ENTF_ECOLI
ID ENTF_ECOLI Reviewed; 1293 AA.
AC P11454; P75723; P77095; Q2MBL5;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Enterobactin synthase component F {ECO:0000305};
DE EC=6.3.2.14 {ECO:0000269|PubMed:216414, ECO:0000269|PubMed:9485415};
DE AltName: Full=Enterochelin synthase F;
DE AltName: Full=Nonribosomal peptide synthetase EntF {ECO:0000305};
DE Includes:
DE RecName: Full=L-serine--[L-seryl-carrier protein] ligase {ECO:0000305};
DE EC=6.2.1.72 {ECO:0000269|PubMed:9485415, ECO:0000305|PubMed:10688898, ECO:0000305|PubMed:1338974, ECO:0000305|PubMed:1826089, ECO:0000305|PubMed:216414};
DE AltName: Full=Serine-activating enzyme;
DE AltName: Full=Seryl-AMP ligase;
GN Name=entF {ECO:0000303|PubMed:216414}; OrderedLocusNames=b0586, JW0578;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-12, FUNCTION AS AN
RP L-SERINE-ACTIVATING ENZYME, COFACTOR, AND PATHWAY.
RC STRAIN=K12;
RX PubMed=1826089; DOI=10.1021/bi00225a027;
RA Rusnak F., Sakaitani M., Drueckhammer D., Reichert J., Walsh C.T.;
RT "Biosynthesis of the Escherichia coli siderophore enterobactin: sequence of
RT the entF gene, expression and purification of EntF, and analysis of
RT covalent phosphopantetheine.";
RL Biochemistry 30:2916-2927(1991).
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 1-34, AND INDUCTION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=3040679; DOI=10.1128/jb.169.9.4154-4162.1987;
RA Pettis G.S., McIntosh M.A.;
RT "Molecular characterization of the Escherichia coli enterobactin cistron
RT entF and coupled expression of entF and the fes gene.";
RL J. Bacteriol. 169:4154-4162(1987).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34, AND PROTEIN SEQUENCE OF 1-12.
RX PubMed=2974033; DOI=10.1016/s0021-9258(18)37361-7;
RA Pettis G.S., Brickman T.J., McIntosh M.A.;
RT "Transcriptional mapping and nucleotide sequence of the Escherichia coli
RT fepA-fes enterobactin region. Identification of a unique iron-regulated
RT bidirectional promoter.";
RL J. Biol. Chem. 263:18857-18863(1988).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=216414; DOI=10.1016/0304-4165(79)90297-6;
RA Woodrow G.C., Young I.G., Gibson F.;
RT "Biosynthesis of enterochelin in Escherichia coli K-12: separation of the
RT polypeptides coded for by the entD, E, F and G genes.";
RL Biochim. Biophys. Acta 582:145-153(1979).
RN [8]
RP FUNCTION AS AN L-SERINE-ACTIVATING ENZYME, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=1338974; DOI=10.1002/pro.5560010410;
RA Reichert J., Sakaitani M., Walsh C.T.;
RT "Characterization of EntF as a serine-activating enzyme.";
RL Protein Sci. 1:549-556(1992).
RN [9]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, SUBUNIT,
RP PHOSPHOPANTETHEINYLATION BY ENTD, AND MUTAGENESIS OF SER-1138.
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 COFACTOR, DOMAIN, PHOSPHOPANTETHEINYLATION AT SER-1006, ACTIVE SITE, AND
RP MUTAGENESIS OF SER-1138; ASP-1165 AND HIS-1271.
RX PubMed=10375542; DOI=10.1016/s1074-5521(99)80050-7;
RA Shaw-Reid C.A., Kelleher N.L., Losey H.C., Gehring A.M., Berg C.,
RA Walsh C.T.;
RT "Assembly line enzymology by multimodular nonribosomal peptide synthetases:
RT the thioesterase domain of E. coli EntF catalyzes both elongation and
RT cyclolactonization.";
RL Chem. Biol. 6:385-400(1999).
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 AS AN L-SERINE-ACTIVATING ENZYME.
