HLYA_VIBCH
ID HLYA_VIBCH Reviewed; 741 AA.
AC P09545; O08197; O08290; Q56641; Q99290; Q9KMU9;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Hemolysin;
DE Flags: Precursor;
GN Name=hlyA; OrderedLocusNames=VC_A0219;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=El Tor O17 / Serotype O1;
RX PubMed=3050359; DOI=10.1111/j.1365-2958.1988.tb00054.x;
RA Alm R.A., Stroeher U.H., Manning P.A.;
RT "Extracellular proteins of Vibrio cholerae: nucleotide sequence of the
RT structural gene (hlyA) for the haemolysin of the haemolytic El Tor strain
RT O17 and characterization of the hlyA mutation in the non-haemolytic
RT classical strain 569B.";
RL Mol. Microbiol. 2:481-488(1988).
RN [2]
RP SEQUENCE REVISION.
RA Manning P.A.;
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=El Tor RV79;
RX PubMed=2453464; DOI=10.1128/iai.56.6.1414-1419.1988;
RA Rader A.E., Murphy J.R.;
RT "Nucleotide sequences and comparison of the hemolysin determinants of
RT Vibrio cholerae El Tor RV79(Hly+) and RV79(Hly-) and classical
RT 569B(Hly-).";
RL Infect. Immun. 56:1414-1419(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 26-45 AND
RP 158-177.
RC STRAIN=El Tor N86 / Serotype O1;
RX PubMed=2174833; DOI=10.1128/iai.58.12.4106-4116.1990;
RA Yamamoto K., Ichinose Y., Shinagawa H., Makino K., Nakata A., Iwanaga M.,
RA Honda T., Miwatani T.;
RT "Two-step processing for activation of the cytolysin/hemolysin of Vibrio
RT cholerae O1 biotype El Tor: nucleotide sequence of the structural gene
RT (hlyA) and characterization of the processed products.";
RL Infect. Immun. 58:4106-4116(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 26-741, SUBUNIT, FUNCTION, PARTIAL
RP PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVATION BY
RP PROTEOLYTIC CLEAVAGE, SUBCELLULAR LOCATION, DOMAIN, AND DISULFIDE BONDS.
RX PubMed=15978620; DOI=10.1016/j.jmb.2005.05.045;
RA Olson R., Gouaux E.;
RT "Crystal structure of the Vibrio cholerae cytolysin (VCC) pro-toxin and its
RT assembly into a heptameric transmembrane pore.";
RL J. Mol. Biol. 350:997-1016(2005).
CC -!- FUNCTION: Bacterial hemolysin that causes cytolysis by forming
CC heptameric pores in target host membranes.
CC {ECO:0000269|PubMed:15978620}.
CC -!- SUBUNIT: Monomer. Homoheptamer. After binding to target membranes the
CC protein assembles into a heptameric pre-pore complex. Proteolytic
CC cleavage triggers a conformation change that is required for membrane
CC insertion and pore formation. {ECO:0000269|PubMed:15978620}.
CC -!- INTERACTION:
CC P09545; P09545: hlyA; NbExp=4; IntAct=EBI-6409539, EBI-6409539;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15978620}. Host cell
CC membrane {ECO:0000269|PubMed:15978620}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15978620}. Note=In the hemolytic biotype El Tor the
CC 80 kDa hemolysin precursor is secreted as monomer. After binding to
CC target membranes the protein assembles into a heptameric prepore
CC complex. Proteolytic cleavage triggers a conformation change that is
CC required for membrane insertion and pore formation.
CC -!- INDUCTION: By hemolysin B cytoplasmic protein. {ECO:0000305}.
CC -!- DOMAIN: May bind to glycans on target cells via the C-terminal beta-
CC prism domain. {ECO:0000269|PubMed:15978620}.
CC -!- PTM: Proteolytical cleavage is required to convert the 80 kDa hemolysin
CC precursor into the active 65 kDa hemolysin.
CC -!- SIMILARITY: Belongs to the HlyA hemolysin family. {ECO:0000305}.
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DR EMBL; Y00557; CAA68637.1; -; Genomic_DNA.
DR EMBL; M36855; AAA27528.1; -; Genomic_DNA.
DR EMBL; X51746; CAA36035.1; -; Genomic_DNA.
DR EMBL; AE003853; AAF96131.1; -; Genomic_DNA.
DR PIR; A41462; A41462.
DR PIR; A82486; A82486.
