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P11454

- ENTF_ECOLI

UniProt

P11454 - ENTF_ECOLI

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Protein

Enterobactin synthase component F

Gene
entF, b0586, JW0578
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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)serine Inferred

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.

Miscellaneous databases

EvolutionaryTraceiP11454.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini976 – 104368Acyl carrierAdd
BLAST

Region

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

Sequence similaritiesi

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.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti441 – 4422QL → HV in AAA92015. 1 Publication

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

« Hide 'large scale' publications
  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: June 11, 2014
This is version 146 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

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