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] {ECO:0007744|PDB:2ROQ}
RP STRUCTURE BY NMR OF 960-1293, AND DOMAIN.
RX PubMed=18704088; DOI=10.1038/nature07162;
RA Frueh D.P., Arthanari H., Koglin A., Vosburg D.A., Bennett A.E.,
RA Walsh C.T., Wagner G.;
RT "Dynamic thiolation-thioesterase structure of a non-ribosomal peptide
RT synthetase.";
RL Nature 454:903-906(2008).
RN [15] {ECO:0007744|PDB:3TEJ}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 965-1293, DOMAIN, AND MUTAGENESIS
RP OF PHE-1077; TRP-1079 AND GLN-1080.
RX PubMed=22118682; DOI=10.1016/j.chembiol.2011.09.018;
RA Liu Y., Zheng T., Bruner S.D.;
RT "Structural basis for phosphopantetheinyl carrier domain interactions in
RT the terminal module of nonribosomal peptide synthetases.";
RL Chem. Biol. 18:1482-1488(2011).
RN [16] {ECO:0007744|PDB:5T3D}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), AND COFACTOR.
RX PubMed=26762461; DOI=10.1038/nature16163;
RA Drake E.J., Miller B.R., Shi C., Tarrasch J.T., Sundlov J.A., Allen C.L.,
RA Skiniotis G., Aldrich C.C., Gulick A.M.;
RT "Structures of two distinct conformations of holo-non-ribosomal peptide
RT synthetases.";
RL Nature 529:235-238(2016).
RN [17] {ECO:0007744|PDB:5JA1, ECO:0007744|PDB:5JA2}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) IN COMPLEX WITH THE MBTH-LIKE
RP PROTEIN YBDZ, COFACTOR, AND ACTIVITY REGULATION.
RX PubMed=27597544; DOI=10.1074/jbc.m116.746297;
RA Miller B.R., Drake E.J., Shi C., Aldrich C.C., Gulick A.M.;
RT "Structures of a nonribosomal peptide synthetase module bound to MbtH-like
RT proteins support a highly dynamic domain architecture.";
RL J. Biol. Chem. 291:22559-22571(2016).
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 (PubMed:216414, PubMed:1826089,
CC PubMed:1338974, PubMed:9485415). EntF catalyzes the activation of L-
CC serine via ATP-dependent PPi exchange reaction to form seryladenylate
CC (PubMed:1826089, PubMed:1338974, PubMed:9485415, PubMed:10688898).
CC Activated L-serine is loaded onto the peptidyl carrier domain via a
CC thioester linkage to the phosphopanthetheine moiety, forming seryl-S-
CC Ppant-EntF (PubMed:9485415). EntF acts then as the sole catalyst for
CC the formation of the three amide and three ester linkages found in
CC enterobactin, using seryladenylate and 2,3-dihydroxybenzoate-S-Ppant-
CC EntB (DHB-S-Ppant-EntB) as substrates, via the formation of a DHB-Ser-
CC S-Ppant-EntF intermediate (PubMed:9485415).
CC {ECO:0000269|PubMed:10688898, ECO:0000269|PubMed:1338974,
CC ECO:0000269|PubMed:1826089, ECO:0000269|PubMed:216414,
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; Evidence={ECO:0000269|PubMed:216414,
CC ECO:0000269|PubMed:9485415};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + holo-[peptidyl-carrier protein] + L-serine = AMP +
CC diphosphate + L-seryl-[peptidyl-carrier protein];
CC Xref=Rhea:RHEA:61704, Rhea:RHEA-COMP:11480, Rhea:RHEA-COMP:15913,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:144955, ChEBI:CHEBI:456215;
CC EC=6.2.1.72; Evidence={ECO:0000269|PubMed:9485415,
CC ECO:0000305|PubMed:10688898, ECO:0000305|PubMed:1338974,
CC ECO:0000305|PubMed:1826089, ECO:0000305|PubMed:216414};
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000269|PubMed:10375542, ECO:0000269|PubMed:1826089,
CC ECO:0000269|PubMed:26762461, ECO:0000269|PubMed:27597544,
CC ECO:0000269|PubMed:9485415};
CC Note=Binds 1 phosphopantetheine covalently.