DR RefSeq; NP_232618.1; NC_002506.1.
DR PDB; 1XEZ; X-ray; 2.30 A; A=26-741.
DR PDB; 3O44; X-ray; 2.88 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=149-741.
DR PDB; 4GX7; X-ray; 2.85 A; A/B/C/D/E/F=611-741.
DR PDBsum; 1XEZ; -.
DR PDBsum; 3O44; -.
DR PDBsum; 4GX7; -.
DR AlphaFoldDB; P09545; -.
DR SMR; P09545; -.
DR MINT; P09545; -.
DR STRING; 243277.VC_A0219; -.
DR TCDB; 1.C.14.1.1; the cytohemolysin (chl) family.
DR UniLectin; P09545; -.
DR DNASU; 2612877; -.
DR EnsemblBacteria; AAF96131; AAF96131; VC_A0219.
DR GeneID; 57741666; -.
DR KEGG; vch:VC_A0219; -.
DR PATRIC; fig|243277.26.peg.2852; -.
DR eggNOG; ENOG502ZBG7; Bacteria.
DR HOGENOM; CLU_439829_0_0_6; -.
DR OMA; HVAFYLN; -.
DR BioCyc; VCHO:VCA0219-MON; -.
DR EvolutionaryTrace; P09545; -.
DR Proteomes; UP000000584; Chromosome 2.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.100.10.30; -; 1.
DR Gene3D; 3.30.110.130; -; 1.
DR Gene3D; 6.20.40.20; -; 1.
DR InterPro; IPR032496; Hemolysin_beta-prism_lec.
DR InterPro; IPR022220; Hemolysin_N.
DR InterPro; IPR043080; Hemolysin_N_sf.
DR InterPro; IPR044883; Hemolysin_pre-stem_dom_sf.
DR InterPro; IPR036404; Jacalin-like_lectin_dom_sf.
DR InterPro; IPR016183; Leukocidin/Hemolysin_toxin.
DR InterPro; IPR036435; Leukocidin/porin_MspA_sf.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR Pfam; PF16458; Beta-prism_lec; 1.
DR Pfam; PF12563; Hemolysin_N; 1.
DR Pfam; PF07968; Leukocidin; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF50370; SSF50370; 1.
DR SUPFAM; SSF56959; SSF56959; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytolysis; Direct protein sequencing; Disulfide bond;
KW Hemolysis; Host cell membrane; Host membrane; Lectin; Membrane;
KW Reference proteome; Secreted; Signal; Toxin; Transmembrane;
KW Transmembrane beta strand; Virulence.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:2174833"
FT PROPEP 26..157
FT /evidence="ECO:0000269|PubMed:2174833"
FT /id="PRO_0000013357"
FT CHAIN 158..741
FT /note="Hemolysin"
FT /id="PRO_0000013358"
FT DOMAIN 484..575
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 607..741
FT /note="Beta-prism domain"
FT SITE 144..145
FT /note="Susceptible to proteolytic cleavage"
FT SITE 148..149
FT /note="Susceptible to proteolytic cleavage"
FT DISULFID 182..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0000269|PubMed:15978620"
FT DISULFID 497..511
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0000269|PubMed:15978620"
FT DISULFID 537..549
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0000269|PubMed:15978620"
FT VARIANT 245..741
FT /note="Missing (in strain: nonhemolytic 569B)"
FT VARIANT 453
FT /note="S -> F (in strain: N16961)"
FT CONFLICT 115
FT /note="T -> S (in Ref. 3; AAA27528)"
FT /evidence="ECO:0000305"
FT CONFLICT 562
FT /note="G -> S (in Ref. 3; AAA27528)"
FT /evidence="ECO:0000305"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:1XEZ"
FT HELIX 52..56
FT /evidence="ECO:0007829|PDB:1XEZ"
FT HELIX 65..72
FT /evidence="ECO:0007829|PDB:1XEZ"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:1XEZ"
FT HELIX 89..103
FT /evidence="ECO:0007829|PDB:1XEZ"
FT STRAND 109..117
FT /evidence="ECO:0007829|PDB:1XEZ"
FT STRAND 120..128
