(data stored in ACNUC7421 zone)

SWISSPROT: 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   05-JUL-2017, entry version 116.
DE   RecName: Full=Enterobactin synthase component F;
DE            EC=2.7.7.-;
DE   AltName: Full=Enterochelin synthase F;
DE   AltName: Full=Serine-activating enzyme;
DE   AltName: Full=Seryl-AMP ligase;
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.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., 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.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Activates the carboxylate group of L-serine via ATP-
CC       dependent PPi exchange reactions to the aminoacyladenylate,
CC       preparing that molecule for the final stages of enterobactin
CC       synthesis. Holo-EntF acts as the catalyst for the formation of the
CC       three amide and three ester bonds present in the cyclic (2,3-
CC       dihydroxybenzoyl)serine trimer enterobactin, using seryladenylate
CC       and acyl-holo-EntB (acylated with 2,3-dihydroxybenzoate by EntE)
CC       (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-serine = diphosphate + L-serine-
CC       adenylate.
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 phosphopantetheine covalently. {ECO:0000250};
CC   -!- PATHWAY: Siderophore biosynthesis; enterobactin biosynthesis.
CC   -!- SUBUNIT: EntB, EntD, EntE, and EntF form a multienzyme complex
CC       called enterobactin synthase. EntF acts as a catalytic monomer (By
CC       similarity). {ECO:0000250}.
CC   -!- PTM: 4'-phosphopantetheine is transferred from CoA to a specific
CC       serine of apo-EntF by EntD. Holo-EntF so formed is then acylated
CC       with seryl-AMP (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC       family. EntF subfamily. {ECO:0000305}.
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_MWVM01000011.1.
DR   ProteinModelPortal; Q8XBV9; -.
DR   SMR; Q8XBV9; -.
DR   STRING; 155864.Z0727; -.
DR   ESTHER; ecoli-entf; Thioesterase.
DR   PRIDE; Q8XBV9; -.
DR   EnsemblBacteria; AAG54921; AAG54921; Z0727.
DR   EnsemblBacteria; BAB34048; BAB34048; BAB34048.
DR   GeneID; 916984; -.
DR   KEGG; ece:Z0727; -.
DR   KEGG; ecs:ECs0625; -.
DR   PATRIC; fig|386585.9.peg.735; -.
DR   eggNOG; ENOG4105C0W; Bacteria.
DR   eggNOG; COG1020; LUCA.
DR   eggNOG; COG3319; LUCA.
DR   HOGENOM; HOG000229993; -.
DR   KO; K02364; -.
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:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
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; 3.40.50.1820; -; 1.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
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;
DR   PRODOM; Q8XBV9.
DR   SWISS-2DPAGE; Q8XBV9.
KW   ATP-binding; Complete proteome; Enterobactin biosynthesis; Ligase;
KW   Multifunctional enzyme; Nucleotide-binding; Phosphopantetheine;
KW   Phosphoprotein; Transferase.
FT   CHAIN         1   1293       Enterobactin synthase component F.
FT                                /FTId=PRO_0000193078.
FT   DOMAIN      971   1046       Carrier. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00258}.
FT   REGION        1    301       Elongation/condensation.
FT   REGION      482    887       Adenylation.
FT   REGION     1066   1293       Thioesterase.
FT   MOD_RES    1006   1006       O-(pantetheine 4'-phosphoryl)serine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00258}.
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
//

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