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Hemolysin E, chromosomal (Cytotoxin ClyA) (Hemolysis-inducing protein) (Latent pore-forming 34 kDa hemolysin) (Silent hemolysin SheA)

 HLYE_ECOLI              Reviewed;         303 AA.
P77335; Q47276; Q8VU70; Q9R3G4;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
22-NOV-2017, entry version 143.
RecName: Full=Hemolysin E, chromosomal;
AltName: Full=Cytotoxin ClyA;
AltName: Full=Hemolysis-inducing protein;
AltName: Full=Latent pore-forming 34 kDa hemolysin;
AltName: Full=Silent hemolysin SheA;
Name=hlyE; Synonyms=clyA, hpr, sheA, ycgD;
OrderedLocusNames=b1182, JW5181;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12 / XL1-Blue;
McNamara P.J., Iandolo J.J., Uhlich G.;
Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=11902713; DOI=10.1046/j.1365-2958.1997.4391813.x;
del Castillo F.J., Leal S.C., Moreno F., del Castillo I.;
"The Escherichia coli K-12 sheA gene encodes a 34-kDa secreted
haemolysin.";
Mol. Microbiol. 25:107-115(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-13,
SUBCELLULAR LOCATION, AND INDUCTION.
STRAIN=K12;
PubMed=10027972; DOI=10.1046/j.1365-2958.1999.01196.x;
Ludwig A., Bauer S., Benz R., Bergmann B., Goebel W.;
"Analysis of the SlyA-controlled expression, subcellular localization
and pore-forming activity of a 34 kDa haemolysin (ClyA) from
Escherichia coli K-12.";
Mol. Microbiol. 31:557-567(1999).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=3030-2;
Xing J., Fernandez S.V., Kapur V., Barletta R.G., Moxley R.A.;
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=8905232; DOI=10.1093/dnares/3.3.137;
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
Yano M., Horiuchi T.;
"A 718-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 12.7-28.0 min region on the linkage map.";
DNA Res. 3:137-155(1996).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=CH9802;
Chang G.-N., Ho K.-C.;
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-296.
STRAIN=K12 / XL1-Blue;
King C.H., Shinnick T.M.;
Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-156.
STRAIN=K12 / AB1157;
Woodgate R.;
Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases.
[11]
PROTEIN SEQUENCE OF 2-18, AND MUTAGENESIS OF 88-GLY--VAL-90;
143-ASN-ALA-144; 183-ALA-GLY-184; 187-ALA-GLY-188; ASP-268 AND
293-GLY-LYS-294.
PubMed=10383763; DOI=10.1046/j.1365-2958.1999.01435.x;
Oscarsson J., Mizunoe Y., Li L., Lai X.-H., Wieslander A., Uhlin B.E.;
"Molecular analysis of the cytolytic protein ClyA (SheA) from
Escherichia coli.";
Mol. Microbiol. 32:1226-1238(1999).
[12]
PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION,
OLIGOMERIZATION, AND DISULFIDE BOND FORMATION.
PubMed=14532000; DOI=10.1016/S0092-8674(03)00754-2;
Wai S.N., Lindmark B., Soederblom T., Takade A., Westermark M.,
Oscarsson J., Jass J., Richter-Dahlfors A., Mizunoe Y., Uhlin B.E.;
"Vesicle-mediated export and assembly of pore-forming oligomers of the
enterobacterial clyA cytotoxin.";
Cell 115:25-35(2003).
[13]
MASS SPECTROMETRY, DISULFIDE BOND, AND MUTAGENESIS OF TYR-97; ASN-157;
TYR-165 AND ARG-261.
PubMed=11006277; DOI=10.1074/jbc.M005420200;
Atkins A., Wyborn N.R., Wallace A.J., Stillman T.J., Black L.K.,
Fielding A.B., Hisakado M., Artymiuk P.J., Green J.;
"Structure-function relationships of a novel bacterial toxin,
hemolysin E. The role of alpha G.";
J. Biol. Chem. 275:41150-41155(2000).
[14]
INDUCTION.
PubMed=11053378; DOI=10.1128/JB.182.22.6347-6357.2000;
Westermark M., Oscarsson J., Mizunoe Y., Urbonaviciene J., Uhlin B.E.;
"Silencing and activation of ClyA cytotoxin expression in Escherichia
coli.";
J. Bacteriol. 182:6347-6357(2000).
[15]
INDUCTION.
PubMed=12057949; DOI=10.1128/JB.184.13.3549-3559.2002;
Spory A., Bosserhoff A., von Rhein C., Goebel W., Ludwig A.;
"Differential regulation of multiple proteins of Escherichia coli and
Salmonella enterica serovar Typhimurium by the transcriptional
regulator SlyA.";
J. Bacteriol. 184:3549-3559(2002).
[16]
MUTANT PMWK16 DEL.
