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Protein

Intimin

Gene

eae

Organism
Escherichia coli O127:H6 (strain E2348/69 / EPEC)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Necessary for the production of attaching and effacing lesions on tissue culture cells. Believed to mediate adherence.

GO - Biological processi

  • cell adhesion Source: InterPro
  • pathogenesis Source: CACAO
Complete GO annotation...

Keywords - Biological processi

Virulence

Enzyme and pathway databases

BioCyciECOL574521:GJAO-4082-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Intimin
Alternative name(s):
Attaching and effacing protein
Short name:
Eae protein
Gene namesi
Name:eae
Synonyms:eaeA
Ordered Locus Names:E2348C_3939
OrganismiEscherichia coli O127:H6 (strain E2348/69 / EPEC)
Taxonomic identifieri574521 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000008205 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei20 – 3920HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell outer membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 939939IntiminPRO_0000211827Add
BLAST

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
tirQ9KWH91EBI-1029391,EBI-1029383From a different organism.

Protein-protein interaction databases

IntActiP19809. 1 interaction.

Structurei

Secondary structure

1
939
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi41 – 433Combined sources
Beta strandi50 – 523Combined sources
Helixi54 – 618Combined sources
Beta strandi62 – 665Combined sources
Helixi73 – 808Combined sources
Helixi84 – 918Combined sources
Turni92 – 943Combined sources
Beta strandi95 – 973Combined sources
Helixi98 – 1025Combined sources
Beta strandi109 – 1135Combined sources
Beta strandi118 – 1214Combined sources
Beta strandi141 – 1433Combined sources
Beta strandi659 – 6668Combined sources
Beta strandi668 – 6747Combined sources
Beta strandi678 – 6869Combined sources
Beta strandi695 – 70612Combined sources
Beta strandi708 – 7114Combined sources
Beta strandi716 – 7238Combined sources
Beta strandi728 – 7303Combined sources
Beta strandi732 – 7365Combined sources
Beta strandi748 – 7514Combined sources
Beta strandi761 – 7633Combined sources
Turni764 – 7663Combined sources
Beta strandi769 – 7713Combined sources
Beta strandi774 – 7774Combined sources
Beta strandi781 – 7833Combined sources
Beta strandi786 – 7883Combined sources
Beta strandi790 – 7923Combined sources
Beta strandi793 – 7986Combined sources
Turni800 – 8023Combined sources
Beta strandi803 – 8053Combined sources
Turni807 – 8093Combined sources
Beta strandi811 – 8144Combined sources
Beta strandi816 – 8183Combined sources
Beta strandi820 – 8267Combined sources
Turni827 – 8293Combined sources
Beta strandi830 – 8367Combined sources
Beta strandi840 – 85112Combined sources
Helixi853 – 86210Combined sources
Beta strandi864 – 8663Combined sources
Helixi871 – 88111Combined sources
Helixi884 – 8863Combined sources
Helixi888 – 8903Combined sources
Beta strandi897 – 8993Combined sources
Helixi904 – 9096Combined sources
Beta strandi911 – 9166Combined sources
Turni917 – 9193Combined sources
Beta strandi920 – 9278Combined sources
Beta strandi928 – 9303Combined sources
Beta strandi933 – 9386Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E5UNMR-I753-939[»]
1F00X-ray1.90I658-939[»]
1F02X-ray2.90I658-939[»]
2MPWNMR-A39-143[»]
ProteinModelPortaliP19809.
SMRiP19809. Positions 566-939.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19809.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini63 – 11250LysMPROSITE-ProRule annotationAdd
BLAST
Domaini560 – 65394Big-1 1PROSITE-ProRule annotationAdd
BLAST
Domaini660 – 75192Big-1 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the intimin/invasin family.Curated
Contains 1 LysM domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

KOiK12790.
OMAiPENMLGY.