FT /evidence="ECO:0007829|PDB:1XEZ"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:1XEZ"
FT STRAND 166..176
FT /evidence="ECO:0007829|PDB:1XEZ"
FT TURN 179..182
FT /evidence="ECO:0007829|PDB:1XEZ"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:1XEZ"
FT TURN 189..193
FT /evidence="ECO:0007829|PDB:1XEZ"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:1XEZ"
FT STRAND 204..217
FT /evidence="ECO:0007829|PDB:1XEZ"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:1XEZ"
FT STRAND 229..236
FT /evidence="ECO:0007829|PDB:1XEZ"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:1XEZ"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:1XEZ"
FT STRAND 253..257
FT /evidence="ECO:0007829|PDB:1XEZ"
FT STRAND 263..287
FT /evidence="ECO:0007829|PDB:1XEZ"
FT STRAND 291..299
FT /evidence="ECO:0007829|PDB:1XEZ"
FT STRAND 306..317
FT /evidence="ECO:0007829|PDB:1XEZ"
FT TURN 321..323
FT /evidence="ECO:0007829|PDB:1XEZ"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:1XEZ"
FT STRAND 336..347
FT /evidence="ECO:0007829|PDB:1XEZ"
FT STRAND 351..356
FT /evidence="ECO:0007829|PDB:1XEZ"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:1XEZ"
FT STRAND 363..369
FT /evidence="ECO:0007829|PDB:1XEZ"
FT HELIX 376..378
FT /evidence="ECO:0007829|PDB:1XEZ"
FT HELIX 395..397
FT /evidence="ECO:0007829|PDB:1XEZ"
FT HELIX 400..402
FT /evidence="ECO:0007829|PDB:1XEZ"
FT STRAND 410..417
FT /evidence="ECO:0007829|PDB:1XEZ"
FT STRAND 422..445
FT /evidence="ECO:0007829|PDB:1XEZ"
FT STRAND 450..457
FT /evidence="ECO:0007829|PDB:1XEZ"
FT STRAND 463..474
FT /evidence="ECO:0007829|PDB:1XEZ"
FT HELIX 478..481
FT /evidence="ECO:0007829|PDB:1XEZ"
FT STRAND 486..490
FT /evidence="ECO:0007829|PDB:1XEZ"
FT TURN 491..495
FT /evidence="ECO:0007829|PDB:1XEZ"
FT STRAND 496..500
FT /evidence="ECO:0007829|PDB:1XEZ"
FT STRAND 505..509
FT /evidence="ECO:0007829|PDB:1XEZ"
FT HELIX 516..518
FT /evidence="ECO:0007829|PDB:1XEZ"
FT STRAND 520..522
FT /evidence="ECO:0007829|PDB:1XEZ"
FT STRAND 528..530
FT /evidence="ECO:0007829|PDB:1XEZ"
FT STRAND 533..537
FT /evidence="ECO:0007829|PDB:1XEZ"
FT HELIX 553..555
FT /evidence="ECO:0007829|PDB:1XEZ"
FT STRAND 557..559
FT /evidence="ECO:0007829|PDB:1XEZ"
FT STRAND 566..568
FT /evidence="ECO:0007829|PDB:1XEZ"
FT TURN 569..571
FT /evidence="ECO:0007829|PDB:1XEZ"
FT STRAND 574..578
FT /evidence="ECO:0007829|PDB:1XEZ"
FT TURN 579..581
FT /evidence="ECO:0007829|PDB:1XEZ"
FT STRAND 584..589
FT /evidence="ECO:0007829|PDB:1XEZ"
FT STRAND 592..595
FT /evidence="ECO:0007829|PDB:3O44"
FT STRAND 598..604
FT /evidence="ECO:0007829|PDB:1XEZ"
FT STRAND 614..616
FT /evidence="ECO:0007829|PDB:3O44"
FT STRAND 620..626
FT /evidence="ECO:0007829|PDB:1XEZ"
FT STRAND 632..647
FT /evidence="ECO:0007829|PDB:1XEZ"
FT HELIX 648..650
FT /evidence="ECO:0007829|PDB:3O44"
FT STRAND 657..663
FT /evidence="ECO:0007829|PDB:1XEZ"
FT STRAND 667..677
FT /evidence="ECO:0007829|PDB:1XEZ"
FT STRAND 680..691
FT /evidence="ECO:0007829|PDB:1XEZ"
FT STRAND 696..700
FT /evidence="ECO:0007829|PDB:1XEZ"
FT STRAND 705..714
FT /evidence="ECO:0007829|PDB:1XEZ"
FT STRAND 721..728
FT /evidence="ECO:0007829|PDB:1XEZ"
FT STRAND 733..740
FT /evidence="ECO:0007829|PDB:1XEZ"
SQ 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
