Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Enterobactin synthase component F

Gene

entF

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: 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

pantetheine 4'-phosphateNote: Binds 1 phosphopantetheine covalently.

Pathwayi: enterobactin biosynthesis

This protein is involved in the pathway enterobactin biosynthesis, which is part of Siderophore biosynthesis.
View all proteins of this organism that are known to be involved in the pathway enterobactin biosynthesis and in Siderophore biosynthesis.

GO - Molecular functioni

  • 2,3-dihydroxybenzoate-serine ligase activity Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • hydrolase activity, acting on ester bonds Source: InterPro
  • nucleotidyltransferase activity Source: UniProtKB
  • phosphopantetheine binding Source: EcoCyc

GO - Biological processi

  • amino acid activation for nonribosomal peptide biosynthetic process Source: EcoCyc
  • 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.
BRENDAi6.3.2.14. 2026.
UniPathwayiUPA00017.

Protein family/group databases

ESTHERiecoli-entf. Thioesterase.

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10264. entF.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • enterobactin synthetase complex Source: EcoCyc
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1138S → A: No enterobactin synthase activity. This mutant holo-EntF is still able to adenylate serine and to autoacylate itself with serine. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001930771 – 1293Enterobactin synthase component FAdd BLAST1293

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1006O-(pantetheine 4'-phosphoryl)serineCurated1

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

EPDiP11454.
PaxDbiP11454.
PRIDEiP11454.

Expressioni

Inductioni

Transcriptionally regulated by iron and the fur protein.

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

BioGridi4259895. 295 interactors.
DIPiDIP-9516N.
IntActiP11454. 10 interactors.
STRINGi511145.b0586.

Structurei

Secondary structure

11293
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi11 – 20Combined sources10
Beta strandi23 – 25Combined sources3
Beta strandi28 – 37Combined sources10
Helixi41 – 54Combined sources14
Helixi56 – 59Combined sources4
Beta strandi60 – 65Combined sources6
Beta strandi68 – 73Combined sources6
Beta strandi83 – 85Combined sources3
Beta strandi88 – 92Combined sources5
Helixi95 – 104Combined sources10
Helixi111 – 113Combined sources3
Beta strandi117 – 123Combined sources7
Beta strandi126 – 128Combined sources3
Beta strandi130 – 137Combined sources8
Turni138 – 140Combined sources3
Turni143 – 145Combined sources3
Helixi146 – 161Combined sources16
Helixi174 – 185Combined sources12
Helixi188 – 203Combined sources16
Beta strandi210 – 213Combined sources4
Beta strandi224 – 231Combined sources8
Helixi235 – 243Combined sources9
Helixi249 – 264Combined sources16
Beta strandi267 – 275Combined sources9
Helixi282 – 285Combined sources4
Beta strandi292 – 299Combined sources8
Helixi306 – 322Combined sources17
Turni323 – 325Combined sources3
Helixi328 – 334Combined sources7
Beta strandi346 – 350Combined sources5
Beta strandi367 – 371Combined sources5
Beta strandi376 – 384Combined sources9
Beta strandi390 – 397Combined sources8
Turni398 – 400Combined sources3
Helixi403 – 422Combined sources20
Helixi428 – 430Combined sources3
Helixi438 – 445Combined sources8
Helixi457 – 467Combined sources11
Beta strandi471 – 475Combined sources5
Beta strandi480 – 482Combined sources3
Helixi483 – 499Combined sources17
Beta strandi507 – 510Combined sources4
Helixi516 – 527Combined sources12
Beta strandi531 – 534Combined sources4
Helixi541 – 551Combined sources11
Beta strandi554 – 558Combined sources5
Turni560 – 564Combined sources5
Helixi565 – 568Combined sources4
Beta strandi569 – 571Combined sources3
Beta strandi574 – 576Combined sources3
Beta strandi596 – 603Combined sources8
Turni606 – 608Combined sources3
Beta strandi611 – 616Combined sources6
Helixi617 – 630Combined sources14
Beta strandi638 – 641Combined sources4
Helixi650 – 660Combined sources11
Beta strandi663 – 666Combined sources4
Helixi671 – 673Combined sources3
Helixi675 – 684Combined sources10
Beta strandi689 – 692Combined sources4
Helixi694 – 702Combined sources9
Helixi706 – 712Combined sources7
Helixi713 – 715Combined sources3
Beta strandi718 – 724Combined sources7
Helixi728 – 738Combined sources11
Beta strandi742 – 746Combined sources5
Beta strandi751 – 753Combined sources3
Beta strandi755 – 759Combined sources5
Helixi762 – 766Combined sources5
Beta strandi770 – 772Combined sources3
Beta strandi776 – 778Combined sources3
Beta strandi782 – 787Combined sources6
Beta strandi800 – 806Combined sources7
Beta strandi811 – 814Combined sources4
Helixi817 – 823Combined sources7
Beta strandi824 – 826Combined sources3
Beta strandi834 – 844Combined sources11
Beta strandi850 – 862Combined sources13
Beta strandi865 – 868Combined sources4
Helixi869 – 877Combined sources9
Beta strandi882 – 890Combined sources9
Helixi894 – 896Combined sources3
Beta strandi898 – 900Combined sources3
Beta strandi904 – 915Combined sources12
Helixi919 – 929Combined sources11
Helixi932 – 934Combined sources3
Beta strandi937 – 941Combined sources5
Beta strandi951 – 953Combined sources3
Helixi955 – 957Combined sources3
Beta strandi968 – 971Combined sources4
Helixi976 – 988Combined sources13
Beta strandi994 – 996Combined sources3
Turni999 – 1003Combined sources5
Helixi1006 – 1020Combined sources15
Helixi1026 – 1031Combined sources6
Helixi1035 – 1043Combined sources9
Turni1050 – 1053Combined sources4
Beta strandi1054 – 1061Combined sources8
Beta strandi1063 – 1065Combined sources3
Beta strandi1067 – 1071Combined sources5
Helixi1079 – 1086Combined sources8
Beta strandi1093 – 1097Combined sources5
Turni1101 – 1103Combined sources3
Helixi1105 – 1108Combined sources4
Helixi1112 – 1126Combined sources15
Beta strandi1128 – 1130Combined sources3
Beta strandi1132 – 1137Combined sources6
Helixi1139 – 1153Combined sources15
Beta strandi1158 – 1165Combined sources8
Helixi1170 – 1173Combined sources4
Helixi1174 – 1180Combined sources7
Helixi1186 – 1199Combined sources14
Turni1200 – 1203Combined sources4
Helixi1208 – 1224Combined sources17
Beta strandi1232 – 1241Combined sources10
Helixi1242 – 1244Combined sources3
Turni1248 – 1250Combined sources3
Helixi1251 – 1255Combined sources5
Turni1256 – 1258Combined sources3
Beta strandi1259 – 1269Combined sources11
Helixi1271 – 1275Combined sources5
Turni1277 – 1279Combined sources3
Helixi1280 – 1291Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2ROQNMR-A960-1293[»]
3TEJX-ray1.90A/B965-1293[»]
5JA1X-ray3.00A1-1293[»]
5JA2X-ray3.00A1-1293[»]
5T3DX-ray2.80A1-1293[»]
ProteinModelPortaliP11454.
SMRiP11454.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11454.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini976 – 1043Acyl carrierPROSITE-ProRule annotationAdd BLAST68