CC {ECO:0000269|PubMed:10375542, ECO:0000269|PubMed:26762461,
CC ECO:0000269|PubMed:27597544};
CC -!- ACTIVITY REGULATION: Adenylation activity is increased in the presence
CC of the MbtH-like protein YbdZ. {ECO:0000269|PubMed:27597544}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.26 mM for L-serine {ECO:0000269|PubMed:1338974};
CC KM=0.75 mM for ATP {ECO:0000269|PubMed:1338974};
CC KM=5.0 mM for O-acetyl-L-serine {ECO:0000269|PubMed:1338974};
CC KM=8.0 mM for L-beta-chloroalanine {ECO:0000269|PubMed:1338974};
CC KM=3.1 mM for S-methyl-L-cysteine {ECO:0000269|PubMed:1338974};
CC Note=kcat is 760 min(-1) with L-serine as substrate. kcat is 660
CC min(-1) with ATP as substrate. kcat is 720 min(-1) with O-acetyl-L-
CC serine as substrate. kcat is 870 min(-1) with L-beta-chloroalanine as
CC substrate. kcat is 38 min(-1) with S-methyl-L-cysteine as substrate.
CC {ECO:0000269|PubMed:1338974};
CC -!- PATHWAY: Siderophore biosynthesis; enterobactin biosynthesis.
CC {ECO:0000269|PubMed:1826089, ECO:0000269|PubMed:216414,
CC ECO:0000269|PubMed:9485415}.
CC -!- SUBUNIT: Proteins EntB, EntD, EntE and EntF are the component of the
CC enterobactin synthase (PubMed:216414, PubMed:9485415). Components
CC probably do not form a stable complex (PubMed:9485415). EntF acts as a
CC catalytic monomer (PubMed:9485415). Interacts with the MbtH-like
CC protein YbdZ. YbdZ binds to the adenylation domain, but does not alter
CC the structure of the domain (PubMed:27597544).
CC {ECO:0000269|PubMed:216414, ECO:0000269|PubMed:27597544,
CC ECO:0000269|PubMed:9485415}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10692387}.
CC Note=Membrane-associated. {ECO:0000269|PubMed:10692387}.
CC -!- INDUCTION: Transcriptionally regulated by iron and the fur protein.
CC {ECO:0000269|PubMed:3040679}.
CC -!- DOMAIN: Modular protein that contains an elongation/condensation
CC domain, an adenylation domain which activates the serine residue into
CC an aminoacyl-AMP ester, a peptidyl carrier protein domain which bears a
CC phosphopantetheinyl arm to attach the activated amino acid and a
CC thioesterase domain (Probable). The thioesterase domain is both a
CC cyclotrimerizing lactone synthetase and an elongation catalyst for
CC ester-bond formation between covalently tethered DHB-Ser moieties
CC (PubMed:10375542). The carrier-thioesterase di-domain forms a compact
CC structure with a well-defined domain interface; the two active sites
CC are at a suitable distance for substrate transfer from the peptidyl
CC carrier protein domain to the thioesterase domain (PubMed:18704088).
CC Phosphopantetheinylation leads to enhanced interaction between the two
CC domains (PubMed:22118682). {ECO:0000269|PubMed:10375542,
CC ECO:0000269|PubMed:18704088, ECO:0000269|PubMed:22118682, ECO:0000305}.
CC -!- PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine
CC of apo-EntF by EntD (PubMed:9485415). Holo-EntF so formed is then
CC acylated with seryl-AMP (PubMed:9485415). {ECO:0000269|PubMed:9485415}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC EntF subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB40785.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M60177; AAA92015.1; -; Genomic_DNA.
DR EMBL; U82598; AAB40785.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73687.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76341.1; -; Genomic_DNA.
DR EMBL; M17354; AAA23727.1; -; Genomic_DNA.
DR EMBL; J04216; AAA23759.1; -; Genomic_DNA.
