Enterobactin synthase component F - Escherichia coli (strain K12)

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P11454 (ENTF_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 136. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	1293 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Enterobactin biosynthesis
Ligand	ATP-binding Nucleotide-binding Phosphopantetheine
Molecular function	Ligase Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	amino acid activation for nonribosomal peptide biosynthetic process Inferred from direct assay Ref.1. Source: EcoCyc enterobactin biosynthetic process Inferred from mutant phenotype Ref.8. Source: EcoCyc
Cellular_component	cytosol Inferred from direct assay PubMed 10692387. Source: EcoCyc enterobactin synthetase complex Inferred from direct assay Ref.8. Source: EcoCyc plasma membrane Inferred from direct assay PubMed 10692387. Source: EcoCyc
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW hydrolase activity, acting on ester bonds Inferred from electronic annotation. Source: InterPro ligase activity Inferred from electronic annotation. Source: UniProtKB-KW phosphopantetheine binding Inferred from direct assay PubMed 8939709. Source: EcoCyc transferase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1293

1293

Enterobactin synthase component F

PRO_0000193077

Regions

Domain

976 – 1043

Acyl carrier

Region

1 – 301

301

Elongation/condensation

Region

482 – 887

406

Adenylation

Region

1066 – 1293

228

Thioesterase

Amino acid modifications

Modified residue

1006

O-(pantetheine 4'-phosphoryl)serine Probable

Experimental info

Mutagenesis

1138

S → A: No enterobactin synthase activity. This mutant holo-EntF is still able to adenylate serine and to autoacylate itself with serine. Ref.8

Sequence conflict

441 – 442

QL → HV in AAA92015. Ref.1

Secondary structure

1293

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P11454 [UniParc].

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

FASTA

1,293

141,991

        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' referencesShow '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 277:1453-1474(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.

PIR

YGECEF. H64791.

RefSeq

NP_415118.1. NC_000913.2.
YP_488875.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2ROQ	NMR	-	A	960-1293	[»]
3TEJ	X-ray	1.90	A/B	965-1293	[»]

ProteinModelPortal

P11454.

SMR

P11454. Positions 28-1293.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-9516N.

IntAct

P11454. 7 interactions.

STRING

511145.b0586.

Proteomic databases

PaxDb

P11454.

PRIDE

P11454.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73687; AAC73687; b0586.
BAE76341; BAE76341; BAE76341.

GeneID

12930901.
945184.

KEGG

ecj:Y75_p0575.
eco:b0586.

PATRIC

32116346. VBIEscCol129921_0613.

Organism-specific databases

EchoBASE

EB0260.

EcoGene

EG10264. entF.

Phylogenomic databases

eggNOG

COG3319.

HOGENOM

HOG000229993.

K02364.

OMA

CYNAPLK.

ProtClustDB

PRK10252.

Enzyme and pathway databases

BioCyc

EcoCyc:ENTF-MONOMER.
ECOL316407:JW0578-MONOMER.
MetaCyc:ENTF-MONOMER.

UniPathway

UPA00017.

Gene expression databases

Genevestigator

P11454.

Family and domain databases

Gene3D

1.10.1200.10. 1 hit.

InterPro

IPR010071. AA_adenyl_domain.
IPR009081. Acyl_carrier_prot-like.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR001242. Condensatn.
IPR006162. PPantetheine_attach_site.
IPR001031. Thioesterase.
[Graphical view]

Pfam

PF00501. AMP-binding. 1 hit.
PF00668. Condensation. 1 hit.
PF00550. PP-binding. 1 hit.
PF00975. Thioesterase. 1 hit.
[Graphical view]

SUPFAM

SSF47336. ACP_like. 1 hit.

TIGRFAMs

TIGR01733. AA-adenyl-dom. 1 hit.

PROSITE

PS50075. ACP_DOMAIN. 1 hit.
PS00455. AMP_BINDING. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P11454.

Entry information

Entry name

ENTF_ECOLI

Accession

Primary (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:	May 1, 2013
This is version 136 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents