ID   PA1_SERLI               Reviewed;         319 AA.
AC   P18952; Q6LBK6;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 2.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Extracellular phospholipase A1;
DE            EC=3.1.1.32;
DE   Flags: Precursor;
GN   Name=phlA;
OS   Serratia liquefaciens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3056919; DOI=10.1128/jb.170.12.5855-5862.1988;
RA   Givskov M., Olsen L., Molin S.;
RT   "Cloning and expression in Escherichia coli of the gene for extracellular
RT   phospholipase A1 from Serratia liquefaciens.";
RL   J. Bacteriol. 170:5855-5862(1988).
RN   [2]
RP   SEQUENCE REVISION TO 200-245, AND MUTAGENESIS OF GLY-228.
RX   PubMed=8316077; DOI=10.1111/j.1365-2958.1993.tb01567.x;
RA   Givskov M., Molin S.;
RT   "Secretion of Serratia liquefaciens phospholipase from Escherichia coli.";
RL   Mol. Microbiol. 8:229-242(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-119.
RX   PubMed=1640837; DOI=10.1111/j.1365-2958.1992.tb00857.x;
RA   Givskov M., Molin S.;
RT   "Expression of extracellular phospholipase from Serratia liquefaciens is
RT   growth-phase-dependent, catabolite-repressed and regulated by
RT   anaerobiosis.";
RL   Mol. Microbiol. 6:1363-1374(1992).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-
CC         glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC         ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32;
CC   -!- DEVELOPMENTAL STAGE: Growth phase regulated (late expression).
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DR   EMBL; M23640; AAA26552.1; ALT_SEQ; mRNA.
DR   EMBL; X66505; CAA47137.1; -; Genomic_DNA.
DR   PIR; S32923; S32923.
DR   AlphaFoldDB; P18952; -.
DR   SMR; P18952; -.
DR   ESTHER; serli-pa1; Duf_2974.
DR   GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008970; F:phospholipase A1 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   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Lipid degradation; Lipid metabolism; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..319
FT                   /note="Extracellular phospholipase A1"
FT                   /id="PRO_0000021990"
FT   MUTAGEN         228
FT                   /note="G->D: Loss of ability to bind PhlB."
FT                   /evidence="ECO:0000269|PubMed:8316077"
SQ   SEQUENCE   319 AA;  32848 MW;  FFEC47676E9A227B CRC64;
     MSMPLSFTSA VSPVAAIPTP RAAAETRTAA SLRHAGKSGP VASPSQNTLN AQNLLNTLVG
     DISAAAPTAA AAPGVTRGQQ SQEGDYALAL LAKDVYSLNG QGAAGFNRLS DSALLGFGID
     PASLHDAGSG FQAGIYSNDK QYVLAFAGTN DWRDWLSNVR QATGYDDVQY NQAVAAAKSA
     KAAFGDALVI AGHSLGGGLA ATAALATGTV AVTFNAAGVS DYTLNRLGID PAAAKKDAEA
     GGIRRYSEQY DMLTSTQEST SLIPDAIGHN ITLANNDTLT GIDDWRPSKH LDRSLTAHGI
     DKVISSMAEQ KPWEAKANA