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 301Elongation/condensationAdd BLAST301
Regioni482 – 887AdenylationAdd BLAST406
Regioni1066 – 1293ThioesteraseAdd BLAST228

Sequence similaritiesi

Contains 1 acyl carrier domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105C0W. Bacteria.
COG1020. LUCA.
COG3319. LUCA.
HOGENOMiHOG000229993.
InParanoidiP11454.
KOiK02364.
OMAiFSVLARY.
PhylomeDBiP11454.

Family and domain databases

Gene3Di1.10.1200.10. 1 hit.
3.40.50.1820. 2 hits.
InterProiIPR010071. AA_adenyl_domain.
IPR029058. AB_hydrolase.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR001242. Condensatn.
IPR020806. PKS_PP-bd.
IPR020802. PKS_thioesterase.
IPR009081. PP-bd_ACP.
IPR006162. Ppantetheine_attach_site.
IPR001031. Thioesterase.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF00668. Condensation. 1 hit.
PF00550. PP-binding. 1 hit.
PF00975. Thioesterase. 1 hit.
[Graphical view]
SMARTiSM00823. PKS_PP. 1 hit.
SM00824. PKS_TE. 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

        10         20         30         40         50
MSQHLPLVAA QPGIWMAEKL SELPSAWSVA HYVELTGEVD SPLLARAVVA
60 70 80 90 100
GLAQADTLRM RFTEDNGEVW QWVDDALTFE LPEIIDLRTN IDPHGTAQAL
110 120 130 140 150
MQADLQQDLR VDSGKPLVFH QLIQVADNRW YWYQRYHHLL VDGFSFPAIT
160 170 180 190 200
RQIANIYCTW LRGEPTPASP FTPFADVVEE YQQYRESEAW QRDAAFWAEQ
210 220 230 240 250
RRQLPPPASL SPAPLPGRSA SADILRLKLE FTDGEFRQLA TQLSGVQRTD
260 270 280 290 300
LALALAALWL GRLCNRMDYA AGFIFMRRLG SAALTATGPV LNVLPLGIHI
310 320 330 340 350
AAQETLPELA TRLAAQLKKM RRHQRYDAEQ IVRDSGRAAG DEPLFGPVLN
360 370 380 390 400
IKVFDYQLDI PDVQAQTHTL ATGPVNDLEL ALFPDVHGDL SIEILANKQR
410 420 430 440 450
YDEPTLIQHA ERLKMLIAQF AADPALLCGD VDIMLPGEYA QLAQLNATQV
460 470 480 490 500
EIPETTLSAL VAEQAAKTPD APALADARYL FSYREMREQV VALANLLRER
510 520 530 540 550
GVKPGDSVAV ALPRSVFLTL ALHAIVEAGA AWLPLDTGYP DDRLKMMLED
560 570 580 590 600
ARPSLLITTD DQLPRFSDVP NLTSLCYNAP LTPQGSAPLQ LSQPHHTAYI
610 620 630 640 650
IFTSGSTGRP KGVMVGQTAI VNRLLWMQNH YPLTGEDVVA QKTPCSFDVS
660 670 680 690 700
VWEFFWPFIA GAKLVMAEPE AHRDPLAMQQ FFAEYGVTTT HFVPSMLAAF
710 720 730 740 750
VASLTPQTAR QSCATLKQVF CSGEALPADL CREWQQLTGA PLHNLYGPTE
760 770 780 790 800
AAVDVSWYPA FGEELAQVRG SSVPIGYPVW NTGLRILDAM MHPVPPGVAG
810 820 830 840 850
DLYLTGIQLA QGYLGRPDLT ASRFIADPFA PGERMYRTGD VARWLDNGAV
860 870 880 890 900
EYLGRSDDQL KIRGQRIELG EIDRVMQALP DVEQAVTHAC VINQAAATGG
910 920 930 940 950
DARQLVGYLV SQSGLPLDTS ALQAQLRETL PPHMVPVVLL QLPQLPLSAN
960 970 980 990 1000
GKLDRKALPL PELKAQAPGR APKAGSETII AAAFSSLLGC DVQDADADFF
1010 1020 1030 1040 1050
ALGGHSLLAM KLAAQLSRQV ARQVTPGQVM VASTVAKLAT IIDAEEDSTR
1060 1070 1080 1090 1100
RMGFETILPL REGNGPTLFC FHPASGFAWQ FSVLSRYLDP QWSIIGIQSP
1110 1120 1130 1140 1150
RPNGPMQTAA NLDEVCEAHL ATLLEQQPHG PYYLLGYSLG GTLAQGIAAR
1160 1170 1180 1190 1200
LRARGEQVAF LGLLDTWPPE TQNWQEKEAN GLDPEVLAEI NREREAFLAA
1210 1220 1230 1240 1250
QQGSTSTELF TTIEGNYADA VRLLTTAHSV PFDGKATLFV AERTLQEGMS
1260 1270 1280 1290
PERAWSPWIA ELDIYRQDCA HVDIISPGTF EKIGPIIRAT LNR
Length:1,293
Mass (Da):141,991
Last modified:November 1, 1997 - v3
Checksum:iF3FCBD3836A39358
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti441 – 442QL → HV in AAA92015 (PubMed:1826089).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_000077805.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73687; AAC73687; b0586.
BAE76341; BAE76341; BAE76341.
GeneIDi945184.
KEGGiecj:JW0578.
eco:b0586.
PATRICi32116346. VBIEscCol129921_0613.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_000077805.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2ROQNMR-A960-1293[»]
3TEJX-ray1.90A/B965-1293[»]
5JA1X-ray3.00A1-1293[»]
5JA2X-ray3.00A1-1293[»]
5T3DX-ray2.80A1-1293[»]
ProteinModelPortaliP11454.
SMRiP11454.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259895. 295 interactors.
DIPiDIP-9516N.
IntActiP11454. 10 interactors.
STRINGi511145.b0586.

Protein family/group databases

ESTHERiecoli-entf. Thioesterase.

Proteomic databases

EPDiP11454.
PaxDbiP11454.
PRIDEiP11454.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73687; AAC73687; b0586.
BAE76341; BAE76341; BAE76341.
GeneIDi945184.
KEGGiecj:JW0578.
eco:b0586.
PATRICi32116346. VBIEscCol129921_0613.

Organism-specific databases

EchoBASEiEB0260.
EcoGeneiEG10264. entF.

Phylogenomic databases

eggNOGiENOG4105C0W. Bacteria.
COG1020. LUCA.
COG3319. LUCA.
HOGENOMiHOG000229993.
InParanoidiP11454.
KOiK02364.
OMAiFSVLARY.
PhylomeDBiP11454.

Enzyme and pathway databases

UniPathwayiUPA00017.
BioCyciEcoCyc:ENTF-MONOMER.
ECOL316407:JW0578-MONOMER.
MetaCyc:ENTF-MONOMER.
BRENDAi6.3.2.14. 2026.

Miscellaneous databases

EvolutionaryTraceiP11454.
PROiP11454.

Family and domain databases

Gene3Di1.10.1200.10. 1 hit.
3.40.50.1820. 2 hits.
InterProiIPR010071. AA_adenyl_domain.
IPR029058. AB_hydrolase.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR001242. Condensatn.
IPR020806. PKS_PP-bd.
IPR020802. PKS_thioesterase.
IPR009081. PP-bd_ACP.
IPR006162. Ppantetheine_attach_site.
IPR001031. Thioesterase.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF00668. Condensation. 1 hit.
PF00550. PP-binding. 1 hit.
PF00975. Thioesterase. 1 hit.
[Graphical view]
SMARTiSM00823. PKS_PP. 1 hit.
SM00824. PKS_TE. 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]
ProtoNetiSearch...

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: November 30, 2016
This is version 165 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.