PubMed=12949101; DOI=10.1128/JB.185.18.5491-5499.2003;
Wai S.N., Westermark M., Oscarsson J., Jass J., Maier E., Benz R.,
Uhlin B.E.;
"Characterization of dominantly negative mutant ClyA cytotoxin
proteins in Escherichia coli.";
J. Bacteriol. 185:5491-5499(2003).
[17]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=10660049; DOI=10.1016/S0092-8674(00)81564-0;
Wallace A.J., Stillman T.J., Atkins A., Jamieson S.J., Bullough P.A.,
Green J., Artymiuk P.J.;
"E. coli hemolysin E (HlyE, ClyA, SheA): X-ray crystal structure of
the toxin and observation of membrane pores by electron microscopy.";
Cell 100:265-276(2000).
[18]
X-RAY CRYSTALLOGRAPHY (3.29 ANGSTROMS), PORE FORMATION, MEMBRANE
TOPOLOGY, AND SUBUNIT.
PubMed=19421192; DOI=10.1038/nature08026;
Mueller M., Grauschopf U., Maier T., Glockshuber R., Ban N.;
"The structure of a cytolytic alpha-helical toxin pore reveals its
assembly mechanism.";
Nature 459:726-730(2009).
-!- FUNCTION: Toxin, which has some hemolytic activity towards
mammalian cells. Acts by forming a pore-like structure upon
contact with mammalian cells. {ECO:0000269|PubMed:14532000}.
-!- SUBUNIT: 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. {ECO:0000269|PubMed:19421192}.
-!- INTERACTION:
Self; NbExp=6; IntAct=EBI-8516553, EBI-8516553;
-!- SUBCELLULAR LOCATION: Secreted. Periplasm. Host cell membrane
{ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Note=Exported from the cell by outer membrane vesicles. Also found
in the periplasmic space.
-!- INDUCTION: 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.
{ECO:0000269|PubMed:10027972, ECO:0000269|PubMed:11053378,
ECO:0000269|PubMed:12057949}.
-!- PTM: 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.
-!- MASS SPECTROMETRY: Mass=34940; Method=Electrospray; Range=2-303;
Evidence={ECO:0000269|PubMed:11006277};
-!- SIMILARITY: Belongs to the hemolysin E family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB07048.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAA67204.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; U57430; AAB07048.1; ALT_INIT; Genomic_DNA.
EMBL; X98615; CAA67204.1; ALT_INIT; Genomic_DNA.
EMBL; AJ001829; CAA05035.1; -; Genomic_DNA.
EMBL; U73842; AAD04731.1; -; Genomic_DNA.
EMBL; U00096; AAC74266.2; -; Genomic_DNA.
EMBL; AP009048; BAA36016.2; -; Genomic_DNA.
EMBL; AF240780; AAL55667.1; -; Genomic_DNA.
EMBL; U22466; AAA92081.1; -; Genomic_DNA.
EMBL; U13610; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PIR; C64864; C64864.
RefSeq; NP_415700.4; NC_000913.3.
RefSeq; WP_001336523.1; NZ_LN832404.1.
PDB; 1QOY; X-ray; 2.00 A; A=1-303.
PDB; 2WCD; X-ray; 3.29 A; 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.
PDB; 4PHO; X-ray; 2.12 A; A/B/C=2-303.
PDB; 4PHQ; X-ray; 1.94 A; A/B/C/D=6-303.
PDBsum; 1QOY; -.
PDBsum; 2WCD; -.
PDBsum; 4PHO; -.
PDBsum; 4PHQ; -.
ProteinModelPortal; P77335; -.
SMR; P77335; -.
BioGrid; 4260100; 4.
DIP; DIP-9915N; -.
MINT; MINT-2737936; -.
TCDB; 1.C.10.1.1; the pore-forming haemolysin e (hlye) family.
PaxDb; P77335; -.
PRIDE; P77335; -.
EnsemblBacteria; AAC74266; AAC74266; b1182.
EnsemblBacteria; BAA36016; BAA36016; BAA36016.
GeneID; 945745; -.
KEGG; ecj:JW5181; -.
KEGG; eco:b1182; -.
PATRIC; fig|1411691.4.peg.1105; -.
EchoBASE; EB3032; -.
EcoGene; EG13243; hlyE.
eggNOG; ENOG4106PXS; Bacteria.
eggNOG; ENOG410YAUV; LUCA.
HOGENOM; HOG000051663; -.
InParanoid; P77335; -.
KO; K11139; -.
BioCyc; EcoCyc:G6619-MONOMER; -.
EvolutionaryTrace; P77335; -.
