ENTF_SHIFL
ID ENTF_SHIFL Reviewed; 1281 AA.
AC P29698;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2003, sequence version 2.
DT 25-MAY-2022, entry version 155.
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=SF0498, S0504;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1252-1281.
RX PubMed=1846151; DOI=10.1128/jb.173.2.816-825.1991;
RA Schmitt M.P., Payne S.M.;
RT "Genetic analysis of the enterobactin gene cluster in Shigella flexneri.";
RL J. Bacteriol. 173:816-825(1991).
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; AE005674; AAN42148.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP16020.1; -; Genomic_DNA.
DR EMBL; M63304; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_706441.1; NC_004337.2.
DR RefSeq; WP_000077741.1; NZ_UDUU01000106.1.
DR AlphaFoldDB; P29698; -.
DR SMR; P29698; -.
DR STRING; 198214.SF0498; -.
DR ESTHER; shifl-entf; Thioesterase.
DR EnsemblBacteria; AAN42148; AAN42148; SF0498.
DR EnsemblBacteria; AAP16020; AAP16020; S0504.
DR GeneID; 1023397; -.
DR KEGG; sfl:SF0498; -.
DR KEGG; sft:NCTC1_00519; -.
DR KEGG; sfx:S0504; -.
DR PATRIC; fig|198214.7.peg.578; -.
DR HOGENOM; CLU_000022_2_13_6; -.
DR OrthoDB; 572620at2; -.
DR UniPathway; UPA00017; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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; 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 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..1281
FT /note="Enterobactin synthase component F"
FT /id="PRO_0000193079"
FT DOMAIN 975..1050
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 1..301
FT /note="Elongation/condensation"
FT /evidence="ECO:0000305"
FT REGION 486..891
FT /note="Adenylation"
FT /evidence="ECO:0000305"
FT REGION 1070..1281
FT /note="Thioesterase"
FT /evidence="ECO:0000305"
FT ACT_SITE 1259
FT /note="Proton acceptor; for thioesterase activity"
FT /evidence="ECO:0000250|UniProtKB:P11454"
FT MOD_RES 1010
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000250|UniProtKB:P11454"
FT CONFLICT 1267..1269
FT /note="AFV -> TFE (in Ref. 3; M63304)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1281 AA; 140696 MW; 5F1C4AF64E4143C5 CRC64;
MSQHLPLVAA QPGIWMAEKL SDLPSAWSVA HYVELTGEVD APLLARAVVA GLAQADTLRM
RFTEDNGEVW QWVDDALIFE LPEIIDLRTN IDPHGTAQAL MLADLQQDLR VDSGKPLVFH
QLIQVADNRW YWYQRYHHLL VDGFSFPAIT RQIANIYCAL LRGEPTPASP FTPFADVVEE
YQQYRESEAW QRDAAFWVEQ RRQLPPPASL SPAPLAGRSA SADILRLKME FTDGEFRQLA
TQLSGVQRTD LALALTALWL GRLCNRMDYA AGFIFMRRLG SAALTATGPV LNVLPLGIHI
AAQETLPELA TRLATRLAAQ LKKMRRHQRY DAEQIVRDSG RAAGDEPLFG PVLNIKVFDY
QLDIPGVQAQ THTLATGPVN DLELALFPDE HGDLSIEILA NKQRYDEPTL IQHAERLKML
IAQFAADPAL LCGDVDIMLP GEYAQLAQIN ATQVEIPETT LSALVAEQAA KTPDAPALAD
ARYLFSYREM HEQVVALANL LRERGVKPGD SVAVALPRSV FLTLALHAIV EAGAAWLPLD
TGYPDDRLKM MLEDARPSLL ITTDDQLPRF SDVPNLTNLC YNAPLTPQGS APLQLSQPHH
TAYIIFTSGS TGRPKGVMVG QTAIVNRLLW MQNHYPLTGE DVVAQKTPCS FDVSVWEFFW
PFIAGAKLVM AEPEAHRDPL AMQQFFAEYG VTTTHFVPSM LAAFVASLTP QTARQSCVTL
KQVFCSGEAL PADLCREWQQ LTGAPLHNLY GPTEAAVDVS WYPAFGEELA QVRGSSVPIG
YPVWNTGLRI LDAMMHPVPP GVAGDLYLTG IQLAQGYLGR PDLTASRFIA DPFAPGERMY
RTGDVARWLD NGAVEYLGRS DDQLKIRGQR IELGEIDRVM QALPDVKQAV THACVINQAA
ATGGDARQLV GYLVSQSGLP LDTSALQAQL RETLPPHMVP VVLLQLPQLP LSANGKLDRK
ALPLPELKAQ APGRAPKAGS ETIIAAAFAS LLGCDVQDAD ADFFALGGHS LLAMKLAAQL
SRQFARQVTP GQVMVASTVA KLATIIDGEE DSSRRMGFET ILPLREGNGP TLFCFHPASG
FAWQFSVLSR YLDPQWSIIG IQSPRPHGPM QTATNLDEVC EAHLATLLEQ QPHGIAARLR
ARGEQVAFLG LLDTWPPETQ NWQEKEANGL DPEVLAEINR EREAFLAAQQ GSTSTELFTT
IEGNYADAVR LLTTAHSVPF DGKATLFVAE RTLQEGMSPE RAWSPWIAEL DIYRQDCAHV
DIISPGAFVK IGPIIRATLN R