DR PIR; H64791; YGECEF.
DR RefSeq; NP_415118.1; NC_000913.3.
DR RefSeq; WP_000077805.1; NZ_SSZK01000032.1.
DR PDB; 2ROQ; NMR; -; A=960-1293.
DR PDB; 3TEJ; X-ray; 1.90 A; A/B=965-1293.
DR PDB; 5JA1; X-ray; 3.00 A; A=1-1293.
DR PDB; 5JA2; X-ray; 3.00 A; A=1-1293.
DR PDB; 5T3D; X-ray; 2.80 A; A=1-1293.
DR PDBsum; 2ROQ; -.
DR PDBsum; 3TEJ; -.
DR PDBsum; 5JA1; -.
DR PDBsum; 5JA2; -.
DR PDBsum; 5T3D; -.
DR AlphaFoldDB; P11454; -.
DR SMR; P11454; -.
DR BioGRID; 4259895; 304.
DR BioGRID; 849570; 2.
DR DIP; DIP-9516N; -.
DR IntAct; P11454; 10.
DR STRING; 511145.b0586; -.
DR ESTHER; ecoli-entf; Thioesterase.
DR jPOST; P11454; -.
DR PaxDb; P11454; -.
DR PRIDE; P11454; -.
DR EnsemblBacteria; AAC73687; AAC73687; b0586.
DR EnsemblBacteria; BAE76341; BAE76341; BAE76341.
DR GeneID; 945184; -.
DR KEGG; ecj:JW0578; -.
DR KEGG; eco:b0586; -.
DR PATRIC; fig|1411691.4.peg.1684; -.
DR EchoBASE; EB0260; -.
DR eggNOG; COG1020; Bacteria.
DR eggNOG; COG3319; Bacteria.
DR HOGENOM; CLU_000022_2_13_6; -.
DR InParanoid; P11454; -.
DR OMA; IISPQAF; -.
DR PhylomeDB; P11454; -.
DR BioCyc; EcoCyc:ENTF-MON; -.
DR BioCyc; MetaCyc:ENTF-MON; -.
DR BRENDA; 6.2.1.72; 2026.
DR BRENDA; 6.3.2.14; 2026.
DR UniPathway; UPA00017; -.
DR EvolutionaryTrace; P11454; -.
DR PRO; PR:P11454; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0009366; C:enterobactin synthetase complex; 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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IDA:UniProtKB.
DR GO; GO:0031177; F:phosphopantetheine binding; IDA:EcoCyc.
DR GO; GO:0043041; P:amino acid activation for nonribosomal peptide biosynthetic process; IDA:EcoCyc.
DR GO; GO:0009239; P:enterobactin biosynthetic process; IMP:EcoCyc.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.30.559.10; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR020802; PKS_thioesterase.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR001031; Thioesterase.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SMART; SM00824; PKS_TE; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Direct protein sequencing;
KW Enterobactin biosynthesis; Ligase; Multifunctional enzyme;
KW Nucleotide-binding; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..1293
FT /note="Enterobactin synthase component F"
FT /id="PRO_0000193077"
FT DOMAIN 971..1046
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 1..301
FT /note="Elongation/condensation"
FT /evidence="ECO:0000305"
FT REGION 482..887
FT /note="Adenylatione"
FT /evidence="ECO:0000305"
FT REGION 1066..1293
FT /note="Thioesterase"
FT /evidence="ECO:0000305"
FT ACT_SITE 1271
FT /note="Proton acceptor; for thioesterase activity"
FT /evidence="ECO:0000305|PubMed:10375542"
FT MOD_RES 1006
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000269|PubMed:10375542,
FT ECO:0000269|PubMed:26762461, ECO:0000269|PubMed:27597544"
FT MUTAGEN 1077
FT /note="F->A: Retains 2% of activity."
FT /evidence="ECO:0000269|PubMed:22118682"
FT MUTAGEN 1079
FT /note="W->A: Abolishes enterobactin production."
FT /evidence="ECO:0000269|PubMed:22118682"
FT MUTAGEN 1080
FT /note="Q->A: Retains 50% of activity."
