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P11454 (ENTF_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Enterobactin synthase component F

EC=2.7.7.-
Alternative name(s):
Enterochelin synthase F
Serine-activating enzyme
Seryl-AMP ligase
Gene names
Name:entF
Ordered Locus Names:b0586, JW0578
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length1293 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Cofactor

Binds 1 phosphopantetheine covalently.

Pathway

Siderophore biosynthesis; enterobactin biosynthesis.

Subunit structure

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

Induction

Transcriptionally regulated by iron and the fur protein.

Post-translational modification

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.

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family. EntF subfamily.

Contains 1 acyl carrier domain.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12931293Enterobactin synthase component F
PRO_0000193077

Regions

Domain976 – 104368Acyl carrier
Region1 – 301301Elongation/condensation
Region482 – 887406Adenylation
Region1066 – 1293228Thioesterase

Amino acid modifications

Modified residue10061O-(pantetheine 4'-phosphoryl)serine Probable

Experimental info

Mutagenesis11381S → A: No enterobactin synthase activity. This mutant holo-EntF is still able to adenylate serine and to autoacylate itself with serine. Ref.8
Sequence conflict441 – 4422QL → HV in AAA92015. Ref.1

Secondary structure

.......................................................... 1293
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11454 [UniParc].

Last modified November 1, 1997. Version 3.
Checksum: F3FCBD3836A39358

FASTA1,293141,991
        10         20         30         40         50         60 
MSQHLPLVAA QPGIWMAEKL SELPSAWSVA HYVELTGEVD SPLLARAVVA GLAQADTLRM 

        70         80         90        100        110        120 
RFTEDNGEVW QWVDDALTFE LPEIIDLRTN IDPHGTAQAL MQADLQQDLR VDSGKPLVFH 

       130        140        150        160        170        180 
QLIQVADNRW YWYQRYHHLL VDGFSFPAIT RQIANIYCTW LRGEPTPASP FTPFADVVEE 

       190        200        210        220        230        240 
YQQYRESEAW QRDAAFWAEQ RRQLPPPASL SPAPLPGRSA SADILRLKLE FTDGEFRQLA 

       250        260        270        280        290        300 
TQLSGVQRTD LALALAALWL GRLCNRMDYA AGFIFMRRLG SAALTATGPV LNVLPLGIHI 

       310        320        330        340        350        360 
AAQETLPELA TRLAAQLKKM RRHQRYDAEQ IVRDSGRAAG DEPLFGPVLN IKVFDYQLDI 

       370        380        390        400        410        420 
PDVQAQTHTL ATGPVNDLEL ALFPDVHGDL SIEILANKQR YDEPTLIQHA ERLKMLIAQF 

       430        440        450        460        470        480 
AADPALLCGD VDIMLPGEYA QLAQLNATQV EIPETTLSAL VAEQAAKTPD APALADARYL 

       490        500        510        520        530        540 
FSYREMREQV VALANLLRER GVKPGDSVAV ALPRSVFLTL ALHAIVEAGA AWLPLDTGYP 

       550        560        570        580        590        600 
DDRLKMMLED ARPSLLITTD DQLPRFSDVP NLTSLCYNAP LTPQGSAPLQ LSQPHHTAYI 

       610        620        630        640        650        660 
IFTSGSTGRP KGVMVGQTAI VNRLLWMQNH YPLTGEDVVA QKTPCSFDVS VWEFFWPFIA 

       670        680        690        700        710        720 
GAKLVMAEPE AHRDPLAMQQ FFAEYGVTTT HFVPSMLAAF VASLTPQTAR QSCATLKQVF 

       730        740        750        760        770        780 
CSGEALPADL CREWQQLTGA PLHNLYGPTE AAVDVSWYPA FGEELAQVRG SSVPIGYPVW 

       790        800        810        820        830        840 
NTGLRILDAM MHPVPPGVAG DLYLTGIQLA QGYLGRPDLT ASRFIADPFA PGERMYRTGD 

       850        860        870        880        890        900 
VARWLDNGAV EYLGRSDDQL KIRGQRIELG EIDRVMQALP DVEQAVTHAC VINQAAATGG 

       910        920        930        940        950        960 
DARQLVGYLV SQSGLPLDTS ALQAQLRETL PPHMVPVVLL QLPQLPLSAN GKLDRKALPL 

       970        980        990       1000       1010       1020 
PELKAQAPGR APKAGSETII AAAFSSLLGC DVQDADADFF ALGGHSLLAM KLAAQLSRQV 

      1030       1040       1050       1060       1070       1080 
ARQVTPGQVM VASTVAKLAT IIDAEEDSTR RMGFETILPL REGNGPTLFC FHPASGFAWQ 

      1090       1100       1110       1120       1130       1140 
FSVLSRYLDP QWSIIGIQSP RPNGPMQTAA NLDEVCEAHL ATLLEQQPHG PYYLLGYSLG 

      1150       1160       1170       1180       1190       1200 
GTLAQGIAAR LRARGEQVAF LGLLDTWPPE TQNWQEKEAN GLDPEVLAEI NREREAFLAA 

      1210       1220       1230       1240       1250       1260 
QQGSTSTELF TTIEGNYADA VRLLTTAHSV PFDGKATLFV AERTLQEGMS PERAWSPWIA 

      1270       1280       1290 
ELDIYRQDCA HVDIISPGTF EKIGPIIRAT LNR 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRYGECEF. H64791.
RefSeqNP_415118.1. NC_000913.3.
YP_488875.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ROQNMR-A960-1293[»]
3TEJX-ray1.90A/B965-1293[»]
ProteinModelPortalP11454.
SMRP11454. Positions 7-1293.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9516N.
IntActP11454. 10 interactions.
STRING511145.b0586.

Proteomic databases

PaxDbP11454.
PRIDEP11454.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73687; AAC73687; b0586.
BAE76341; BAE76341; BAE76341.
GeneID12930901.
945184.
KEGGecj:Y75_p0575.
eco:b0586.
PATRIC32116346. VBIEscCol129921_0613.

Organism-specific databases

EchoBASEEB0260.
EcoGeneEG10264. entF.

Phylogenomic databases

eggNOGCOG3319.
HOGENOMHOG000229993.
KOK02364.
OMAINLHATE.
OrthoDBEOG6QP0WP.
PhylomeDBP11454.

Enzyme and pathway databases

BioCycEcoCyc:ENTF-MONOMER.
ECOL316407:JW0578-MONOMER.
MetaCyc:ENTF-MONOMER.
UniPathwayUPA00017.

Gene expression databases

GenevestigatorP11454.

Family and domain databases

Gene3D1.10.1200.10. 1 hit.
3.40.50.1820. 2 hits.
InterProIPR010071. 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]
PfamPF00501. 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]
SUPFAMSSF47336. SSF47336. 1 hit.
SSF53474. SSF53474. 1 hit.
TIGRFAMsTIGR01733. AA-adenyl-dom. 1 hit.
PROSITEPS50075. ACP_DOMAIN. 1 hit.
PS00455. AMP_BINDING. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP11454.
PROP11454.

Entry information

Entry nameENTF_ECOLI
AccessionPrimary (citable) accession number: P11454
Secondary accession number(s): P75723, P77095, Q2MBL5
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene