UniProtKB - P10378 (ENTE_ECOLI)

BLAST

>sp|P10378|ENTE_ECOLI Enterobactin synthase component E OS=Escherichia coli (strain K12) OX=83333 GN=entE PE=1 SV=3
MSIPFTRWPEEFARRYREKGYWQDLPLTDILTRHAASDSIAVIDGERQLSYRELNQAADN
LACSLRRQGIKPGETALVQLGNVAELYITFFALLKLGVAPVLALFSHQRSELNAYASQIE
PALLIADRQHALFSGDDFLNTFVTEHSSIRVVQLLNDSGEHNLQDAINHPAEDFTATPSP
ADEVAYFQLSGGTTGTPKLIPRTHNDYYYSVRRSVEICQFTQQTRYLCAIPAAHNYAMSS
PGSLGVFLAGGTVVLAADPSATLCFPLIEKHQVNVTALVPPAVSLWLQALIEGESRAQLA
SLKLLQVGGARLSATLAARIPAEIGCQLQQVFGMAEGLVNYTRLDDSAEKIIHTQGYPMC
PDDEVWVADAEGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLISID
PEGYITVQGREKDQINRGGEKIAAEEIENLLLRHPAVIYAALVSMEDELMGEKSCAYLVV
KEPLRAVQVRRFLREQGIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWLASRASA

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History
Entry version 158 (07 Nov 2018)
Sequence version 3 (01 Nov 1997)
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Protein

Enterobactin synthase component E

Gene

entE

Organism

Escherichia coli (strain K12)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provide hexadentate coordination for the tightly ligated iron²⁺ atoms. EntE proccesses via a two-step adenylation-ligation reaction (bi-uni-uni-bi ping-pong mechanism). First, it catalyzes the activation of the carboxylate group of 2,3-dihydroxy-benzoate (DHB), via a reversible ATP-dependent pyrophosphate exchange reactions to yield the acyladenylate intermediate 2,3-dihydroxybenzoyl-AMP. It can also transfer AMP to salicylate, 2,4-dihydroxybenzoate, gentisate and 2,3,4-trihydroxybenzoate. In the second step, DHB is transferred from 2,3-dihydroxybenzoyl-AMP onto the phosphopantetheinylated EntB (holo-EntB) to form DHB-holo-EntB. Then this product will serve in the formation of the amide bond between 2,3-dihydroxybenzoate (DHB) and L-serine. It can also transfer adenylated salicylate to holo-EntB.10 Publications

Miscellaneous

In the absence of holo-EntB, EntE can transfer the adenylate moiety of the 2,3-dihydroxybenzoyl-AMP intermediate to ATP, generating the stress signaling molecule Ap4A involved in the regulation of cell division during oxidative stress, and releasing 2,3-dihydroxybenzoate. It seems that the expression of EntE during iron starvation produces Ap₄A to slow growth until intracellular iron stores can be restored.1 Publication

Catalytic activityⁱ

6 ATP + 3 2,3-dihydroxybenzoate + 3 L-serine = enterobactin + 6 AMP + 6 diphosphate.7 Publications

ATP + 2,3-dihydroxybenzoate = diphosphate + (2,3-dihydroxybenzoyl)adenylate.6 Publications

(2,3-dihydroxybenzoyl)adenylate + holo-entB = adenosine 5'-monophosphate + aryl-holo-entB.7 Publications

Activity regulationⁱ

Inhibited by the adenylate analogs, 5'-O-[N-(salicyl)sulfamoyl]adenosine (Sal-AMS) and 5'-O-[N-(2,3-dihydroxybenzoyl)sulfamoyl]adenosine (DHB-AMS). Adenylation of 2,3-dihydroxybenzoate (DHB) is enhanced by a protein-protein interaction between the EntA and EntE.2 Publications

