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Hemolysin

 HLYA_VIBCH              Reviewed;         741 AA.
P09545; O08197; O08290; Q56641; Q99290; Q9KMU9;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-DEC-2000, sequence version 2.
05-DEC-2018, entry version 142.
RecName: Full=Hemolysin;
Flags: Precursor;
Name=hlyA; OrderedLocusNames=VC_A0219;
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
Vibrionaceae; Vibrio.
NCBI_TaxID=243277;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=El Tor O17 / Serotype O1;
PubMed=3050359; DOI=10.1111/j.1365-2958.1988.tb00054.x;
Alm R.A., Stroeher U.H., Manning P.A.;
"Extracellular proteins of Vibrio cholerae: nucleotide sequence of the
structural gene (hlyA) for the haemolysin of the haemolytic El Tor
strain O17 and characterization of the hlyA mutation in the non-
haemolytic classical strain 569B.";
Mol. Microbiol. 2:481-488(1988).
[2]
SEQUENCE REVISION.
Manning P.A.;
Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=El Tor RV79;
PubMed=2453464;
Rader A.E., Murphy J.R.;
"Nucleotide sequences and comparison of the hemolysin determinants of
Vibrio cholerae El Tor RV79(Hly+) and RV79(Hly-) and classical
569B(Hly-).";
Infect. Immun. 56:1414-1419(1988).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 26-45 AND
158-177.
STRAIN=El Tor N86 / Serotype O1;
PubMed=2174833;
Yamamoto K., Ichinose Y., Shinagawa H., Makino K., Nakata A.,
Iwanaga M., Honda T., Miwatani T.;
"Two-step processing for activation of the cytolysin/hemolysin of
Vibrio cholerae O1 biotype El Tor: nucleotide sequence of the
structural gene (hlyA) and characterization of the processed
products.";
Infect. Immun. 58:4106-4116(1990).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 39315 / El Tor Inaba N16961;
PubMed=10952301; DOI=10.1038/35020000;
Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A.,
Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L.,
Ermolaeva M.D., Vamathevan J.J., Bass S., Qin H., Dragoi I.,
Sellers P., McDonald L.A., Utterback T.R., Fleischmann R.D.,
Nierman W.C., White O., Salzberg S.L., Smith H.O., Colwell R.R.,
Mekalanos J.J., Venter J.C., Fraser C.M.;
"DNA sequence of both chromosomes of the cholera pathogen Vibrio
cholerae.";
Nature 406:477-483(2000).
[6]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 26-741, SUBUNIT, FUNCTION,
PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY,
ACTIVATION BY PROTEOLYTIC CLEAVAGE, SUBCELLULAR LOCATION, DOMAIN, AND
DISULFIDE BONDS.
PubMed=15978620; DOI=10.1016/j.jmb.2005.05.045;
Olson R., Gouaux E.;
"Crystal structure of the Vibrio cholerae cytolysin (VCC) pro-toxin
and its assembly into a heptameric transmembrane pore.";
J. Mol. Biol. 350:997-1016(2005).
-!- FUNCTION: Bacterial hemolysin that causes cytolysis by forming
heptameric pores in target host membranes.
{ECO:0000269|PubMed:15978620}.
-!- SUBUNIT: Monomer. Homoheptamer. After binding to target membranes
the protein assembles into a heptameric pre-pore complex.
Proteolytic cleavage triggers a conformation change that is
required for membrane insertion and pore formation.
{ECO:0000269|PubMed:15978620}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-6409539, EBI-6409539;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15978620}. Host
cell membrane {ECO:0000269|PubMed:15978620}; Multi-pass membrane
protein {ECO:0000269|PubMed:15978620}. Note=In the hemolytic
biotype El Tor the 80 kDa hemolysin precursor is secreted as
monomer. After binding to target membranes the protein assembles
into a heptameric prepore complex. Proteolytic cleavage triggers a
conformation change that is required for membrane insertion and
pore formation.
-!- INDUCTION: By hemolysin B cytoplasmic protein. {ECO:0000305}.
-!- DOMAIN: May bind to glycans on target cells via the C-terminal
beta-prism domain. {ECO:0000269|PubMed:15978620}.
-!- PTM: Proteolytical cleavage is required to convert the 80 kDa
hemolysin precursor into the active 65 kDa hemolysin.
-!- SIMILARITY: Belongs to the HlyA hemolysin family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Y00557; CAA68637.1; -; Genomic_DNA.
EMBL; M36855; AAA27528.1; -; Genomic_DNA.
EMBL; X51746; CAA36035.1; -; Genomic_DNA.
EMBL; AE003853; AAF96131.1; -; Genomic_DNA.
PIR; A41462; A41462.
PIR; A82486; A82486.
RefSeq; NP_232618.1; NC_002506.1.
PDB; 1XEZ; X-ray; 2.30 A; A=26-741.
PDB; 3O44; X-ray; 2.88 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=149-741.
PDB; 4GX7; X-ray; 2.85 A; A/B/C/D/E/F=611-741.
