ID   LIP1_PSYIM              Reviewed;         317 AA.
AC   Q02104;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Lipase 1;
DE            EC=3.1.1.3;
DE   AltName: Full=Triacylglycerol lipase;
DE   Flags: Precursor;
GN   Name=lip1;
OS   Psychrobacter immobilis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Psychrobacter.
OX   NCBI_TaxID=498;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC   STRAIN=B10;
RX   PubMed=7916627; DOI=10.1016/0167-4781(93)90078-r;
RA   Arpigny J.L., Feller G., Gerday C.;
RT   "Cloning, sequence and structural features of a lipase from the antarctic
RT   facultative psychrophile Psychrobacter immobilis B10.";
RL   Biochim. Biophys. Acta 1171:331-333(1993).
RN   [2]
RP   ERRATUM OF PUBMED:7916627, AND SEQUENCE REVISION.
RX   PubMed=7632728; DOI=10.1016/0167-4781(95)00086-v;
RA   Arpigny J.L., Feller G., Gerday C.;
RL   Biochim. Biophys. Acta 1263:103-103(1995).
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Active at temperatures close to 0 degree Celsius.;
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000255|PROSITE-ProRule:PRU00303}.
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DR   EMBL; X67712; CAA47949.1; -; Genomic_DNA.
DR   PIR; S57274; S57274.
DR   PIR; S57275; S57275.
DR   AlphaFoldDB; Q02104; -.
DR   SMR; Q02104; -.
DR   ESTHER; psyim-1lip; ABHD6-Lip.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
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   InterPro; IPR000639; Epox_hydrolase-like.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   PRINTS; PR00412; EPOXHYDRLASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   Cell outer membrane; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Lipoprotein; Membrane; Palmitate; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           19..317
FT                   /note="Lipase 1"
FT                   /id="PRO_0000017730"
FT   DOMAIN          69..296
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        74
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        142
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        270
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        292
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   LIPID           19
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           19
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   317 AA;  35252 MW;  2ACF344644D54B5C CRC64;
     MLLKRLCFAA LFSLSMVGCT NAPNALAVNT TQKIIQYERN KSDLEIKSLT LASGDKMVYA
     ENGNVAGEPL LLIHGFGGNK DNFTRIARQL EGYHLIIPDL LGFGESSKPM SADYRSEAQR
     TRLHELLQAK GLASNIHVGG NSMGGAISVA YAAKYPKDVK SLWLVDSAGF WSAGIPKSLE
     GATLENNPLL IKSNEDFYKM YDFVMYKPPY LPKSVKAVFA QERIKNKELD AKILEQIVTD
     NVEERAKIIA QYKIPTLVVW GDKDQIIKPE TVNLIKKIIP QAQVIMMEDV GHVPMVEALD
     ETADNYKAFR SILEAQR