FT /evidence="ECO:0000269|PubMed:22118682"
FT MUTAGEN 1138
FT /note="S->A: No enterobactin synthase activity. This mutant
FT holo-EntF is still able to adenylate serine and to
FT autoacylate itself with serine."
FT /evidence="ECO:0000269|PubMed:9485415"
FT MUTAGEN 1138
FT /note="S->C: 1000-fold decrease in kcat. Releases both
FT enterobactin an linear dimers (DHB-Ser)2."
FT /evidence="ECO:0000269|PubMed:10375542"
FT MUTAGEN 1165
FT /note="D->A: 20-fold decrease in kcat."
FT /evidence="ECO:0000269|PubMed:10375542"
FT MUTAGEN 1165
FT /note="D->S: 200-fold decrease in kcat."
FT /evidence="ECO:0000269|PubMed:10375542"
FT MUTAGEN 1271
FT /note="H->A: 10000-fold decrease in kcat. Releases only
FT enterobactin, but accumulates both DHB-Ser-O-TE and (DHB-
FT Ser)2-O-TE acyl enzyme intermediates."
FT /evidence="ECO:0000269|PubMed:10375542"
FT CONFLICT 441..442
FT /note="QL -> HV (in Ref. 1; AAA92015)"
FT /evidence="ECO:0000305"
FT HELIX 11..20
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 28..37
FT /evidence="ECO:0007829|PDB:5T3D"
FT HELIX 41..54
FT /evidence="ECO:0007829|PDB:5T3D"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:5T3D"
FT HELIX 95..104
FT /evidence="ECO:0007829|PDB:5T3D"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 130..137
FT /evidence="ECO:0007829|PDB:5T3D"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:5T3D"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:5T3D"
FT HELIX 146..161
FT /evidence="ECO:0007829|PDB:5T3D"
FT HELIX 174..185
FT /evidence="ECO:0007829|PDB:5T3D"
FT HELIX 188..203
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 224..231
FT /evidence="ECO:0007829|PDB:5T3D"
FT HELIX 235..243
FT /evidence="ECO:0007829|PDB:5T3D"
FT HELIX 249..264
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 267..275
FT /evidence="ECO:0007829|PDB:5T3D"
FT HELIX 282..285
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 292..299
FT /evidence="ECO:0007829|PDB:5T3D"
FT HELIX 306..322
FT /evidence="ECO:0007829|PDB:5T3D"
FT TURN 323..325
FT /evidence="ECO:0007829|PDB:5T3D"
FT HELIX 328..334
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 346..350
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 367..371
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 376..384
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 390..397
FT /evidence="ECO:0007829|PDB:5T3D"
FT TURN 398..400
FT /evidence="ECO:0007829|PDB:5T3D"
FT HELIX 403..422
FT /evidence="ECO:0007829|PDB:5T3D"
FT HELIX 428..430
FT /evidence="ECO:0007829|PDB:5T3D"
FT HELIX 438..445
FT /evidence="ECO:0007829|PDB:5T3D"
FT HELIX 457..467
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 471..475
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 480..482
FT /evidence="ECO:0007829|PDB:5T3D"
FT HELIX 483..499
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 507..510
FT /evidence="ECO:0007829|PDB:5T3D"
FT HELIX 516..527
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 531..534
FT /evidence="ECO:0007829|PDB:5T3D"
FT HELIX 541..551
