ENTE_ECO57
ID ENTE_ECO57 Reviewed; 536 AA.
AC Q8XBV3;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Enterobactin synthase component E {ECO:0000250|UniProtKB:P10378};
DE EC=6.3.2.14 {ECO:0000250|UniProtKB:P10378};
DE AltName: Full=2,3-dihydroxybenzoate-AMP liase {ECO:0000250|UniProtKB:P10378};
DE Short=DHB-AMP ligase {ECO:0000250|UniProtKB:P10378};
DE AltName: Full=2,3-dihydroxybenzoate-AMP synthase {ECO:0000250|UniProtKB:P10378};
DE EC=6.2.1.71 {ECO:0000250|UniProtKB:P10378};
DE AltName: Full=Dihydroxybenzoic acid-activating enzyme {ECO:0000250|UniProtKB:P10378};
DE AltName: Full=Enterochelin synthase E {ECO:0000250|UniProtKB:P10378};
GN Name=entE {ECO:0000250|UniProtKB:P10378}; OrderedLocusNames=Z0736, ECs0633;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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 proccesses
CC via 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.
CC {ECO:0000250|UniProtKB:P10378}.
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:0000250|UniProtKB:P10378};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2,3-dihydroxybenzoate + ATP + holo-[aryl-carrier protein] =
CC 2,3-dihydroxybenzoyl-[aryl-carrier protein] + AMP + diphosphate;
CC Xref=Rhea:RHEA:61652, Rhea:RHEA-COMP:15903, Rhea:RHEA-COMP:17559,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:36654,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:90610, ChEBI:CHEBI:456215;
CC EC=6.2.1.71; Evidence={ECO:0000250|UniProtKB:P10378};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2,3-dihydroxybenzoyl-5'-AMP + holo-[aryl-carrier protein] =
CC 2,3-dihydroxybenzoyl-[aryl-carrier protein] + AMP + H(+);
CC Xref=Rhea:RHEA:48604, Rhea:RHEA-COMP:15903, Rhea:RHEA-COMP:17559,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57417, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:90610, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:P10378};
CC -!- PATHWAY: Siderophore biosynthesis; enterobactin biosynthesis.
CC {ECO:0000250|UniProtKB:P10378}.
CC -!- SUBUNIT: Proteins EntB, EntD, EntE, and EntF form a multienzyme complex
CC called enterobactin synthase. Monomer. EntA and EntE interact together.
CC {ECO:0000250|UniProtKB:P10378}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P10378}.
CC -!- INDUCTION: Under conditions of iron deficiency and by the fur protein.
CC {ECO:0000250|UniProtKB:P10378}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC EntE subfamily. {ECO:0000250|UniProtKB:P10378}.
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DR EMBL; AE005174; AAG54929.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB34056.1; -; Genomic_DNA.
DR PIR; A99708; A99708.
DR PIR; E85558; E85558.
DR RefSeq; NP_308660.1; NC_002695.1.
DR RefSeq; WP_000026781.1; NZ_SEKU01000009.1.
DR AlphaFoldDB; Q8XBV3; -.
DR SMR; Q8XBV3; -.
DR STRING; 155864.EDL933_0664; -.
DR PRIDE; Q8XBV3; -.
DR EnsemblBacteria; AAG54929; AAG54929; Z0736.
DR EnsemblBacteria; BAB34056; BAB34056; ECs_0633.
DR GeneID; 916992; -.
DR KEGG; ece:Z0736; -.
DR KEGG; ecs:ECs_0633; -.
DR PATRIC; fig|386585.9.peg.743; -.
DR eggNOG; COG1021; Bacteria.
DR HOGENOM; CLU_000022_59_7_6; -.
DR OMA; PNIRFIR; -.
DR UniPathway; UPA00017; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008668; F:(2,3-dihydroxybenzoyl)adenylate synthase activity; ISS:UniProtKB.
DR GO; GO:0047527; F:2,3-dihydroxybenzoate-serine ligase activity; ISS:UniProtKB.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009239; P:enterobactin biosynthetic process; ISS:UniProtKB.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR011963; DHB_AMP_lig.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR TIGRFAMs; TIGR02275; DHB_AMP_lig; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 3: Inferred from homology;
KW Acyltransferase; ATP-binding; Enterobactin biosynthesis; Ligase; Membrane;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..536
FT /note="Enterobactin synthase component E"
FT /id="PRO_0000193076"
FT REGION 438..439
FT /note="Phosphopantetheine binding"
FT /evidence="ECO:0000250|UniProtKB:P10378"
FT BINDING 235
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10378"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10378"
FT BINDING 309
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10378"
FT BINDING 331
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10378"
FT BINDING 335
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10378"
FT BINDING 415
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10378"
FT BINDING 432
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10378"
FT BINDING 441
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10378"
SQ SEQUENCE 536 AA; 59040 MW; ABC8E0B3209940A5 CRC64;
MSIPFTRWPE EFARRYREKG YWQDLPLTDI LTRHAASDSI AVIDGERQLS YRELNQAADN
LACSLRRQGI KPGETALVQL GNVAELYITF FALLKLGVAP VLALFSHQRS ELNAYASQIE
PALLIADRQH ALFSGDDFLN TFVAEHSSIR VVQLLNDSGE HNLQDAINHP ADGFTATPSP
ADEVVYFQLS GGTTGTPKLI PRTHNDYYYS VRRSVEICQF TQQTRYLCAI PAAHNYAMSS
PGSLGVFLAG GTVVLAADPS ATLCFPLIEK HQINVTALVP PAVSLWLQAL TEGESRAQLA
SLKLLQVGGA RLSATLAARI PAEIGCQLQQ VFGMAEGLVN YTRLDDSAEK IIHTQGYPMC
PDDEVWVADA EGNPLPQGEV GRLMTRGPYT FRGYYKSPQH NASAFDANGF YCSGDLISID
PEGYITVQGR EKDQINRGGE KIAAEEIENL LLRHPAVIYA ALVSMEDELM GEKSCAYLVV
KEPLRAVQVR RFLREQGIAE FKLPDRVECV DSLPLTAVGK VDKKQLRQWL ASRASA