Family and domain databases

Gene3Di2.60.40.920. 2 hits.
3.10.100.10. 1 hit.
InterProiIPR003344. Big_1_dom.
IPR003343. Big_2.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
IPR003535. Intimin/invasin_bac.
IPR013117. Intimin_C.
IPR008964. Invasin/intimin_cell_adhesion.
IPR024519. Invasin_beta.
IPR018392. LysM_dom.
[Graphical view]
PfamiPF02369. Big_1. 1 hit.
PF07979. Intimin_C. 1 hit.
PF11924. Invasin_beta. 1 hit.
PF01476. LysM. 1 hit.
[Graphical view]
PRINTSiPR01369. INTIMIN.
SMARTiSM00634. BID_1. 2 hits.
SM00635. BID_2. 1 hit.
SM00257. LysM. 1 hit.
[Graphical view]
SUPFAMiSSF49373. SSF49373. 3 hits.
SSF56436. SSF56436. 1 hit.
PROSITEiPS51127. BIG1. 2 hits.
PS51782. LYSM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P19809-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MITHGFYART RHKHKLKKTF IMLSAGLGLF FYVNQNSFAN GENYFKLGSD
60 70 80 90 100
SKLLTHNSYQ NRLFYTLKTG ETVADLSKSQ DINLSTIWSL NKHLYSSESE
110 120 130 140 150
MMKAAPGQQI ILPLKKLPFE YSALPLLGSA PLVAAGGVAG HTNKLTKMSP
160 170 180 190 200
DVTKSNMTDD KALNYAAQQA ASLGSQLQSR SLNGDYAKDT ALGIAGNQAS
210 220 230 240 250
SQLQAWLQHY GTAEVNLQSG NNFDGSSLDF LLPFYDSEKM LAFGQVGARY
260 270 280 290 300
IDSRFTANLG AGQRFFLPEN MLGYNVFIDQ DFSGDNTRLG IGGEYWRDYF
310 320 330 340 350
KSSVNGYFRM SGWHESYNKK DYDERPANGF DIRFNGYLPS YPALGAKLMY
360 370 380 390 400
EQYYGDNVAL FNSDKLQSNP GAATVGVNYT PIPLVTMGID YRHGTGNEND
410 420 430 440 450
LLYSMQFRYQ FDKPWSQQIE PQYVNELRTL SGSRYDLVQR NNNIILEYKK
460 470 480 490 500
QDILSLNIPH DINGTERSTQ KIQLIVKSKY GLDRIVWDDS ALRSQGGQIQ
510 520 530 540 550
HSGSQSAQDY QAILPAYVQG GSNVYKVTAR AYDRNGNSSN NVLLTITVLS
560 570 580 590 600
NGQVVDQVGV TDFTADKTSA KADGTEAITY TATVKKNGVA QANVPVSFNI
610 620 630 640 650
VSGTAVLSAN SANTNGSGKA TVTLKSDKPG QVVVSAKTAE MTSALNANAV
660 670 680 690 700
IFVDQTKASI TEIKADKTTA VANGQDAITY TVKVMKGDKP VSNQEVTFTT
710 720 730 740 750
TLGKLSNSTE KTDTNGYAKV TLTSTTPGKS LVSARVSDVA VDVKAPEVEF
760 770 780 790 800
FTTLTIDDGN IEIVGTGVKG KLPTVWLQYG QVNLKASGGN GKYTWRSANP
810 820 830 840 850
AIASVDASSG QVTLKEKGTT TISVISSDNQ TATYTIATPN SLIVPNMSKR
860 870 880 890 900
VTYNDAVNTC KNFGGKLPSS QNELENVFKA WGAANKYEYY KSSQTIISWV
910 920 930
QQTAQDAKSG VASTYDLVKQ NPLNNIKASE SNAYATCVK
Length:939
Mass (Da):102,353
Last modified:May 5, 2009 - v2
Checksum:iC42BC5C0A965B0BD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti105 – 1051A → E in AAA62775 (PubMed:2172966).Curated
Sequence conflicti105 – 1051A → E in AAC38392 (PubMed:9593291).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58154 Genomic DNA. Translation: AAA62775.1.
AF022236 Genomic DNA. Translation: AAC38392.1.
FM180568 Genomic DNA. Translation: CAS11487.1.
PIRiI41197.
RefSeqiWP_000627890.1. NC_011601.1.

Genome annotation databases

EnsemblBacteriaiCAS11487; CAS11487; E2348C_3939.
KEGGiecg:E2348C_3939.
PATRICi18347094. VBIEscCol90278_4030.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58154 Genomic DNA. Translation: AAA62775.1.
AF022236 Genomic DNA. Translation: AAC38392.1.
FM180568 Genomic DNA. Translation: CAS11487.1.
PIRiI41197.
RefSeqiWP_000627890.1. NC_011601.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E5UNMR-I753-939[»]
1F00X-ray1.90I658-939[»]
1F02X-ray2.90I658-939[»]
2MPWNMR-A39-143[»]
ProteinModelPortaliP19809.
SMRiP19809. Positions 566-939.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP19809. 1 interaction.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAS11487; CAS11487; E2348C_3939.
KEGGiecg:E2348C_3939.
PATRICi18347094. VBIEscCol90278_4030.

Phylogenomic databases

KOiK12790.
OMAiPENMLGY.

Enzyme and pathway databases

BioCyciECOL574521:GJAO-4082-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP19809.

Family and domain databases

Gene3Di2.60.40.920. 2 hits.
3.10.100.10. 1 hit.
InterProiIPR003344. Big_1_dom.
IPR003343. Big_2.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
IPR003535. Intimin/invasin_bac.
IPR013117. Intimin_C.
IPR008964. Invasin/intimin_cell_adhesion.
IPR024519. Invasin_beta.
IPR018392. LysM_dom.
[Graphical view]
PfamiPF02369. Big_1. 1 hit.
PF07979. Intimin_C. 1 hit.
PF11924. Invasin_beta. 1 hit.
PF01476. LysM. 1 hit.
[Graphical view]
PRINTSiPR01369. INTIMIN.
SMARTiSM00634. BID_1. 2 hits.
SM00635. BID_2. 1 hit.
SM00257. LysM. 1 hit.
[Graphical view]
SUPFAMiSSF49373. SSF49373. 3 hits.
SSF56436. SSF56436. 1 hit.
PROSITEiPS51127. BIG1. 2 hits.
PS51782. LYSM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A genetic locus of enteropathogenic Escherichia coli necessary for the production of attaching and effacing lesions on tissue culture cells."
    Jerse A.E., Yu J., Tall B.D., Kaper J.B.
    Proc. Natl. Acad. Sci. U.S.A. 87:7839-7843(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: E2348/69 / EPEC.
  2. "The complete sequence of the locus of enterocyte effacement (LEE) from enteropathogenic Escherichia coli E2348/69."
    Elliott S.J., Wainwright L.A., McDaniel T.K., Jarvis K.G., Deng Y.K., Lai L.C., McNamara B.P., Donnenberg M.S., Kaper J.B.
    Mol. Microbiol. 28:1-4(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: E2348/69 / EPEC.
  3. "Complete genome sequence and comparative genome analysis of enteropathogenic Escherichia coli O127:H6 strain E2348/69."
    Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.
    J. Bacteriol. 191:347-354(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: E2348/69 / EPEC.

Entry informationi

Entry nameiEAE_ECO27
AccessioniPrimary (citable) accession number: P19809
Secondary accession number(s): B7UM97
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: May 5, 2009
Last modified: January 20, 2016
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.