Kineticsⁱ

Kcat is 0.3 sec(-1) for 2,3-dihydroxybenzoate-AMP ligase activity with 3-hydroxybenzoate as substrate (at pH 7.8 and 25 degrees Celsius). Kcat is 0.8 sec(-1) for 2,3-dihydroxybenzoate-AMP ligase activity with salicylate as substrate (at pH 7.8 and 25 degrees Celsius). Kcat is 0.9 sec(-1) for S-dihydroxybenzoyltransferase activity with D-pantetheine as substrate (at pH 7.8 and 25 degrees Celsius). Kcat is 2.8 sec(-1) for 2,3-dihydroxybenzoate-AMP ligase activity with ATP and DHB as substrates (at pH 7.8 and 25 degrees Celsius). Kcat is 2.8 sec(-1) for S-dihydroxybenzoyltransferase activity with holo-EntB as substrate (at pH 7.8 and 25 degrees Celsius). Kcat is 4.4 sec(-1) for 2,3-dihydroxybenzoate-AMP ligase activity with 4-aminosalicylate as substrate (at pH 7.8 and 25 degrees Celsius). Kcat is 5.94 sec(-1) for S-dihydroxybenzoyltransferase activity with holo-EntB as substrate (at pH 7.8 and 25 degrees Celsius). Kcat is 100 min(-1) for S-dihydroxybenzoyltransferase activity with holo-EntB as substrate (at pH 8.8 and 37 degrees Celsius). Kcat is 140 min(-1) for S-dihydroxybenzoyltransferase activity with holo-EntB as substrate.4 Publications

V_max=
3168.2 pmol/min/mg enzyme
1 Publication
Manual assertion based on experiment inⁱ
- Ref.19
  "MbtH-like proteins as integral components of bacterial nonribosomal peptide synthetases."
  Felnagle E.A., Barkei J.J., Park H., Podevels A.M., McMahon M.D., Drott D.W., Thomas M.G.
  Biochemistry 49:8815-8817(2010) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.

Pathwayⁱ: enterobactin biosynthesis

This protein is involved in the pathway enterobactin biosynthesis, which is part of Siderophore biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway enterobactin biosynthesis and in Siderophore biosynthesis.

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	235	Substrate1 Publication	1
Binding siteⁱ	240	Substrate1 Publication	1
Binding siteⁱ	309	Substrate; via amide nitrogen2 Publications	1
Binding siteⁱ	331	Substrate; via carbonyl oxygen2 Publications	1
Binding siteⁱ	335	Substrate; via amide nitrogen1 Publication	1
Binding siteⁱ	415	Substrate2 Publications	1
Binding siteⁱ	432	Substrate1 Publication	1
Binding siteⁱ	441	Substrate1 Publication	1

GO - Molecular functionⁱ

(2,3-dihydroxybenzoyl)adenylate synthase activity
Source: EcoCyc
Inferred from direct assayⁱ
- 2531000
2,3-dihydroxybenzoate-serine ligase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 9485415
ATP binding Source: UniProtKB-KW
transferase activity, transferring acyl groups Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

enterobactin biosynthetic process
Source: EcoCyc
Inferred from mutant phenotypeⁱ
- 4939766

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Acyltransferase, Ligase, Transferase
Biological process	Enterobactin biosynthesis
Ligand	ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCycⁱ	EcoCyc:ENTE-MONOMER MetaCyc:ENTE-MONOMER
BRENDAⁱ	6.3.2.14 2026
UniPathwayⁱ	UPA00017

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Enterobactin synthase component E1 Publication (EC:6.3.2.147 Publications) Alternative name(s): 2,3-dihydroxybenzoate-AMP ligase1 Publication Short name: DHB-AMP ligase1 Publication 2,3-dihydroxybenzoate-AMP synthaseCurated (EC:2.7.7.586 Publications) Dihydroxybenzoic acid-activating enzyme1 Publication Enterochelin synthase E1 Publication S-dihydroxybenzoyltransferase1 Publication (EC:2.5.1.-6 Publications)
Gene namesⁱ	Name:entE1 Publication Ordered Locus Names:b0594, JW0586
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Organism-specific databases

EcoGeneⁱ	EG10263 entE

EcoGeneⁱ

EG10263 entE

Subcellular locationⁱ

Membrane
1 Publication
Manual assertion based on experiment inⁱ
- Ref.12
  "Membrane association of the Escherichia coli enterobactin synthase proteins EntB/G, EntE, and EntF."
  Hantash F.M., Earhart C.F.
  J. Bacteriol. 182:1768-1773(2000) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBCELLULAR LOCATION.

