ID   LIP1_PHOLU              Reviewed;         645 AA.
AC   P40601;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   02-SEP-2026, entry version 101.
DE   RecName: Full=Lipase 1;
DE            EC=3.1.1.3;
DE   AltName: Full=Triacylglycerol lipase;
DE   Flags: Precursor;
GN   Name=lip-1;
OS   Photorhabdus luminescens (Xenorhabdus luminescens).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=29488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 25-41.
RC   STRAIN=K122;
RX   PubMed=8449874; DOI=10.1128/jb.175.6.1665-1673.1993;
RA   Wang H., Dowds B.C.A.;
RT   "Phase variation in Xenorhabdus luminescens: cloning and sequencing of the
RT   lipase gene and analysis of its expression in primary and secondary phases
RT   of the bacterium.";
RL   J. Bacteriol. 175:1665-1673(1993).
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   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC       {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; X66379; CAA47020.1; -; Genomic_DNA.
DR   PIR; A47081; A47081.
DR   AlphaFoldDB; P40601; -.
DR   SMR; P40601; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019867; C:outer membrane; IEA:InterPro.
DR   GO; GO:0004806; F:triacylglycerol lipase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   CDD; cd01847; Triacylglycerol_lipase_like; 1.
DR   Gene3D; 2.40.128.130; Autotransporter beta-domain; 1.
DR   Gene3D; 3.40.50.1110; SGNH hydrolase; 1.
DR   InterPro; IPR005546; Autotransporte_beta.
DR   InterPro; IPR036709; Autotransporte_beta_dom_sf.
DR   InterPro; IPR001087; GDSL.
DR   InterPro; IPR017186; Lipase_autotranspt_EstA.
DR   InterPro; IPR008265; Lipase_GDSL_AS.
DR   InterPro; IPR006315; OM_autotransptr_brl_dom.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   NCBIfam; TIGR01414; autotrans_barl; 1.
DR   PANTHER; PTHR22835:SF659; GDSL LIPASE_ACYLHYDROLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G00510)-RELATED; 1.
DR   PANTHER; PTHR22835; ZINC FINGER FYVE DOMAIN CONTAINING PROTEIN; 1.
DR   Pfam; PF03797; Autotransporter; 1.
DR   Pfam; PF00657; Lipase_GDSL; 1.
DR   PIRSF; PIRSF037375; Autotrns_EstA; 1.
DR   SMART; SM00869; Autotransporter; 1.
DR   SUPFAM; SSF103515; Autotransporter; 1.
DR   SUPFAM; SSF52266; SGNH hydrolase; 1.
DR   PROSITE; PS51208; AUTOTRANSPORTER; 1.
DR   PROSITE; PS01098; LIPASE_GDSL_SER; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:8449874"
FT   CHAIN           25..645
FT                   /note="Lipase 1"
FT                   /id="PRO_0000017843"
FT   DOMAIN          383..645
FT                   /note="Autotransporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00556"
FT   ACT_SITE        34
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        327
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        330
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   645 AA;  70717 MW;  1271327B7C56932F CRC64;
     MKRSFIFAPG MLALSISAIS NAHAYNNLYV FGDSLSDGGN NGRYTVDGIN GTESKLYNDF
     IAQQLGIELV NSKKGGTNYA AGGATAVADL NNKHNTQDQV MGYLASHSNR ADHNGMYVHW
     IGGNDVDAAL RNPADAQKII TESAMAASSQ VHALLNAGAG LVIVPTVPDV GMTPKIMEFV
     LSKGGATSKD LAKIHAVVNG YPTIDKDTRL QVIHGVFKQI GSDVSGGDAK KAEETTKQLI
     DGYNELSSNA SKLVDNYNQL EDMALSQENG NIVRVDVNAL LHEVIANPLR YGFLNTIGYA
     CAQGVNAGSC RSKDTGFDAS KPFLFADDFH PTPEAHHIVS QYTVSVLNAP YRVMLLTNAN
     NVPVKGALAS LDGRLQQLRN VDNEQGKLGV FGGYSGNHSH TLTLGSDYQI MDNILLGGMI
     SRYQDNSSPA DNFHYDGRGY VFTAYGLWRY YDKGWISGDL HYLDMKYEDI TRGIVLNDWL
     RKENASTSGH QWGGRITAGW DIPLTSAVTT SPIIQYAWDK SYVKGYRESG NNSTAMHFGE
     QRYDSQVGTL GWRLDTNFGY FNPYAEVRFN HQFGDKRYQI RSAINSTQTS FVSESQKQDT
     HWREYTIGMN AVITKDWGAF ASISRNDGDV QNHTYSFSLG VNASF
//