UniProtKB - P77335 (HLYE_ECOLI)
Protein
Hemolysin E, chromosomal
Gene
hlyE
Organism
Escherichia coli (strain K12)
Status
Functioni
Toxin, which has some hemolytic activity towards mammalian cells. Acts by forming a pore-like structure upon contact with mammalian cells.1 Publication
GO - Molecular functioni
- identical protein binding Source: IntAct
- toxin activity Source: UniProtKB-KW
GO - Biological processi
- cytolysis by symbiont of host cells Source: EcoCyc
- hemolysis in other organism Source: EcoCyc
- modulation of apoptotic process in other organism Source: EcoliWiki
- pathogenesis Source: EcoliWiki
Keywordsi
Molecular function | Toxin |
Biological process | Cytolysis, Hemolysis, Virulence |
Enzyme and pathway databases
BioCyci | EcoCyc:G6619-MONOMER |
Protein family/group databases
TCDBi | 1.C.10.1.1, the pore-forming haemolysin e (hlye) family |
Names & Taxonomyi
Protein namesi | Recommended name: Hemolysin E, chromosomalAlternative name(s): Cytotoxin ClyA Hemolysis-inducing protein Latent pore-forming 34 kDa hemolysin Silent hemolysin SheA |
Gene namesi | Name:hlyE Synonyms:clyA, hpr, sheA, ycgD Ordered Locus Names:b1182, JW5181 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
- Secreted
- Periplasm
- Host cell membrane Curated; Single-pass membrane protein Curated Note: Exported from the cell by outer membrane vesicles. Also found in the periplasmic space.
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transmembranei | 183 – 203 | HelicalSequence analysisAdd BLAST | 21 |
GO - Cellular componenti
- extracellular region Source: EcoCyc
- host cell plasma membrane Source: UniProtKB-SubCell
- integral component of membrane Source: UniProtKB-KW
- periplasmic space Source: EcoCyc
Keywords - Cellular componenti
Host cell membrane, Host membrane, Membrane, Periplasm, SecretedPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 88 – 90 | GVA → DVD: Abolishes cytotoxic activity. 1 Publication | 3 | |
Mutagenesisi | 97 | Y → H: Strongly reduces cytotoxic activity. 1 Publication | 1 | |
Mutagenesisi | 143 – 144 | NA → DD: Abolishes cytotoxic activity. 1 Publication | 2 | |
Mutagenesisi | 157 | N → H: Strongly reduces cytotoxic activity. 1 Publication | 1 | |
Mutagenesisi | 165 | Y → C: Strongly reduces cytotoxic activity. 1 Publication | 1 | |
Mutagenesisi | 183 – 186 | Missing in PMWK16; retained in cytosol. Loss of function. | 4 | |
Mutagenesisi | 183 – 184 | AG → DD: Abolishes cytotoxic activity. 1 Publication | 2 | |
Mutagenesisi | 187 – 188 | AG → DD: Abolishes cytotoxic activity. 1 Publication | 2 | |
Mutagenesisi | 261 | R → K: Strongly reduces cytotoxic activity. 1 Publication | 1 | |
Mutagenesisi | 268 | D → A: Strongly reduces cytotoxic activity. 1 Publication | 1 | |
Mutagenesisi | 293 – 294 | GK → DA: Strongly reduces cytotoxic activity. 1 Publication | 2 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed2 Publications | |||
ChainiPRO_0000083996 | 2 – 303 | Hemolysin E, chromosomalAdd BLAST | 302 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 87 ↔ 285 | In monomeric form2 Publications |
Post-translational modificationi
In periplasm, it forms a disulfide bond between Cys-87 and Cys-285, which prevents the oligomerization. In outer membrane vesicles, the redox status prevents formation of the disulfide bond, leading to oligomerization and pore formation.
Keywords - PTMi
Disulfide bondProteomic databases
jPOSTi | P77335 |
PaxDbi | P77335 |
PRIDEi | P77335 |
Expressioni
Inductioni
During anaerobic growth. Weakly or not expressed in most strains. It is activated by SlyA, while it is silenced by H-NS. Its expression is also regulated by CRP and FNR.3 Publications
Interactioni
Subunit structurei
Monomer and oligomer. In periplasm, it is present as a monomer, while in outer membrane vesicles, it oligomerizes to form a pore structure that is active. The pore is formed by a dodecamer.
