ENTD_SALTI
ID ENTD_SALTI Reviewed; 234 AA.
AC Q8Z8L9;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Enterobactin synthase component D {ECO:0000250|UniProtKB:P19925};
DE AltName: Full=4'-phosphopantetheinyl transferase EntD {ECO:0000250|UniProtKB:P19925};
DE EC=2.7.8.- {ECO:0000250|UniProtKB:P19925};
DE AltName: Full=Enterochelin synthase D {ECO:0000250|UniProtKB:P19925};
GN Name=entD {ECO:0000250|UniProtKB:P19925}; OrderedLocusNames=STY0627, t2284;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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. Plays an essential
CC role in the assembly of the enterobactin by catalyzing the transfer of
CC the 4'-phosphopantetheine (Ppant) moiety from coenzyme A to the apo-
CC domains of both EntB (ArCP domain) and EntF (PCP domain) to yield their
CC holo-forms which make them competent for the activation of 2,3-
CC dihydroxybenzoate (DHB) and L-serine, respectively.
CC {ECO:0000250|UniProtKB:P19925}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=apo-[aryl-carrier protein] + CoA = adenosine 3',5'-
CC bisphosphate + H(+) + holo-[aryl-carrier protein];
CC Xref=Rhea:RHEA:48404, Rhea:RHEA-COMP:15903, Rhea:RHEA-COMP:17557,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:64479;
CC Evidence={ECO:0000250|UniProtKB:P19925};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=apo-[peptidyl-carrier protein] + CoA = adenosine 3',5'-
CC bisphosphate + H(+) + holo-[peptidyl-carrier protein];
CC Xref=Rhea:RHEA:46228, Rhea:RHEA-COMP:11479, Rhea:RHEA-COMP:11480,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:64479;
CC Evidence={ECO:0000250|UniProtKB:P19925};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P24224};
CC -!- PATHWAY: Siderophore biosynthesis; enterobactin biosynthesis.
CC {ECO:0000250|UniProtKB:P19925}.
CC -!- SUBUNIT: EntB, EntD, EntE, and EntF form a multienzyme complex called
CC enterobactin synthase. {ECO:0000250|UniProtKB:P19925}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P19925}.
CC -!- SIMILARITY: Belongs to the P-Pant transferase superfamily. EntD family.
CC {ECO:0000250|UniProtKB:P19925}.
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DR EMBL; AL513382; CAD05060.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO69885.1; -; Genomic_DNA.
DR RefSeq; NP_455161.1; NC_003198.1.
DR RefSeq; WP_001681620.1; NZ_WSUR01000008.1.
DR AlphaFoldDB; Q8Z8L9; -.
DR SMR; Q8Z8L9; -.
DR STRING; 220341.16501836; -.
DR EnsemblBacteria; AAO69885; AAO69885; t2284.
DR KEGG; stt:t2284; -.
DR KEGG; sty:STY0627; -.
DR PATRIC; fig|220341.7.peg.628; -.
DR eggNOG; COG2977; Bacteria.
DR HOGENOM; CLU_075076_1_0_6; -.
DR OMA; WFGSISH; -.
DR UniPathway; UPA00017; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; Chromosome.
DR GO; GO:0009366; C:enterobactin synthetase complex; ISS:UniProtKB.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0009239; P:enterobactin biosynthetic process; ISS:UniProtKB.
DR Gene3D; 3.90.470.20; -; 1.
DR InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
DR InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
DR InterPro; IPR041354; 4PPT_N.
DR InterPro; IPR003542; Enbac_synth_compD-like.
DR PANTHER; PTHR38096; PTHR38096; 1.
DR Pfam; PF17837; 4PPT_N; 1.
DR Pfam; PF01648; ACPS; 1.
DR PRINTS; PR01399; ENTSNTHTASED.
DR SUPFAM; SSF56214; SSF56214; 1.
PE 3: Inferred from homology;
KW Enterobactin biosynthesis; Magnesium; Membrane; Metal-binding; Transferase.
FT CHAIN 1..234
FT /note="Enterobactin synthase component D"
FT /id="PRO_0000206072"
FT BINDING 107
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 234 AA; 25739 MW; BF37D9FE47A8FEA0 CRC64;
MLTSHFPLPF AGHRLHIVDF DASSFHEHDL LWLPHHDRLR SAGRKRKAEH LAGRIAAVHA
LREVGVRAVP GIGDKRQPLW PDGLFGSISH CASTALAVIS RQRVGVDIEK IMSQHTATEL
APSIIDSDER QILQASSLPF PLALTLAFSA KESVYKAFSD RVTLPGFDSA KITSLNATHI
SLHLLPAFAA MMAERTVRTE WFQRGNSVIT LVSAITRFPH DRSAPASILS AIPR