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 554..558
FT /evidence="ECO:0007829|PDB:5T3D"
FT TURN 560..564
FT /evidence="ECO:0007829|PDB:5T3D"
FT HELIX 565..568
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 569..571
FT /evidence="ECO:0007829|PDB:5JA1"
FT STRAND 574..576
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 596..603
FT /evidence="ECO:0007829|PDB:5T3D"
FT TURN 606..608
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 611..616
FT /evidence="ECO:0007829|PDB:5T3D"
FT HELIX 617..630
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 638..641
FT /evidence="ECO:0007829|PDB:5T3D"
FT HELIX 650..660
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 663..666
FT /evidence="ECO:0007829|PDB:5T3D"
FT HELIX 671..673
FT /evidence="ECO:0007829|PDB:5T3D"
FT HELIX 675..684
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 689..692
FT /evidence="ECO:0007829|PDB:5T3D"
FT HELIX 694..702
FT /evidence="ECO:0007829|PDB:5T3D"
FT HELIX 706..712
FT /evidence="ECO:0007829|PDB:5T3D"
FT HELIX 713..715
FT /evidence="ECO:0007829|PDB:5JA1"
FT STRAND 718..724
FT /evidence="ECO:0007829|PDB:5T3D"
FT HELIX 728..738
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 742..746
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 751..753
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 755..759
FT /evidence="ECO:0007829|PDB:5T3D"
FT HELIX 762..766
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 770..772
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 776..778
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 782..787
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 800..806
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 811..814
FT /evidence="ECO:0007829|PDB:5JA1"
FT HELIX 817..823
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 824..826
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 834..844
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 850..862
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 865..868
FT /evidence="ECO:0007829|PDB:5T3D"
FT HELIX 869..877
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 882..890
FT /evidence="ECO:0007829|PDB:5T3D"
FT HELIX 894..896
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 898..900
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 904..915
FT /evidence="ECO:0007829|PDB:5T3D"
FT HELIX 919..929
FT /evidence="ECO:0007829|PDB:5T3D"
FT HELIX 932..934
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 937..941
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 951..953
FT /evidence="ECO:0007829|PDB:5T3D"
FT HELIX 955..957
FT /evidence="ECO:0007829|PDB:5T3D"
FT STRAND 968..971
FT /evidence="ECO:0007829|PDB:2ROQ"
FT HELIX 976..988
FT /evidence="ECO:0007829|PDB:3TEJ"
FT STRAND 994..996
FT /evidence="ECO:0007829|PDB:5JA1"
FT TURN 999..1003
FT /evidence="ECO:0007829|PDB:3TEJ"
FT HELIX 1006..1020
FT /evidence="ECO:0007829|PDB:3TEJ"
FT HELIX 1026..1031
FT /evidence="ECO:0007829|PDB:3TEJ"
FT HELIX 1035..1043
FT /evidence="ECO:0007829|PDB:3TEJ"
