ENTF_ECO57
ID ENTF_ECO57 Reviewed; 1293 AA.
AC Q8XBV9;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Enterobactin synthase component F {ECO:0000250|UniProtKB:P11454};
DE EC=6.3.2.14 {ECO:0000250|UniProtKB:P11454};
DE AltName: Full=Enterochelin synthase F {ECO:0000250|UniProtKB:P11454};
DE AltName: Full=Nonribosomal peptide synthetase EntF {ECO:0000250|UniProtKB:P11454};
DE Includes:
DE RecName: Full=L-serine--[L-seryl-carrier protein] ligase {ECO:0000250|UniProtKB:P11454};
DE EC=6.2.1.72 {ECO:0000250|UniProtKB:P11454};
DE AltName: Full=Serine-activating enzyme {ECO:0000250|UniProtKB:P11454};
DE AltName: Full=Seryl-AMP ligase {ECO:0000250|UniProtKB:P11454};
GN Name=entF; OrderedLocusNames=Z0727, ECs0625;
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. EntF catalyzes the activation of L-serine via
CC ATP-dependent PPi exchange reaction to form seryladenylate. Activated
CC L-serine is loaded onto the peptidyl carrier domain via a thioester
CC linkage to the phosphopanthetheine moiety, forming seryl-S-Ppant-EntF.
CC EntF acts then as the sole catalyst for the formation of the three
CC amide and three ester linkages found in enterobactin, using
CC seryladenylate and 2,3-dihydroxybenzoate-S-Ppant-EntB (DHB-S-Ppant-
CC EntB) as substrates, via the formation of a DHB-Ser-S-Ppant-EntF
CC intermediate. {ECO:0000250|UniProtKB:P11454}.
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:P11454};
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:0000250|UniProtKB:P11454};
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000250|UniProtKB:P11454};
CC Note=Binds 1 phosphopantetheine covalently.
CC {ECO:0000250|UniProtKB:P11454};
CC -!- PATHWAY: Siderophore biosynthesis; enterobactin biosynthesis.
CC {ECO:0000250|UniProtKB:P11454}.
CC -!- SUBUNIT: Proteins EntB, EntD, EntE and EntF are the component of the
CC enterobactin synthase. Components probably do not form a stable
CC complex. EntF acts as a catalytic monomer.
CC {ECO:0000250|UniProtKB:P11454}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P11454}.
CC Note=Membrane-associated. {ECO:0000250|UniProtKB:P11454}.
CC -!- PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine
CC of apo-EntF by EntD. Holo-EntF so formed is then acylated with seryl-
CC AMP. {ECO:0000250|UniProtKB:P11454}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC EntF subfamily. {ECO:0000305}.
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DR EMBL; AE005174; AAG54921.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB34048.1; -; Genomic_DNA.
DR PIR; A90707; A90707.
DR PIR; E85557; E85557.
DR RefSeq; NP_308652.1; NC_002695.1.
DR RefSeq; WP_000077784.1; NZ_SEKU01000009.1.
DR AlphaFoldDB; Q8XBV9; -.
DR SMR; Q8XBV9; -.
DR STRING; 155864.EDL933_0656; -.
DR ESTHER; ecoli-entf; Thioesterase.
DR EnsemblBacteria; AAG54921; AAG54921; Z0727.
DR EnsemblBacteria; BAB34048; BAB34048; ECs_0625.
DR GeneID; 916984; -.
DR KEGG; ece:Z0727; -.
DR KEGG; ecs:ECs_0625; -.
DR PATRIC; fig|386585.9.peg.735; -.
DR eggNOG; COG1020; Bacteria.
DR eggNOG; COG3319; Bacteria.
DR HOGENOM; CLU_000022_2_13_6; -.
DR OMA; IISPQAF; -.
DR UniPathway; UPA00017; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0009366; C:enterobactin synthetase complex; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0047527; F:2,3-dihydroxybenzoate-serine ligase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; ISS:UniProtKB.
