ID   HLT_VIBPA               Reviewed;         418 AA.
AC   Q99289;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2003, sequence version 2.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=Thermolabile hemolysin;
DE            Short=TL;
DE   AltName: Full=Atypical phospholipase;
DE   AltName: Full=Lecithin-dependent hemolysin;
DE            Short=LDH;
DE   AltName: Full=Lysophospholipase;
DE   AltName: Full=Phospholipase A2;
DE   Flags: Precursor;
GN   OrderedLocusNames=VPA0226;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3508495; DOI=10.1016/0882-4010(86)90004-5;
RA   Taniguchi H., Hirano H., Kubomura S., Higashi K., Mizuguchi Y.;
RT   "Comparison of the nucleotide sequences of the genes for the thermostable
RT   direct hemolysin and the thermolabile hemolysin from Vibrio
RT   parahaemolyticus.";
RL   Microb. Pathog. 1:425-432(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
RN   [3]
RP   PROTEIN SEQUENCE OF 20-47, AND CHARACTERIZATION.
RX   PubMed=1791426; DOI=10.1099/00221287-137-12-2705;
RA   Shinoda S., Matsuoka H., Tsuchie T., Miyoshi S., Yamamoto S., Taniguchi H.,
RA   Mizuguchi Y.;
RT   "Purification and characterization of a lecithin-dependent haemolysin from
RT   Escherichia coli transformed by a Vibrio parahaemolyticus gene.";
RL   J. Gen. Microbiol. 137:2705-2711(1991).
CC   -!- FUNCTION: Phospholipase hydrolyzing both fatty acid esters of
CC       phospholipid, i.e. it hydrolyzes phosphatidylcholine (PC) to
CC       lysophosphatidylcholine (LPC) and then LPC to glycerophosphorylcholine
CC       (GPC).
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: There are two forms of LDH. The LDH(S) may be a protein in which
CC       13 residues of the N-terminal of LDH(L) are deleted.
CC   -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; M36437; AAA27526.1; -; Genomic_DNA.
DR   EMBL; BA000032; BAC61569.1; -; Genomic_DNA.
DR   PIR; A53888; A53888.
DR   RefSeq; NP_799736.1; NC_004605.1.
DR   RefSeq; WP_005481504.1; NC_004605.1.
DR   AlphaFoldDB; Q99289; -.
DR   SMR; Q99289; -.
DR   STRING; 223926.28808364; -.
DR   PRIDE; Q99289; -.
DR   EnsemblBacteria; BAC61569; BAC61569; BAC61569.
DR   GeneID; 1190914; -.
DR   KEGG; vpa:VPA0226; -.
DR   PATRIC; fig|223926.6.peg.3181; -.
DR   eggNOG; COG3240; Bacteria.
DR   HOGENOM; CLU_045229_0_0_6; -.
DR   OMA; NSWFLGH; -.
DR   Proteomes; UP000002493; Chromosome 2.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016298; F:lipase activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1110; -; 1.
DR   InterPro; IPR001087; GDSL.
DR   InterPro; IPR008265; Lipase_GDSL_AS.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   Pfam; PF00657; Lipase_GDSL; 1.
DR   PROSITE; PS01098; LIPASE_GDSL_SER; 1.
PE   1: Evidence at protein level;
KW   Cytolysis; Direct protein sequencing; Hemolysis; Hydrolase;
KW   Lipid degradation; Lipid metabolism; Reference proteome; Secreted; Signal;
KW   Toxin; Virulence.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:1791426"
FT   CHAIN           20..418
FT                   /note="Thermolabile hemolysin"
FT                   /id="PRO_0000017849"
FT   ACT_SITE        153
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        390
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        393
FT                   /evidence="ECO:0000250"
FT   VARIANT         20..32
FT                   /note="Missing (in LDH(S))"
FT   CONFLICT        20
FT                   /note="A -> T (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        219
FT                   /note="E -> D (in Ref. 1; AAA27526)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        390
FT                   /note="D -> N (in Ref. 1; AAA27526)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   418 AA;  47392 MW;  DC59A641DD04B1BD CRC64;
     MMKKTITLLT ALLPLASAVA EEPTLSPEMV SASEVISTQE NQTYTYVRCW YRTSYSKDDP
     ATDWEWAKNE DGSYFTIDGY WWSSVSFKNM FYTNTSQNVI RQRCEATLDL ANENADITFF
     AADNRFSYNH TIWSNDAAMQ PDQINKVVAL GDSLSDTGNI FNASQWRFPN PNSWFLGHFS
     NGFVWTEYIA KAKNLPLYNW AVGGAAGENQ YIALTGVGEQ VSSYLTYAKL AKNYKPANTL
     FTLEFGLNDF MNYNRGVPEV KADYAEALIR LTDAGAKNFM LMTLPDATKA PQFKYSTQEE
     IDKIRAKVLE MNEFIKAQAM YYKAQGYNIT LFDTHALFET LTSAPEEHGF VNASDPCLDI
     NRSSSVDYMY THALRSECAA SGAEKFVFWD VTHPTTATHR YVAEKMLESS NNLAEYRF