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P11454

- ENTF_ECOLI

UniProt

P11454 - ENTF_ECOLI

Protein

Enterobactin synthase component F

Gene

entF

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 3 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Activates the carboxylate group of L-serine via ATP-dependent PPi exchange reactions to the aminoacyladenylate, preparing that molecule for the final stages of enterobactin synthesis. Holo-EntF acts as the catalyst for the formation of the three amide and three ester bonds present in the cyclic (2,3-dihydroxybenzoyl)serine trimer enterobactin, using seryladenylate and acyl-holo-EntB (acylated with 2,3-dihydroxybenzoate by EntE).

    Catalytic activityi

    ATP + L-serine = diphosphate + L-serine-adenylate.

    Cofactori

    Binds 1 phosphopantetheine covalently.

    Pathwayi

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. hydrolase activity, acting on ester bonds Source: InterPro
    3. ligase activity Source: UniProtKB-KW
    4. phosphopantetheine binding Source: EcoCyc
    5. transferase activity Source: UniProtKB-KW

    GO - Biological processi

    1. amino acid activation for nonribosomal peptide biosynthetic process Source: EcoCyc
    2. enterobactin biosynthetic process Source: EcoCyc

    Keywords - Molecular functioni

    Ligase, Transferase

    Keywords - Biological processi

    Enterobactin biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:ENTF-MONOMER.
    ECOL316407:JW0578-MONOMER.
    MetaCyc:ENTF-MONOMER.
    UniPathwayiUPA00017.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Enterobactin synthase component F (EC:2.7.7.-)
    Alternative name(s):
    Enterochelin synthase F
    Serine-activating enzyme
    Seryl-AMP ligase
    Gene namesi
    Name:entF
    Ordered Locus Names:b0586, JW0578
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10264. entF.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: EcoCyc
    2. enterobactin synthetase complex Source: EcoCyc
    3. plasma membrane Source: EcoCyc

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1138 – 11381S → A: No enterobactin synthase activity. This mutant holo-EntF is still able to adenylate serine and to autoacylate itself with serine. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12931293Enterobactin synthase component FPRO_0000193077Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1006 – 10061O-(pantetheine 4'-phosphoryl)serineCurated

    Post-translational modificationi

    4'-phosphopantetheine is transferred from CoA to a specific serine of apo-EntF by EntD. Holo-EntF so formed is then acylated with seryl-AMP.

    Keywords - PTMi

    Phosphopantetheine, Phosphoprotein

    Proteomic databases

    PaxDbiP11454.
    PRIDEiP11454.

    Expressioni

    Inductioni

    Transcriptionally regulated by iron and the fur protein.

    Gene expression databases

    GenevestigatoriP11454.

    Interactioni

    Subunit structurei

    EntB, EntD, EntE, and EntF form a multienzyme complex called enterobactin synthase. EntF acts as a catalytic monomer.

    Protein-protein interaction databases

    DIPiDIP-9516N.
    IntActiP11454. 10 interactions.
    STRINGi511145.b0586.

    Structurei

    Secondary structure

    1
    1293
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi968 – 9714
    Helixi976 – 98813
    Turni999 – 10035
    Helixi1006 – 102015
    Helixi1026 – 10316
    Helixi1035 – 10439
    Turni1050 – 10534
    Beta strandi1054 – 10618
    Beta strandi1063 – 10653
    Beta strandi1067 – 10715
    Helixi1079 – 10868
    Beta strandi1093 – 10975
    Turni1101 – 11033
    Helixi1105 – 11084
    Helixi1112 – 112615
    Beta strandi1128 – 11303
    Beta strandi1132 – 11376
    Helixi1139 – 115315
    Beta strandi1158 – 11658
    Helixi1170 – 11734
    Helixi1174 – 11807
    Helixi1186 – 119914
    Turni1200 – 12023
    Helixi1208 – 122417
    Beta strandi1232 – 124110
    Helixi1242 – 12443
    Helixi1251 – 12555
    Turni1256 – 12583
    Beta strandi1259 – 126911
    Helixi1271 – 12755
    Turni1277 – 12793
    Helixi1280 – 129112

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ROQNMR-A960-1293[»]
    3TEJX-ray1.90A/B965-1293[»]
    ProteinModelPortaliP11454.
    SMRiP11454. Positions 7-1293.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11454.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini976 – 104368Acyl carrierPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 301301Elongation/condensationAdd
    BLAST
    Regioni482 – 887406AdenylationAdd
    BLAST
    Regioni1066 – 1293228ThioesteraseAdd
    BLAST

    Sequence similaritiesi

    Contains 1 acyl carrier domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG3319.
    HOGENOMiHOG000229993.
    KOiK02364.
    OMAiINLHATE.
    OrthoDBiEOG6QP0WP.
    PhylomeDBiP11454.