DR GO; GO:0031177; F:phosphopantetheine binding; ISS:UniProtKB.
DR GO; GO:0043041; P:amino acid activation for nonribosomal peptide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0009239; P:enterobactin biosynthetic process; ISS:UniProtKB.
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 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Enterobactin biosynthesis; Ligase;
KW Multifunctional enzyme; Nucleotide-binding; Phosphopantetheine;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..1293
FT /note="Enterobactin synthase component F"
FT /id="PRO_0000193078"
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="Adenylation"
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:0000250|UniProtKB:P11454"
FT MOD_RES 1006
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000250|UniProtKB:P11454"
SQ SEQUENCE 1293 AA; 141953 MW; BB8F5B21CB439183 CRC64;
MSQHLPLVAA QPGIWMAEKL SELPSAWSVA HYVELTGEVD APLLARAVVA GLAQADTLRM
RFTEDNGEVW QWVDDALIFE LPEIIDLRTN IDPHGTAQAL MQADLQQDLR VDSGKPLVFH
QLIQVADNRW YWYQRYHHLL VDGFSFPAIT RQIANIYCAL LRGEQTPASP FTPFADVVEE
YQQYRESEAW QRDAAFWAEQ RRQLPPPASL SPAPLAGRSA SADILRLKLE FTDGEFRQLA
TQLSGVQRTD LALALAAFWL GRLCNRMDYA AGFIFMRRLG SAALTATGPV LNVLPLGIHI
AAQETLPELA TRLAAQLKKM RRHQRYDAEQ IVRDSGRAAG DEPLFGPVLN IKVFDYQLDI
PGVQAQTHTL ATGPVNDLEL ALFPDEHGDL SIEILANKQH YDEPTLIQHA ERLKMLIAQF
AADPALLCGD VDIMLPGEYA QLAQINATQV EIPETTLSAL VAEQAAKTPD APALADARYQ
FSYREMREQV VALANLLREH GVKPGDSVAV ALPRSVFLTL ALHAIVEAGA AWLPLDTGYP
DDRLKMMLED ARPSLLITTD DQLPRFADVP DLTNLCYNAP LTPQGSAPLQ LSQPHHTAYI
IFTSGSTGRP KGVMVGQTAI VNRLLWMQNH YPLTGEDVVA QKTPCSFDVS VWEFFWPFIA
GAKLVMAEPE AHRDPLAMQQ FFAEYGVTTT HFVPSMLAAF VASLTPQTAR QNCATLKQVF
CSGEALPADL CREWQQLTGA PLHNLYGPTE AAVDVSWYPA FGEELAQVRG SSVPIGYPVW
NTGLRILDAM MHPVPPGVAG DLYLTGIQLA QGYLGRPDLT ASRFIADPFV PGERMYRTGD
VARWLDNGAV EYLGRSDDQL KIRGQRIELG EIDRVMQALP DVEQAVTHAC VINQAAATGG
DARQLVGYLV SQSGLPLDTS ALQAQLRETL PPHMAPVVLL QLPQLPLSAN GKLDRKALPL
PELKAQTPGR APKAGSETII AAAFASLLGC DVQDADADFF ALGGHSLLAM KLAAQLSRQF
ARQVTPGQVM VASTVAKLAT IIDGEEDSSR RMGFETILPL REGNGPTLFC FHPASGFAWQ
FSVLSRYLDP LWSIIGIQSP RPHGPMQTAT NLDEVCEAHL ATLLEQQPHG PYYLLGYSLG
GTLAQGIAAR LRARGEQVAF LGLLDTWPPE TQNWQEKEAN GLDPEVLAEI NREREAFLAA
QQGSTSTELF TTIEGNYADA VRLLTTAHSV PFDGKATLFV AERTLQEGMS PERAWSPWIA
ELDIYRQDCA HVDIISPGAF EKIGPIIRAT LNR
