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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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
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)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)serineCurated

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 interactions.
DIPiDIP-9516N.
IntActiP11454. 10 interactions.
STRINGi511145.b0586.

Structurei

Secondary structure

1
1293
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 2010Combined sources
Beta strandi23 – 253Combined sources
Beta strandi28 – 3710Combined sources
Helixi41 – 5313Combined sources
Helixi56 – 594Combined sources
Beta strandi60 – 656Combined sources
Beta strandi68 – 736Combined sources
Beta strandi83 – 853Combined sources
Beta strandi88 – 925Combined sources
Helixi96 – 1049Combined sources
Helixi111 – 1133Combined sources
Beta strandi117 – 1248Combined sources
Beta strandi126 – 13712Combined sources
Turni138 – 1403Combined sources
Turni143 – 1453Combined sources
Helixi146 – 16116Combined sources
Helixi174 – 18512Combined sources
Helixi188 – 20316Combined sources
Beta strandi210 – 2134Combined sources
Beta strandi224 – 2318Combined sources
Helixi235 – 2439Combined sources
Helixi249 – 26416Combined sources
Beta strandi267 – 2759Combined sources
Helixi282 – 2854Combined sources
Beta strandi292 – 2998Combined sources
Helixi306 – 32217Combined sources
Turni323 – 3253Combined sources
Helixi328 – 3347Combined sources
Beta strandi346 – 3505Combined sources
Beta strandi367 – 3715Combined sources
Beta strandi376 – 3849Combined sources
Beta strandi390 – 3978Combined sources
Turni398 – 4003Combined sources
Helixi403 – 42220Combined sources
Beta strandi427 – 4304Combined sources
Helixi438 – 4458Combined sources
Helixi457 – 46711Combined sources
Beta strandi471 – 4755Combined sources
Beta strandi480 – 4823Combined sources
Helixi483 – 49917Combined sources
Beta strandi507 – 5115Combined sources
Helixi516 – 52813Combined sources
Beta strandi531 – 5344Combined sources
Helixi541 – 55111Combined sources
Beta strandi554 – 5585Combined sources
Turni560 – 5645Combined sources
Beta strandi574 – 5763Combined sources
Beta strandi596 – 6038Combined sources
Turni606 – 6083Combined sources
Beta strandi611 – 6166Combined sources
Helixi617 – 63014Combined sources
Beta strandi638 – 6414Combined sources
Helixi650 – 66011Combined sources
Beta strandi663 – 6664Combined sources
Helixi671 – 6733Combined sources
Helixi675 – 68511Combined sources
Beta strandi689 – 6924Combined sources
Helixi694 – 7029Combined sources
Helixi706 – 7127Combined sources
Beta strandi718 – 7247Combined sources
Helixi728 – 73811Combined sources
Beta strandi742 – 7465Combined sources
Beta strandi751 – 7533Combined sources
Beta strandi755 – 7595Combined sources
Helixi762 – 7665Combined sources
Beta strandi770 – 7723Combined sources
Beta strandi776 – 7783Combined sources
Beta strandi782 – 7876Combined sources
Beta strandi800 – 8067Combined sources
Helixi817 – 8237Combined sources
Beta strandi824 – 8263Combined sources
Beta strandi834 – 84411Combined sources
Beta strandi850 – 86213Combined sources
Beta strandi865 – 8684Combined sources
Helixi869 – 8779Combined sources
Beta strandi882 – 8909Combined sources
Helixi894 – 8963Combined sources
Beta strandi898 – 9003Combined sources
Beta strandi904 – 91512Combined sources
Helixi919 – 92911Combined sources
Helixi932 – 9343Combined sources
Beta strandi937 – 9415Combined sources
Beta strandi951 – 9533Combined sources
Helixi955 – 9573Combined sources
Beta strandi968 – 9714Combined sources
Helixi976 – 98813Combined sources
Turni999 – 10035Combined sources
Helixi1006 – 102015Combined sources
Helixi1026 – 10316Combined sources
Helixi1035 – 10439Combined sources
Turni1050 – 10534Combined sources
Beta strandi1054 – 10618Combined sources
Beta strandi1063 – 10653Combined sources
Beta strandi1067 – 10715Combined sources
Helixi1079 – 10868Combined sources
Beta strandi1093 – 10975Combined sources
Turni1101 – 11033Combined sources
Helixi1105 – 11084Combined sources
Helixi1112 – 112615Combined sources
Beta strandi1128 – 11303Combined sources
Beta strandi1132 – 11376Combined sources
Helixi1139 – 115315Combined sources
Beta strandi1158 – 11658Combined sources
Helixi1170 – 11734Combined sources
Helixi1174 – 11807Combined sources
Helixi1186 – 119914Combined sources
Turni1200 – 12023Combined sources
Helixi1208 – 122417Combined sources
Beta strandi1232 – 124110Combined sources
Helixi1242 – 12443Combined sources
Helixi1251 – 12555Combined sources
Turni1256 – 12583Combined sources
Beta strandi1259 – 126911Combined sources
Helixi1271 – 12755Combined sources
Turni1277 – 12793Combined sources
Helixi1280 – 129112Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ROQNMR-A960-1293[»]
3TEJX-ray1.90A/B965-1293[»]
4ZXJX-ray2.80A1-1293[»]
ProteinModelPortaliP11454.
SMRiP11454. Positions 960-1293.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11454.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini976 – 104368Acyl carrierPROSITE-ProRule annotationAdd
BLAST

Region

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

Sequence similaritiesi

Contains 1 acyl carrier domain.PROSITE-ProRule annotation

Phylogenomic databases

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

        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 AAB40785.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti441 – 4422QL → HV in AAA92015 (PubMed:1826089).Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
2ROQNMR-A960-1293[»]
3TEJX-ray1.90A/B965-1293[»]
4ZXJX-ray2.80A1-1293[»]
ProteinModelPortaliP11454.
SMRiP11454. Positions 960-1293.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259895. 295 interactions.
DIPiDIP-9516N.
IntActiP11454. 10 interactions.
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.
OrthoDBiEOG6QP0WP.
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.
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]
ProtoNetiSearch...

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: March 16, 2016
This is version 160 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.