    Family and domain databases

    Gene3Di1.10.1200.10. 1 hit.
    3.40.50.1820. 2 hits.
    InterProiIPR010071. AA_adenyl_domain.
    IPR029058. AB_hydrolase.
    IPR009081. Acyl_carrier_prot-like.
    IPR025110. AMP-bd_C.
    IPR020845. AMP-binding_CS.
    IPR000873. AMP-dep_Synth/Lig.
    IPR001242. Condensatn.
    IPR006162. PPantetheine_attach_site.
    IPR001031. Thioesterase.
    [Graphical view]
    PfamiPF00501. AMP-binding. 1 hit.
    PF13193. AMP-binding_C. 1 hit.
    PF00668. Condensation. 1 hit.
    PF00550. PP-binding. 1 hit.
    PF00975. Thioesterase. 1 hit.
    [Graphical view]
    SUPFAMiSSF47336. SSF47336. 1 hit.
    SSF53474. SSF53474. 1 hit.
    TIGRFAMsiTIGR01733. AA-adenyl-dom. 1 hit.
    PROSITEiPS50075. ACP_DOMAIN. 1 hit.
    PS00455. AMP_BINDING. 1 hit.
    PS00012. PHOSPHOPANTETHEINE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P11454-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSQHLPLVAA QPGIWMAEKL SELPSAWSVA HYVELTGEVD SPLLARAVVA     50
    GLAQADTLRM RFTEDNGEVW QWVDDALTFE LPEIIDLRTN IDPHGTAQAL 100
    MQADLQQDLR VDSGKPLVFH QLIQVADNRW YWYQRYHHLL VDGFSFPAIT 150
    RQIANIYCTW LRGEPTPASP FTPFADVVEE YQQYRESEAW QRDAAFWAEQ 200
    RRQLPPPASL SPAPLPGRSA SADILRLKLE FTDGEFRQLA TQLSGVQRTD 250
    LALALAALWL GRLCNRMDYA AGFIFMRRLG SAALTATGPV LNVLPLGIHI 300
    AAQETLPELA TRLAAQLKKM RRHQRYDAEQ IVRDSGRAAG DEPLFGPVLN 350
    IKVFDYQLDI PDVQAQTHTL ATGPVNDLEL ALFPDVHGDL SIEILANKQR 400
    YDEPTLIQHA ERLKMLIAQF AADPALLCGD VDIMLPGEYA QLAQLNATQV 450
    EIPETTLSAL VAEQAAKTPD APALADARYL FSYREMREQV VALANLLRER 500
    GVKPGDSVAV ALPRSVFLTL ALHAIVEAGA AWLPLDTGYP DDRLKMMLED 550
    ARPSLLITTD DQLPRFSDVP NLTSLCYNAP LTPQGSAPLQ LSQPHHTAYI 600
    IFTSGSTGRP KGVMVGQTAI VNRLLWMQNH YPLTGEDVVA QKTPCSFDVS 650
    VWEFFWPFIA GAKLVMAEPE AHRDPLAMQQ FFAEYGVTTT HFVPSMLAAF 700
    VASLTPQTAR QSCATLKQVF CSGEALPADL CREWQQLTGA PLHNLYGPTE 750
    AAVDVSWYPA FGEELAQVRG SSVPIGYPVW NTGLRILDAM MHPVPPGVAG 800
    DLYLTGIQLA QGYLGRPDLT ASRFIADPFA PGERMYRTGD VARWLDNGAV 850
    EYLGRSDDQL KIRGQRIELG EIDRVMQALP DVEQAVTHAC VINQAAATGG 900
    DARQLVGYLV SQSGLPLDTS ALQAQLRETL PPHMVPVVLL QLPQLPLSAN 950
    GKLDRKALPL PELKAQAPGR APKAGSETII AAAFSSLLGC DVQDADADFF 1000
    ALGGHSLLAM KLAAQLSRQV ARQVTPGQVM VASTVAKLAT IIDAEEDSTR 1050
    RMGFETILPL REGNGPTLFC FHPASGFAWQ FSVLSRYLDP QWSIIGIQSP 1100
    RPNGPMQTAA NLDEVCEAHL ATLLEQQPHG PYYLLGYSLG GTLAQGIAAR 1150
    LRARGEQVAF LGLLDTWPPE TQNWQEKEAN GLDPEVLAEI NREREAFLAA 1200
    QQGSTSTELF TTIEGNYADA VRLLTTAHSV PFDGKATLFV AERTLQEGMS 1250
    PERAWSPWIA ELDIYRQDCA HVDIISPGTF EKIGPIIRAT LNR 1293
    Length:1,293
    Mass (Da):141,991
    Last modified:November 1, 1997 - v3
    Checksum:iF3FCBD3836A39358
    GO