PDBsum; 1XEZ; -.
PDBsum; 3O44; -.
PDBsum; 4GX7; -.
ProteinModelPortal; P09545; -.
SMR; P09545; -.
MINT; P09545; -.
STRING; 243277.VCA0219; -.
TCDB; 1.C.14.1.1; the cytohemolysin (chl) family.
UniLectin; P09545; -.
PRIDE; P09545; -.
DNASU; 2612877; -.
EnsemblBacteria; AAF96131; AAF96131; VC_A0219.
GeneID; 2612877; -.
KEGG; vch:VCA0219; -.
PATRIC; fig|243277.26.peg.2852; -.
eggNOG; ENOG4106M3D; Bacteria.
eggNOG; ENOG410YBQ4; LUCA.
KO; K10948; -.
OMA; HVAFYLN; -.
BioCyc; VCHO:VCA0219-MONOMER; -.
EvolutionaryTrace; P09545; -.
Proteomes; UP000000584; Chromosome 2.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0044179; P:hemolysis in other organism; IEA:UniProtKB-KW.
CDD; cd00161; RICIN; 1.
Gene3D; 2.100.10.30; -; 1.
InterPro; IPR032496; Hemolysin_beta-prism_lec.
InterPro; IPR022220; Hemolysin_N.
InterPro; IPR036404; Jacalin-like_lectin_dom_sf.
InterPro; IPR016183; Leukocidin/Hemolysin_toxin.
InterPro; IPR036435; Leukocidin/porin_MspA_sf.
InterPro; IPR035992; Ricin_B-like_lectins.
InterPro; IPR000772; Ricin_B_lectin.
Pfam; PF16458; Beta-prism_lec; 1.
Pfam; PF12563; Hemolysin_N; 1.
Pfam; PF07968; Leukocidin; 1.
SMART; SM00458; RICIN; 1.
SUPFAM; SSF50370; SSF50370; 1.
SUPFAM; SSF56959; SSF56959; 1.
PROSITE; PS50231; RICIN_B_LECTIN; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytolysis; Direct protein sequencing;
Disulfide bond; Hemolysis; Host cell membrane; Host membrane; Lectin;
Membrane; Reference proteome; Secreted; Signal; Toxin; Transmembrane;
Transmembrane beta strand.
SIGNAL 1 25 {ECO:0000269|PubMed:2174833}.
PROPEP 26 157 {ECO:0000269|PubMed:2174833}.
/FTId=PRO_0000013357.
CHAIN 158 741 Hemolysin.
/FTId=PRO_0000013358.
DOMAIN 484 575 Ricin B-type lectin.
{ECO:0000255|PROSITE-ProRule:PRU00174}.
REGION 607 741 Beta-prism domain.
SITE 144 145 Susceptible to proteolytic cleavage.
SITE 148 149 Susceptible to proteolytic cleavage.
DISULFID 182 200 {ECO:0000255|PROSITE-ProRule:PRU00174,
ECO:0000269|PubMed:15978620}.
DISULFID 497 511 {ECO:0000255|PROSITE-ProRule:PRU00174,
ECO:0000269|PubMed:15978620}.
DISULFID 537 549 {ECO:0000255|PROSITE-ProRule:PRU00174,
ECO:0000269|PubMed:15978620}.
VARIANT 245 741 Missing (in strain: nonhemolytic 569B).
VARIANT 453 453 S -> F (in strain: N16961).
CONFLICT 115 115 T -> S (in Ref. 3; AAA27528).
{ECO:0000305}.
CONFLICT 562 562 G -> S (in Ref. 3; AAA27528).
{ECO:0000305}.
STRAND 47 51 {ECO:0000244|PDB:1XEZ}.
HELIX 52 56 {ECO:0000244|PDB:1XEZ}.
HELIX 65 72 {ECO:0000244|PDB:1XEZ}.
STRAND 78 82 {ECO:0000244|PDB:1XEZ}.
HELIX 89 103 {ECO:0000244|PDB:1XEZ}.
STRAND 109 117 {ECO:0000244|PDB:1XEZ}.
STRAND 120 128 {ECO:0000244|PDB:1XEZ}.
TURN 161 163 {ECO:0000244|PDB:1XEZ}.
STRAND 166 176 {ECO:0000244|PDB:1XEZ}.
TURN 179 182 {ECO:0000244|PDB:1XEZ}.
STRAND 183 186 {ECO:0000244|PDB:1XEZ}.
TURN 189 193 {ECO:0000244|PDB:1XEZ}.
STRAND 196 199 {ECO:0000244|PDB:1XEZ}.
STRAND 204 217 {ECO:0000244|PDB:1XEZ}.
STRAND 219 221 {ECO:0000244|PDB:1XEZ}.
STRAND 229 236 {ECO:0000244|PDB:1XEZ}.
TURN 238 240 {ECO:0000244|PDB:1XEZ}.
STRAND 244 246 {ECO:0000244|PDB:1XEZ}.
STRAND 253 257 {ECO:0000244|PDB:1XEZ}.