1 PublicationBinary interactionsi
P77335
With | #Exp. | IntAct |
---|---|---|
itself | 6 | EBI-8516553,EBI-8516553 |
GO - Molecular functioni
- identical protein binding Source: IntAct
Protein-protein interaction databases
BioGRIDi | 4260100, 4 interactors |
DIPi | DIP-9915N |
MINTi | P77335 |
STRINGi | 511145.b1182 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P77335 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P77335 |
Family & Domainsi
Sequence similaritiesi
Belongs to the hemolysin E family.Curated
Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | ENOG502ZB9A, Bacteria |
HOGENOMi | CLU_080941_0_0_6 |
InParanoidi | P77335 |
Family and domain databases
InterProi | View protein in InterPro IPR027018, Hemolysin_E |
Pfami | View protein in Pfam PF06109, HlyE, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P77335-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MTEIVADKTV EVVKNAIETA DGALDLYNKY LDQVIPWQTF DETIKELSRF
60 70 80 90 100
KQEYSQAASV LVGDIKTLLM DSQDKYFEAT QTVYEWCGVA TQLLAAYILL
110 120 130 140 150
FDEYNEKKAS AQKDILIKVL DDGITKLNEA QKSLLVSSQS FNNASGKLLA
160 170 180 190 200
LDSQLTNDFS EKSSYFQSQV DKIRKEAYAG AAAGVVAGPF GLIISYSIAA
210 220 230 240 250
GVVEGKLIPE LKNKLKSVQN FFTTLSNTVK QANKDIDAAK LKLTTEIAAI
260 270 280 290 300
GEIKTETETT RFYVDYDDLM LSLLKEAAKK MINTCNEYQK RHGKKTLFEV
PEV
Sequence cautioni
The sequence AAB07048 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
The sequence CAA67204 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
Mass spectrometryi
Molecular mass is 34940 Da. Determined by ESI. 1 Publication
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 175 | K → R in strain: CH9802. | 1 | |
Natural varianti | 201 | G → A in strain: CH9802. | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U57430 Genomic DNA Translation: AAB07048.1 Different initiation. X98615 Genomic DNA Translation: CAA67204.1 Different initiation. AJ001829 Genomic DNA Translation: CAA05035.1 U73842 Genomic DNA Translation: AAD04731.1 U00096 Genomic DNA Translation: AAC74266.2 AP009048 Genomic DNA Translation: BAA36016.2 AF240780 Genomic DNA Translation: AAL55667.1 U22466 Genomic DNA Translation: AAA92081.1 U13610 Genomic DNA No translation available. |
PIRi | C64864 |
RefSeqi | NP_415700.4, NC_000913.3 WP_001336523.1, NZ_SSZK01000010.1 |
Genome annotation databases
EnsemblBacteriai | AAC74266; AAC74266; b1182 BAA36016; BAA36016; BAA36016 |
GeneIDi | 945745 |
KEGGi | ecj:JW5181 eco:b1182 |
PATRICi | fig|1411691.4.peg.1105 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U57430 Genomic DNA Translation: AAB07048.1 Different initiation. X98615 Genomic DNA Translation: CAA67204.1 Different initiation. AJ001829 Genomic DNA Translation: CAA05035.1 U73842 Genomic DNA Translation: AAD04731.1 U00096 Genomic DNA Translation: AAC74266.2 AP009048 Genomic DNA Translation: BAA36016.2 AF240780 Genomic DNA Translation: AAL55667.1 U22466 Genomic DNA Translation: AAA92081.1 U13610 Genomic DNA No translation available. |
PIRi | C64864 |
RefSeqi | NP_415700.4, NC_000913.3 WP_001336523.1, NZ_SSZK01000010.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1QOY | X-ray | 2.00 | A | 1-303 | [»] | |
2WCD | X-ray | 3.29 | A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X | 2-303 | [»] | |
4PHO | X-ray | 2.12 | A/B/C | 2-303 | [»] | |
4PHQ | X-ray | 1.94 | A/B/C/D | 6-303 | [»] | |
6MRT | electron microscopy | 2.80 | A/B/C/D/E/F/G/H/I/J/K/L | 1-303 | [»] | |
6MRU | electron microscopy | 3.20 | A/B/C/D/E/F/G/H/I/J/K/L/M | 1-303 | [»] | |
6MRW | electron microscopy | 4.30 | A/B/C/D/E/F/G/H/I/J/K/L/M/N | 1-303 | [»] | |
SMRi | P77335 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4260100, 4 interactors |
DIPi | DIP-9915N |
MINTi | P77335 |
STRINGi | 511145.b1182 |
Protein family/group databases
TCDBi | 1.C.10.1.1, the pore-forming haemolysin e (hlye) family |
Proteomic databases
jPOSTi | P77335 |
PaxDbi | P77335 |
PRIDEi | P77335 |
Genome annotation databases
EnsemblBacteriai | AAC74266; AAC74266; b1182 BAA36016; BAA36016; BAA36016 |
GeneIDi | 945745 |
KEGGi | ecj:JW5181 eco:b1182 |
PATRICi | fig|1411691.4.peg.1105 |
Organism-specific databases
EchoBASEi | EB3032 |
Phylogenomic databases
eggNOGi | ENOG502ZB9A, Bacteria |
HOGENOMi | CLU_080941_0_0_6 |
InParanoidi | P77335 |
Enzyme and pathway databases
BioCyci | EcoCyc:G6619-MONOMER |
Miscellaneous databases
EvolutionaryTracei | P77335 |
PROi | PR:P77335 |
Family and domain databases
InterProi | View protein in InterPro IPR027018, Hemolysin_E |
Pfami | View protein in Pfam PF06109, HlyE, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | HLYE_ECOLI | |
Accessioni | P77335Primary (citable) accession number: P77335 Secondary accession number(s): Q47276, Q8VU70, Q9R3G4 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1997 |
Last sequence update: | January 23, 2007 | |
Last modified: | December 2, 2020 | |
This is version 162 of the entry and version 4 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families