    Sequence cautioni

    The sequence AAB40785.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti441 – 4422QL → HV in AAA92015. (PubMed:1826089)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M60177 Genomic DNA. Translation: AAA92015.1.
    U82598 Genomic DNA. Translation: AAB40785.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC73687.1.
    AP009048 Genomic DNA. Translation: BAE76341.1.
    M17354 Genomic DNA. Translation: AAA23727.1.
    J04216 Genomic DNA. Translation: AAA23759.1.
    PIRiH64791. YGECEF.
    RefSeqiNP_415118.1. NC_000913.3.
    YP_488875.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73687; AAC73687; b0586.
    BAE76341; BAE76341; BAE76341.
    GeneIDi12930901.
    945184.
    KEGGiecj:Y75_p0575.
    eco:b0586.
    PATRICi32116346. VBIEscCol129921_0613.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M60177 Genomic DNA. Translation: AAA92015.1 .
    U82598 Genomic DNA. Translation: AAB40785.1 . Different initiation.
    U00096 Genomic DNA. Translation: AAC73687.1 .
    AP009048 Genomic DNA. Translation: BAE76341.1 .
    M17354 Genomic DNA. Translation: AAA23727.1 .
    J04216 Genomic DNA. Translation: AAA23759.1 .
    PIRi H64791. YGECEF.
    RefSeqi NP_415118.1. NC_000913.3.
    YP_488875.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2ROQ NMR - A 960-1293 [» ]
    3TEJ X-ray 1.90 A/B 965-1293 [» ]
    ProteinModelPortali P11454.
    SMRi P11454. Positions 7-1293.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-9516N.
    IntActi P11454. 10 interactions.
    STRINGi 511145.b0586.

    Proteomic databases

    PaxDbi P11454.
    PRIDEi P11454.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73687 ; AAC73687 ; b0586 .
    BAE76341 ; BAE76341 ; BAE76341 .
    GeneIDi 12930901.
    945184.
    KEGGi ecj:Y75_p0575.
    eco:b0586.
    PATRICi 32116346. VBIEscCol129921_0613.

    Organism-specific databases

    EchoBASEi EB0260.
    EcoGenei EG10264. entF.

    Phylogenomic databases

    eggNOGi COG3319.
    HOGENOMi HOG000229993.
    KOi K02364.
    OMAi INLHATE.
    OrthoDBi EOG6QP0WP.
    PhylomeDBi P11454.

    Enzyme and pathway databases

    UniPathwayi UPA00017 .
    BioCyci EcoCyc:ENTF-MONOMER.
    ECOL316407:JW0578-MONOMER.
    MetaCyc:ENTF-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P11454.
    PROi P11454.

    Gene expression databases

    Genevestigatori P11454.

    Family and domain databases

    Gene3Di 1.10.1200.10. 1 hit.
    3.40.50.1820. 2 hits.
    InterProi IPR010071. AA_adenyl_domain.
    IPR029058. AB_hydrolase.
    IPR009081. Acyl_carrier_prot-like.
    IPR025110. AMP-bd_C.
    IPR020845. AMP-binding_CS.
    IPR000873. AMP-dep_Synth/Lig.
    IPR001242. Condensatn.
    IPR006162. PPantetheine_attach_site.
    IPR001031. Thioesterase.
    [Graphical view ]
    Pfami PF00501. AMP-binding. 1 hit.
    PF13193. AMP-binding_C. 1 hit.
    PF00668. Condensation. 1 hit.
    PF00550. PP-binding. 1 hit.
    PF00975. Thioesterase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47336. SSF47336. 1 hit.
    SSF53474. SSF53474. 1 hit.
    TIGRFAMsi TIGR01733. AA-adenyl-dom. 1 hit.
    PROSITEi PS50075. ACP_DOMAIN. 1 hit.
    PS00455. AMP_BINDING. 1 hit.
    PS00012. PHOSPHOPANTETHEINE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Biosynthesis of the Escherichia coli siderophore enterobactin: sequence of the entF gene, expression and purification of EntF, and analysis of covalent phosphopantetheine."
      Rusnak F., Sakaitani M., Drueckhammer D., Reichert J., Walsh C.T.
      Biochemistry 30:2916-2927(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-12.
      Strain: K12.
    2. "Sequence of minutes 4-25 of Escherichia coli."
      Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "Molecular characterization of the Escherichia coli enterobactin cistron entF and coupled expression of entF and the fes gene."
      Pettis G.S., McIntosh M.A.
      J. Bacteriol. 169:4154-4162(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
    6. "Transcriptional mapping and nucleotide sequence of the Escherichia coli fepA-fes enterobactin region. Identification of a unique iron-regulated bidirectional promoter."
      Pettis G.S., Brickman T.J., McIntosh M.A.
      J. Biol. Chem. 263:18857-18863(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34, PROTEIN SEQUENCE OF 1-12.
    7. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    8. "Reconstitution and characterization of the Escherichia coli enterobactin synthetase from EntB, EntE, and EntF."
      Gehring A.M., Mori I., Walsh C.T.
      Biochemistry 37:2648-2659(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF SER-1138.

    Entry informationi

    Entry nameiENTF_ECOLI
    AccessioniPrimary (citable) accession number: P11454
    Secondary accession number(s): P75723, P77095, Q2MBL5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 147 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3