GO - Cellular componentⁱ

cytosol
Source: EcoCyc
Inferred from direct assayⁱ
- 18304323
membrane Source: UniProtKB-SubCell

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Membrane

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	437	R → D: Catalyzes the adenylation reaction with 10% reduction of activity compared to the wild-type. 3% reduction of activity compared to the wild-type; when associated with D-473. 1 Publication	1
Mutagenesisⁱ	473	K → D: Catalyzes the adenylation reaction with same activity as the wild-type. 3% reduction of activity compared to the wild-type; when associated with D-437. 1 Publication	1
Mutagenesisⁱ	494	R → D: Catalyzes the adenylation reaction with same activity as the wild-type. 1 Publication	1

Chemistry databases

ChEMBLⁱ	CHEMBL4856

ChEMBLⁱ

CHEMBL4856

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000193075	1 – 536	Enterobactin synthase component EAdd BLAST		536

Proteomic databases

EPDⁱ	P10378
PaxDbⁱ	P10378
PRIDEⁱ	P10378

Expressionⁱ

Inductionⁱ

Under conditions of iron deficiency and by the fur protein.2 Publications

Interactionⁱ

Subunit structureⁱ

Proteins EntB, EntD, EntE, and EntF form a multienzyme complex called enterobactin synthase. Monomer. EntA and EntE interact together.5 Publications

Protein-protein interaction databases

BioGridⁱ	4259905, 320 interactors
Database of interacting proteins More...DIPⁱ	DIP-9515N
IntActⁱ	P10378, 13 interactors
STRINGⁱ	316385.ECDH10B_0662

Chemistry databases

BindingDBⁱ

P10378

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	10 – 18	Combined sources	9
Helixⁱ	29 – 32	Combined sources	4
Turnⁱ	33 – 36	Combined sources	4
Beta strandⁱ	39 – 44	Combined sources	6
Beta strandⁱ	47 – 50	Combined sources	4
Helixⁱ	51 – 67	Combined sources	17
Beta strandⁱ	75 – 79	Combined sources	5
Helixⁱ	85 – 96	Combined sources	12
Beta strandⁱ	99 – 103	Combined sources	5
Helixⁱ	109 – 119	Combined sources	11
Beta strandⁱ	122 – 127	Combined sources	6
Helixⁱ	131 – 133	Combined sources	3
Beta strandⁱ	134 – 136	Combined sources	3
Helixⁱ	137 – 145	Combined sources	9
Beta strandⁱ	151 – 155	Combined sources	5
Helixⁱ	163 – 168	Combined sources	6
Beta strandⁱ	183 – 189	Combined sources	7
Beta strandⁱ	193 – 196	Combined sources	4
Beta strandⁱ	199 – 203	Combined sources	5
Helixⁱ	204 – 218	Combined sources	15
Beta strandⁱ	225 – 228	Combined sources	4
Helixⁱ	235 – 239	Combined sources	5
Helixⁱ	242 – 249	Combined sources	8
Beta strandⁱ	252 – 255	Combined sources	4
Helixⁱ	261 – 271	Combined sources	11
Beta strandⁱ	275 – 278	Combined sources	4
Helixⁱ	280 – 291	Combined sources	12
Helixⁱ	296 – 299	Combined sources	4
Beta strandⁱ	304 – 310	Combined sources	7
Helixⁱ	314 – 323	Combined sources	10
Beta strandⁱ	326 – 334	Combined sources	9
Beta strandⁱ	337 – 341	Combined sources	5
Helixⁱ	348 – 353	Combined sources	6
Beta strandⁱ	357 – 360	Combined sources	4
Beta strandⁱ	364 – 368	Combined sources	5
Beta strandⁱ	380 – 386	Combined sources	7
Beta strandⁱ	388 – 390	Combined sources	3
Helixⁱ	398 – 404	Combined sources	7
Beta strandⁱ	411 – 419	Combined sources	9
Beta strandⁱ	425 – 430	Combined sources	6
Beta strandⁱ	432 – 437	Combined sources	6
Beta strandⁱ	440 – 443	Combined sources	4
Helixⁱ	444 – 451	Combined sources	8
Beta strandⁱ	457 – 467	Combined sources	11
Turnⁱ	468 – 470	Combined sources	3
Beta strandⁱ	471 – 482	Combined sources	12
Helixⁱ	486 – 494	Combined sources	9
Turnⁱ	495 – 497	Combined sources	3
Helixⁱ	500 – 502	Combined sources	3
Beta strandⁱ	505 – 509	Combined sources	5
Beta strandⁱ	519 – 521	Combined sources	3
Helixⁱ	523 – 531	Combined sources	9

