LIP_VIBCH
ID LIP_VIBCH Reviewed; 312 AA.
AC P15493; O07349; Q9KMU7;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Triacylglycerol lipase {ECO:0000303|PubMed:9371455};
DE EC=3.1.1.3 {ECO:0000250|UniProtKB:P26876};
DE AltName: Full=Extracellular lipase {ECO:0000250|UniProtKB:P26876};
DE AltName: Full=Triacylglycerol ester hydrolase {ECO:0000250|UniProtKB:P26876};
DE Flags: Precursor;
GN Name=hlyC {ECO:0000303|PubMed:2162464};
GN Synonyms=lipA {ECO:0000303|PubMed:9371455}; OrderedLocusNames=VC_A0221;
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=2162464; DOI=10.1111/j.1365-2958.1990.tb00608.x;
RA Alm R.A., Manning P.A.;
RT "Characterization of the hlyB gene and its role in the production of the El
RT Tor haemolysin of Vibrio cholerae O1.";
RL Mol. Microbiol. 4:413-425(1990).
RN [2]
RP IDENTIFICATION, AND SEQUENCE REVISION.
RA Manning P.A.;
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP FUNCTION, AND INDUCTION.
RX PubMed=8817490; DOI=10.1111/j.1365-2958.1995.mmi_18040671.x;
RA Camilli A., Mekalanos J.J.;
RT "Use of recombinase gene fusions to identify Vibrio cholerae genes induced
RT during infection.";
RL Mol. Microbiol. 18:671-683(1995).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, DISULFIDE BOND, AND NOMENCLATURE.
RC STRAIN=El Tor O17 / Serotype O1;
RX PubMed=9371455; DOI=10.1128/jb.179.22.7072-7080.1997;
RA Ogierman M.A., Fallarino A., Riess T., Williams S.G., Attridge S.R.,
RA Manning P.A.;
RT "Characterization of the Vibrio cholerae El Tor lipase operon lipAB and a
RT protease gene downstream of the hly region.";
RL J. Bacteriol. 179:7072-7080(1997).
CC -!- FUNCTION: Catalyzes the hydrolysis of triacylglycerol.
CC {ECO:0000269|PubMed:9371455, ECO:0000305|PubMed:8817490}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid +
CC H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3;
CC Evidence={ECO:0000250|UniProtKB:P26876};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P26876};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P26876};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P26876}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P26876}.
CC -!- INDUCTION: During infection. {ECO:0000269|PubMed:8817490}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene do not show lipase
CC activity. {ECO:0000269|PubMed:9371455}.
CC -!- MISCELLANEOUS: The lipase chaperone LifO is required for the folding of
CC this protein during its passage through the periplasm.
CC {ECO:0000269|PubMed:9371455}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Pseudomonas lipase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF96133.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y00557; CAA68639.1; -; Genomic_DNA.
DR EMBL; AE003853; AAF96133.1; ALT_INIT; Genomic_DNA.
DR PIR; C82486; C82486.
DR PIR; S15911; S15911.
DR RefSeq; NP_232620.2; NC_002506.1.
DR RefSeq; WP_001033424.1; NZ_LT906615.1.
DR AlphaFoldDB; P15493; -.
DR SMR; P15493; -.
DR STRING; 243277.VC_A0221; -.
DR ESTHER; vibch-lipas; Bacterial_lip_FamI.1.
DR DNASU; 2612550; -.
DR EnsemblBacteria; AAF96133; AAF96133; VC_A0221.
DR GeneID; 57741668; -.
DR KEGG; vch:VC_A0221; -.
DR PATRIC; fig|243277.26.peg.2854; -.
DR eggNOG; COG1075; Bacteria.
DR HOGENOM; CLU_062016_0_0_6; -.
DR OMA; YYFSWSG; -.
DR Proteomes; UP000000584; Chromosome 2.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW Calcium; Disulfide bond; Hydrolase; Lipid degradation; Lipid metabolism;
KW Metal-binding; Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..312
FT /note="Triacylglycerol lipase"
FT /id="PRO_0000017747"
FT DOMAIN 37..228
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 110
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P26876"
FT ACT_SITE 256
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P26876"
FT ACT_SITE 278
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P26876"
FT BINDING 44
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P22088"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26876"
FT BINDING 238
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P26876"
FT BINDING 280
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P26876"
FT BINDING 284
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P26876"
FT BINDING 288
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P26876"
FT DISULFID 212..262
FT /evidence="ECO:0000305|PubMed:9371455"
SQ SEQUENCE 312 AA; 32995 MW; 96AA000A07A568CD CRC64;
MNKIIILIAL SLFSSSIWAG TSAHALSQQG YTQTRYPIVL VHGLFGFDTL AGMDYFHGIP
QSLTRDGAQV YVAQVSATNS SERRGEQLLA QVESLLAVTG AKKVNLIGHS HGGPTIRYVA
SVRPDLVASV TSIGGVHKGS AVADLVRGVI PSGSVSEQVA VGLTQGLVAL IDLLSGGKAH
PQDPLASLAA LTTEGSLKFN QYYPEGVPTS ACGEGAYQVN GVRYYSWSGA ATVTNILDPS
DVAMGLIGLV FNEPNDGLVA TCSTHLGKVI RDDYRMNHLD EINGLLGIHS LFETDPVTLY
RQHANRLKQA GL
