BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:16632253"
FT BINDING 244
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:16632253"
FT MOD_RES 245
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MUTAGEN 240
FT /note="D->R: The catalytic efficiency slightly increases,
FT but a 8-fold decrease of the affinity for the S-
FT 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 S-
FT 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 14..16
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 TURN 153..155
FT /evidence="ECO:0007829|PDB:2FQ1"
FT HELIX 156..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 215..222
FT /evidence="ECO:0007829|PDB:2FQ1"
FT HELIX 223..225
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