PRO; PR:P77335; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005576; C:extracellular region; IMP:EcoCyc.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0042597; C:periplasmic space; IMP:EcoCyc.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0051715; P:cytolysis in other organism; IDA:EcoCyc.
GO; GO:0044179; P:hemolysis in other organism; IDA:EcoCyc.
GO; GO:0044532; P:modulation of apoptotic process in other organism; IDA:EcoliWiki.
GO; GO:0009405; P:pathogenesis; IDA:EcoliWiki.
InterPro; IPR027018; Hemolysin_E.
Pfam; PF06109; HlyE; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytolysis; Direct protein sequencing;
Disulfide bond; Hemolysis; Host cell membrane; Host membrane;
Membrane; Periplasm; Reference proteome; Secreted; Toxin;
Transmembrane; Transmembrane helix.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:10027972,
ECO:0000269|PubMed:10383763}.
CHAIN 2 303 Hemolysin E, chromosomal.
/FTId=PRO_0000083996.
TRANSMEM 183 203 Helical. {ECO:0000255}.
DISULFID 87 285 In monomeric form.
{ECO:0000269|PubMed:11006277,
ECO:0000269|PubMed:14532000}.
VARIANT 175 175 K -> R (in strain: CH9802).
VARIANT 201 201 G -> A (in strain: CH9802).
MUTAGEN 88 90 GVA->DVD: Abolishes cytotoxic activity.
{ECO:0000269|PubMed:10383763}.
MUTAGEN 97 97 Y->H: Strongly reduces cytotoxic
activity. {ECO:0000269|PubMed:11006277}.
MUTAGEN 143 144 NA->DD: Abolishes cytotoxic activity.
{ECO:0000269|PubMed:10383763}.
MUTAGEN 157 157 N->H: Strongly reduces cytotoxic
activity. {ECO:0000269|PubMed:11006277}.
MUTAGEN 165 165 Y->C: Strongly reduces cytotoxic
activity. {ECO:0000269|PubMed:11006277}.
MUTAGEN 183 186 Missing: In PMWK16; retained in cytosol.
Loss of function.
MUTAGEN 183 184 AG->DD: Abolishes cytotoxic activity.
{ECO:0000269|PubMed:10383763}.
MUTAGEN 187 188 AG->DD: Abolishes cytotoxic activity.
{ECO:0000269|PubMed:10383763}.
MUTAGEN 261 261 R->K: Strongly reduces cytotoxic
activity. {ECO:0000269|PubMed:11006277}.
MUTAGEN 268 268 D->A: Strongly reduces cytotoxic
activity. {ECO:0000269|PubMed:10383763}.
MUTAGEN 293 294 GK->DA: Strongly reduces cytotoxic
activity. {ECO:0000269|PubMed:10383763}.
HELIX 7 28 {ECO:0000244|PDB:4PHQ}.
HELIX 31 34 {ECO:0000244|PDB:4PHQ}.
HELIX 37 46 {ECO:0000244|PDB:4PHQ}.
TURN 47 50 {ECO:0000244|PDB:4PHQ}.
HELIX 51 53 {ECO:0000244|PDB:4PHQ}.
HELIX 56 99 {ECO:0000244|PDB:4PHQ}.
TURN 100 103 {ECO:0000244|PDB:4PHQ}.
HELIX 106 159 {ECO:0000244|PDB:4PHQ}.
HELIX 164 179 {ECO:0000244|PDB:4PHQ}.
STRAND 182 187 {ECO:0000244|PDB:4PHQ}.
HELIX 189 191 {ECO:0000244|PDB:4PHQ}.
STRAND 193 195 {ECO:0000244|PDB:4PHQ}.
HELIX 196 199 {ECO:0000244|PDB:4PHQ}.
HELIX 207 258 {ECO:0000244|PDB:4PHQ}.
HELIX 268 291 {ECO:0000244|PDB:4PHQ}.
SEQUENCE 303 AA; 33759 MW; 9BE348DA095668A5 CRC64;
MTEIVADKTV EVVKNAIETA DGALDLYNKY LDQVIPWQTF DETIKELSRF KQEYSQAASV
LVGDIKTLLM DSQDKYFEAT QTVYEWCGVA TQLLAAYILL FDEYNEKKAS AQKDILIKVL
DDGITKLNEA QKSLLVSSQS FNNASGKLLA LDSQLTNDFS EKSSYFQSQV DKIRKEAYAG
AAAGVVAGPF GLIISYSIAA GVVEGKLIPE LKNKLKSVQN FFTTLSNTVK QANKDIDAAK
LKLTTEIAAI GEIKTETETT RFYVDYDDLM LSLLKEAAKK MINTCNEYQK RHGKKTLFEV
PEV


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