Show more details

3D structure databases

ProteinModelPortalⁱ	P10378
SMRⁱ	P10378
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	438 – 439	Phosphopantetheine binding2 Publications		2

Sequence similaritiesⁱ

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

Phylogenomic databases

eggNOGⁱ	ENOG4108IQC Bacteria COG1021 LUCA
HOGENOMⁱ	HOG000230011
InParanoidⁱ	P10378
KEGG Orthology (KO) More...KOⁱ	K02363
PhylomeDBⁱ	P10378

Family and domain databases

InterProⁱ	View protein in InterPro IPR025110 AMP-bd_C IPR020845 AMP-binding_CS IPR000873 AMP-dep_Synth/Lig IPR011963 DHB_AMP_lig
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00501 AMP-binding, 1 hit PF13193 AMP-binding_C, 1 hit
TIGRFAMsⁱ	TIGR02275 DHB_AMP_lig, 1 hit
PROSITEⁱ	View protein in PROSITE PS00455 AMP_BINDING, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P10378-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MSIPFTRWPE EFARRYREKG YWQDLPLTDI LTRHAASDSI AVIDGERQLS 
        60         70         80         90        100
YRELNQAADN LACSLRRQGI KPGETALVQL GNVAELYITF FALLKLGVAP 
       110        120        130        140        150
VLALFSHQRS ELNAYASQIE PALLIADRQH ALFSGDDFLN TFVTEHSSIR 
       160        170        180        190        200
VVQLLNDSGE HNLQDAINHP AEDFTATPSP ADEVAYFQLS GGTTGTPKLI 
       210        220        230        240        250
PRTHNDYYYS VRRSVEICQF TQQTRYLCAI PAAHNYAMSS PGSLGVFLAG 
       260        270        280        290        300
GTVVLAADPS ATLCFPLIEK HQVNVTALVP PAVSLWLQAL IEGESRAQLA 
       310        320        330        340        350
SLKLLQVGGA RLSATLAARI PAEIGCQLQQ VFGMAEGLVN YTRLDDSAEK 
       360        370        380        390        400
IIHTQGYPMC PDDEVWVADA EGNPLPQGEV GRLMTRGPYT FRGYYKSPQH 
       410        420        430        440        450
NASAFDANGF YCSGDLISID PEGYITVQGR EKDQINRGGE KIAAEEIENL 
       460        470        480        490        500
LLRHPAVIYA ALVSMEDELM GEKSCAYLVV KEPLRAVQVR RFLREQGIAE 
       510        520        530 
FKLPDRVECV DSLPLTAVGK VDKKQLRQWL ASRASA

Length:536

Mass (Da):59,112

Last modified:November 1, 1997 - v3

Checksum:ⁱF818942DFDD8DC99

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	369 – 378	DAEGNPLPQG → ECRRKSTAAR in CAA33158 (PubMed:2525505).Curated		10

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X15058 Genomic DNA Translation: CAA33158.1 U82598 Genomic DNA Translation: AAB40794.1 U00096 Genomic DNA Translation: AAC73695.1 AP009048 Genomic DNA Translation: BAE76349.1 M24148 Unassigned DNA Translation: AAA16101.1 M36700 Genomic DNA Translation: AAA18492.1
PIRⁱ	H64792 SYECEB
NCBI Reference Sequences More...RefSeqⁱ	NP_415126.1, NC_000913.3 WP_000026812.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC73695; AAC73695; b0594 BAE76349; BAE76349; BAE76349
GeneIDⁱ	947426
KEGGⁱ	ecj:JW0586 eco:b0594
PATRICⁱ	fig\|1411691.4.peg.1675

Protein	Similar proteins		Species	Score	Length	Source
P10378	Enterobactin synthetase component E [includes: 2,3-dihydroxybenzoate-AMP ligase S-dihydroxybenzoyltransferase]		ECOLX		299	UniRef100_P10378
2,3-dihydroxybenzoate-AMP ligase (Fragment)		human gut metagenome		99
Isochorismatase		SHISO		38
2,3-dihydroxybenzoate-AMP ligase [enterobactin] siderophore		Klebsiella pneumoniae IS22		72
2,3-dihydroxybenzoate-AMP ligase		Shigella sp.		536
+22