FT TURN 1050..1053
FT /evidence="ECO:0007829|PDB:3TEJ"
FT STRAND 1054..1061
FT /evidence="ECO:0007829|PDB:3TEJ"
FT STRAND 1063..1065
FT /evidence="ECO:0007829|PDB:2ROQ"
FT STRAND 1067..1071
FT /evidence="ECO:0007829|PDB:3TEJ"
FT HELIX 1079..1086
FT /evidence="ECO:0007829|PDB:3TEJ"
FT STRAND 1093..1097
FT /evidence="ECO:0007829|PDB:3TEJ"
FT TURN 1101..1103
FT /evidence="ECO:0007829|PDB:3TEJ"
FT HELIX 1105..1108
FT /evidence="ECO:0007829|PDB:3TEJ"
FT HELIX 1112..1126
FT /evidence="ECO:0007829|PDB:3TEJ"
FT STRAND 1128..1130
FT /evidence="ECO:0007829|PDB:3TEJ"
FT STRAND 1132..1137
FT /evidence="ECO:0007829|PDB:3TEJ"
FT HELIX 1139..1153
FT /evidence="ECO:0007829|PDB:3TEJ"
FT STRAND 1158..1165
FT /evidence="ECO:0007829|PDB:3TEJ"
FT HELIX 1170..1173
FT /evidence="ECO:0007829|PDB:3TEJ"
FT HELIX 1174..1180
FT /evidence="ECO:0007829|PDB:2ROQ"
FT HELIX 1186..1199
FT /evidence="ECO:0007829|PDB:3TEJ"
FT TURN 1200..1203
FT /evidence="ECO:0007829|PDB:5JA1"
FT HELIX 1208..1224
FT /evidence="ECO:0007829|PDB:3TEJ"
FT STRAND 1232..1241
FT /evidence="ECO:0007829|PDB:3TEJ"
FT HELIX 1242..1244
FT /evidence="ECO:0007829|PDB:3TEJ"
FT TURN 1248..1250
FT /evidence="ECO:0007829|PDB:5JA2"
FT HELIX 1251..1255
FT /evidence="ECO:0007829|PDB:3TEJ"
FT TURN 1256..1258
FT /evidence="ECO:0007829|PDB:3TEJ"
FT STRAND 1259..1269
FT /evidence="ECO:0007829|PDB:3TEJ"
FT HELIX 1271..1275
FT /evidence="ECO:0007829|PDB:3TEJ"
FT TURN 1277..1279
FT /evidence="ECO:0007829|PDB:3TEJ"
FT HELIX 1280..1291
FT /evidence="ECO:0007829|PDB:3TEJ"
SQ SEQUENCE 1293 AA; 141991 MW; F3FCBD3836A39358 CRC64;
MSQHLPLVAA QPGIWMAEKL SELPSAWSVA HYVELTGEVD SPLLARAVVA GLAQADTLRM
RFTEDNGEVW QWVDDALTFE LPEIIDLRTN IDPHGTAQAL MQADLQQDLR VDSGKPLVFH
QLIQVADNRW YWYQRYHHLL VDGFSFPAIT RQIANIYCTW LRGEPTPASP FTPFADVVEE
YQQYRESEAW QRDAAFWAEQ RRQLPPPASL SPAPLPGRSA SADILRLKLE FTDGEFRQLA
TQLSGVQRTD LALALAALWL GRLCNRMDYA AGFIFMRRLG SAALTATGPV LNVLPLGIHI
AAQETLPELA TRLAAQLKKM RRHQRYDAEQ IVRDSGRAAG DEPLFGPVLN IKVFDYQLDI
PDVQAQTHTL ATGPVNDLEL ALFPDVHGDL SIEILANKQR YDEPTLIQHA ERLKMLIAQF
AADPALLCGD VDIMLPGEYA QLAQLNATQV EIPETTLSAL VAEQAAKTPD APALADARYL
FSYREMREQV VALANLLRER GVKPGDSVAV ALPRSVFLTL ALHAIVEAGA AWLPLDTGYP
DDRLKMMLED ARPSLLITTD DQLPRFSDVP NLTSLCYNAP LTPQGSAPLQ LSQPHHTAYI
IFTSGSTGRP KGVMVGQTAI VNRLLWMQNH YPLTGEDVVA QKTPCSFDVS VWEFFWPFIA
GAKLVMAEPE AHRDPLAMQQ FFAEYGVTTT HFVPSMLAAF VASLTPQTAR QSCATLKQVF
CSGEALPADL CREWQQLTGA PLHNLYGPTE AAVDVSWYPA FGEELAQVRG SSVPIGYPVW
NTGLRILDAM MHPVPPGVAG DLYLTGIQLA QGYLGRPDLT ASRFIADPFA PGERMYRTGD
VARWLDNGAV EYLGRSDDQL KIRGQRIELG EIDRVMQALP DVEQAVTHAC VINQAAATGG
DARQLVGYLV SQSGLPLDTS ALQAQLRETL PPHMVPVVLL QLPQLPLSAN GKLDRKALPL
PELKAQAPGR APKAGSETII AAAFSSLLGC DVQDADADFF ALGGHSLLAM KLAAQLSRQV
ARQVTPGQVM VASTVAKLAT IIDAEEDSTR RMGFETILPL REGNGPTLFC FHPASGFAWQ
FSVLSRYLDP QWSIIGIQSP RPNGPMQTAA NLDEVCEAHL ATLLEQQPHG PYYLLGYSLG
GTLAQGIAAR LRARGEQVAF LGLLDTWPPE TQNWQEKEAN GLDPEVLAEI NREREAFLAA
QQGSTSTELF TTIEGNYADA VRLLTTAHSV PFDGKATLFV AERTLQEGMS PERAWSPWIA
ELDIYRQDCA HVDIISPGTF EKIGPIIRAT LNR
