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Protein

Hemolysin E, chromosomal

Gene

hlyE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

GO - Biological processi

  • cytolysis in other organism Source: EcoCyc
  • hemolysis in other organism Source: EcoCyc
  • modulation of apoptotic process in other organism Source: EcoliWiki
  • pathogenesis Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Toxin

Keywords - Biological processi

Cytolysis, Hemolysis

Enzyme and pathway databases

BioCyciEcoCyc:G6619-MONOMER.
ECOL316407:JW5181-MONOMER.

Protein family/group databases

TCDBi1.C.10.1.1. the pore-forming haemolysin e (hlye) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Hemolysin E, chromosomal
Alternative 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
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13243. hlyE.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei183 – 203HelicalSequence analysisAdd BLAST21

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
Complete GO annotation...

Keywords - Cellular componenti

Host cell membrane, Host membrane, Membrane, Periplasm, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi88 – 90GVA → DVD: Abolishes cytotoxic activity. 1 Publication3
Mutagenesisi97Y → H: Strongly reduces cytotoxic activity. 1 Publication1
Mutagenesisi143 – 144NA → DD: Abolishes cytotoxic activity. 1 Publication2
Mutagenesisi157N → H: Strongly reduces cytotoxic activity. 1 Publication1
Mutagenesisi165Y → C: Strongly reduces cytotoxic activity. 1 Publication1
Mutagenesisi183 – 186Missing in PMWK16; retained in cytosol. Loss of function. 4
Mutagenesisi183 – 184AG → DD: Abolishes cytotoxic activity. 1 Publication2
Mutagenesisi187 – 188AG → DD: Abolishes cytotoxic activity. 1 Publication2
Mutagenesisi261R → K: Strongly reduces cytotoxic activity. 1 Publication1
Mutagenesisi268D → A: Strongly reduces cytotoxic activity. 1 Publication1
Mutagenesisi293 – 294GK → DA: Strongly reduces cytotoxic activity. 1 Publication2

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00000839962 – 303Hemolysin E, chromosomalAdd BLAST302

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi87 ↔ 285In 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 bond

Proteomic databases

PaxDbiP77335.
PRIDEiP77335.

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 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-8516553,EBI-8516553

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4260100. 4 interactors.
DIPiDIP-9915N.
MINTiMINT-2737936.
STRINGi511145.b1182.

Structurei

Secondary structure

1303
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 28Combined sources22
Helixi31 – 34Combined sources4
Helixi37 – 46Combined sources10
Turni47 – 50Combined sources4
Helixi51 – 53Combined sources3
Helixi56 – 99Combined sources44
Turni100 – 103Combined sources4
Helixi106 – 159Combined sources54
Helixi164 – 179Combined sources16
Beta strandi182 – 187Combined sources6
Helixi189 – 191Combined sources3
Beta strandi193 – 195Combined sources3
Helixi196 – 199Combined sources4
Helixi207 – 258Combined sources52
Helixi268 – 291Combined sources24

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QOYX-ray2.00A1-303[»]
2WCDX-ray3.29A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X2-303[»]
4PHOX-ray2.12A/B/C2-303[»]
4PHQX-ray1.94A/B/C/D6-303[»]
ProteinModelPortaliP77335.
SMRiP77335.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP77335.

Family & Domainsi

Sequence similaritiesi

Belongs to the hemolysin E family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4106PXS. Bacteria.
ENOG410YAUV. LUCA.
HOGENOMiHOG000051663.
InParanoidiP77335.
KOiK11139.
OMAiRCAIREY.

Family and domain databases

InterProiIPR027018. Hemolysin_E.
[Graphical view]
PfamiPF06109. HlyE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P77335-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:303
Mass (Da):33,759
Last modified:January 23, 2007 - v4
Checksum:i9BE348DA095668A5
GO

Sequence cautioni

The sequence AAB07048 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAA67204 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Mass spectrometryi

Molecular mass is 34940 Da from positions 2 - 303. Determined by ESI. 1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti175K → R in strain: CH9802. 1
Natural varianti201G → 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.
PIRiC64864.
RefSeqiNP_415700.4. NC_000913.3.
WP_001336523.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74266; AAC74266; b1182.
BAA36016; BAA36016; BAA36016.
GeneIDi945745.
KEGGiecj:JW5181.
eco:b1182.
PATRICi32117610. VBIEscCol129921_1227.

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.
PIRiC64864.
RefSeqiNP_415700.4. NC_000913.3.
WP_001336523.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QOYX-ray2.00A1-303[»]
2WCDX-ray3.29A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X2-303[»]
4PHOX-ray2.12A/B/C2-303[»]
4PHQX-ray1.94A/B/C/D6-303[»]
ProteinModelPortaliP77335.
SMRiP77335.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260100. 4 interactors.
DIPiDIP-9915N.
MINTiMINT-2737936.
STRINGi511145.b1182.

Protein family/group databases

TCDBi1.C.10.1.1. the pore-forming haemolysin e (hlye) family.

Proteomic databases

PaxDbiP77335.
PRIDEiP77335.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74266; AAC74266; b1182.
BAA36016; BAA36016; BAA36016.
GeneIDi945745.
KEGGiecj:JW5181.
eco:b1182.
PATRICi32117610. VBIEscCol129921_1227.

Organism-specific databases

EchoBASEiEB3032.
EcoGeneiEG13243. hlyE.

Phylogenomic databases

eggNOGiENOG4106PXS. Bacteria.
ENOG410YAUV. LUCA.
HOGENOMiHOG000051663.
InParanoidiP77335.
KOiK11139.
OMAiRCAIREY.

Enzyme and pathway databases

BioCyciEcoCyc:G6619-MONOMER.
ECOL316407:JW5181-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP77335.
PROiP77335.

Family and domain databases

InterProiIPR027018. Hemolysin_E.
[Graphical view]
PfamiPF06109. HlyE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHLYE_ECOLI
AccessioniPrimary (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: November 2, 2016
This is version 138 of the entry and version 4 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, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.