STRAND 263 287 {ECO:0000244|PDB:1XEZ}.
STRAND 291 299 {ECO:0000244|PDB:1XEZ}.
STRAND 306 317 {ECO:0000244|PDB:1XEZ}.
TURN 321 323 {ECO:0000244|PDB:1XEZ}.
HELIX 327 329 {ECO:0000244|PDB:1XEZ}.
STRAND 336 347 {ECO:0000244|PDB:1XEZ}.
STRAND 351 356 {ECO:0000244|PDB:1XEZ}.
STRAND 359 361 {ECO:0000244|PDB:1XEZ}.
STRAND 363 369 {ECO:0000244|PDB:1XEZ}.
HELIX 376 378 {ECO:0000244|PDB:1XEZ}.
HELIX 395 397 {ECO:0000244|PDB:1XEZ}.
HELIX 400 402 {ECO:0000244|PDB:1XEZ}.
STRAND 410 417 {ECO:0000244|PDB:1XEZ}.
STRAND 422 445 {ECO:0000244|PDB:1XEZ}.
STRAND 450 457 {ECO:0000244|PDB:1XEZ}.
STRAND 463 474 {ECO:0000244|PDB:1XEZ}.
HELIX 478 481 {ECO:0000244|PDB:1XEZ}.
STRAND 486 490 {ECO:0000244|PDB:1XEZ}.
TURN 491 495 {ECO:0000244|PDB:1XEZ}.
STRAND 496 500 {ECO:0000244|PDB:1XEZ}.
STRAND 505 509 {ECO:0000244|PDB:1XEZ}.
HELIX 516 518 {ECO:0000244|PDB:1XEZ}.
STRAND 520 522 {ECO:0000244|PDB:1XEZ}.
STRAND 528 530 {ECO:0000244|PDB:1XEZ}.
STRAND 533 537 {ECO:0000244|PDB:1XEZ}.
HELIX 553 555 {ECO:0000244|PDB:1XEZ}.
STRAND 557 559 {ECO:0000244|PDB:1XEZ}.
STRAND 566 568 {ECO:0000244|PDB:1XEZ}.
TURN 569 571 {ECO:0000244|PDB:1XEZ}.
STRAND 574 578 {ECO:0000244|PDB:1XEZ}.
TURN 579 581 {ECO:0000244|PDB:1XEZ}.
STRAND 584 589 {ECO:0000244|PDB:1XEZ}.
STRAND 598 604 {ECO:0000244|PDB:1XEZ}.
STRAND 620 626 {ECO:0000244|PDB:1XEZ}.
STRAND 632 647 {ECO:0000244|PDB:1XEZ}.
STRAND 657 663 {ECO:0000244|PDB:1XEZ}.
STRAND 667 677 {ECO:0000244|PDB:1XEZ}.
STRAND 680 691 {ECO:0000244|PDB:1XEZ}.
STRAND 696 700 {ECO:0000244|PDB:1XEZ}.
STRAND 705 714 {ECO:0000244|PDB:1XEZ}.
STRAND 721 728 {ECO:0000244|PDB:1XEZ}.
STRAND 733 740 {ECO:0000244|PDB:1XEZ}.
SEQUENCE 741 AA; 81962 MW; C99FAE2A01F37CCE CRC64;
MPKLNRCAIA IFTILSAISS PTLLANINEP SGEAADIISQ VADSHAIKYY NAADWQAEDN
ALPSLAELRD LVINQQKRVL VDFSQISDAE GQAEMQAQFR KAYGVGFANQ FIVITEHKGE
LLFTPFDQAE EVDPQLLEAP RTARLLARSG FASPAPANSE TNTLPHVAFY ISVNRAISDE
ECTFNNSWLW KNEKGSRPFC KDANISLIYR VNLERSLQYG IVGSATPDAK IVRISLDDDS
TGAGIHLNDQ LGYRQFGASY TTLDAYFREW STDAIAQDYR FVFNASNNKA QILKTFPVDN
INEKFERKEV SGFELGVTGG VEVSGDGPKA KLEARASYTQ SRWLTYNTQD YRIERNAKNA
QAVSFTWNRQ QYATAESLLN RSTDALWVNT YPVDVNRISP LSYASFVPKM DVIYKASATE
TGSTDFIIDS SVNIRPIYNG AYKHYYVVGA HQSYHGFEDT PRRRITKSAS FTVDWDHPVF
TGGRPVNLQL ASFNNRCIQV DAQGRLAANT CDSQQSAQSF IYDQLGRYVS ASNTKLCLDG
EALDALQPCN QNLTQRWEWR KGTDELTNVY SGESLGHDKQ TGELGLYASS NDAVSLRTIT
AYTDVFNAQE SSPILGYTQG KMNQQRVGQD HRLYVRAGAA IDALGSASDL LVGGNGGSLS
SVDLSGVKSI TATSGDFQYG GQQLVALTFT YQDGRQQTVG SKAYVTNAHE DRFDLPAAAK
ITQLKIWSDD WLVKGVQFDL N


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