Protein	Similar proteins		Species	Score	Length	Source
P10378	Enterobactin synthase component E		ECO57		536	UniRef90_P10378
Enterobactin synthetase component E [includes: 2,3-dihydroxybenzoate-AMP ligase S-dihydroxybenzoyltransferase]		ECOLX		299
2,3-dihydroxybenzoate-AMP ligase (Fragment)		human gut metagenome		99
Isochorismatase		SHISO		38
2,3-dihydroxybenzoate-AMP ligase [enterobactin] siderophore		Klebsiella pneumoniae IS22		72
+895

Protein	Similar proteins		Species	Score	Length	Source
P10378	Enterobactin synthase component E		ECO57		536	UniRef50_P10378
Enterobactin synthetase component E [includes: 2,3-dihydroxybenzoate-AMP ligase S-dihydroxybenzoyltransferase]		ECOLX		299
2,3-dihydroxybenzoate-AMP ligase (Fragment)		human gut metagenome		99
Isochorismatase		SHISO		38
2,3-dihydroxybenzoate-AMP ligase [enterobactin] siderophore		Klebsiella pneumoniae IS22		72
+3723

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X15058 Genomic DNA Translation: CAA33158.1 U82598 Genomic DNA Translation: AAB40794.1 U00096 Genomic DNA Translation: AAC73695.1 AP009048 Genomic DNA Translation: BAE76349.1 M24148 Unassigned DNA Translation: AAA16101.1 M36700 Genomic DNA Translation: AAA18492.1
PIRⁱ	H64792 SYECEB
RefSeqⁱ	NP_415126.1, NC_000913.3 WP_000026812.1, NZ_LN832404.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	3RG2	X-ray	3.10	A/B/C/D/E/F/G/H/I/J	1-536	[»]
	4IZ6	X-ray	2.40	A/B	1-536	[»]
ProteinModelPortalⁱ	P10378
SMRⁱ	P10378
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4259905, 320 interactors
DIPⁱ	DIP-9515N
IntActⁱ	P10378, 13 interactors
STRINGⁱ	316385.ECDH10B_0662

Chemistry databases

BindingDBⁱ	P10378
ChEMBLⁱ	CHEMBL4856

Proteomic databases

EPDⁱ	P10378
PaxDbⁱ	P10378
PRIDEⁱ	P10378

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC73695; AAC73695; b0594 BAE76349; BAE76349; BAE76349
GeneIDⁱ	947426
KEGGⁱ	ecj:JW0586 eco:b0594
PATRICⁱ	fig\|1411691.4.peg.1675

Organism-specific databases

EchoBASEⁱ	EB0259
EcoGeneⁱ	EG10263 entE

Phylogenomic databases

eggNOGⁱ	ENOG4108IQC Bacteria COG1021 LUCA
HOGENOMⁱ	HOG000230011
InParanoidⁱ	P10378
KOⁱ	K02363
PhylomeDBⁱ	P10378

Enzyme and pathway databases

UniPathwayⁱ	UPA00017
BioCycⁱ	EcoCyc:ENTE-MONOMER MetaCyc:ENTE-MONOMER
BRENDAⁱ	6.3.2.14 2026

Miscellaneous databases

Protein Ontology More...PROⁱ	PR:P10378

PROⁱ

PR:P10378

Family and domain databases

InterProⁱ	View protein in InterPro IPR025110 AMP-bd_C IPR020845 AMP-binding_CS IPR000873 AMP-dep_Synth/Lig IPR011963 DHB_AMP_lig
Pfamⁱ	View protein in Pfam PF00501 AMP-binding, 1 hit PF13193 AMP-binding_C, 1 hit
TIGRFAMsⁱ	TIGR02275 DHB_AMP_lig, 1 hit
PROSITEⁱ	View protein in PROSITE PS00455 AMP_BINDING, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ENTE_ECOLI
Accessionⁱ	P10378Primary (citable) accession number: P10378 Secondary accession number(s): P15049, P77773, Q2MBK7
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
	Last sequence update:	November 1, 1997
	Last modified:	November 7, 2018
	This is version 158 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

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

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P10378 (ENTE_ECOLI)

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Enterobactin synthase component E

entE

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: enterobactin biosynthesis

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

Kineticsⁱ

Pathwayⁱ: enterobactin biosynthesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