ID   PLSC_NEIGO              Reviewed;         255 AA.
AC   Q59601;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase;
DE            Short=1-AGP acyltransferase;
DE            Short=1-AGPAT;
DE            EC=2.3.1.51;
DE   AltName: Full=Lysophosphatidic acid acyltransferase;
DE            Short=LPAAT;
GN   Name=plsC;
OS   Neisseria gonorrhoeae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FA19;
RX   PubMed=8748025; DOI=10.1111/j.1365-2958.1995.mmi_18030401.x;
RA   Swartley J.S., Balthazar J.T., Coleman J., Shafer W.M., Stephens D.S.;
RT   "Membrane glycerophospholipid biosynthesis in Neisseria meningitidis and
RT   Neisseria gonorrhoeae: identification, characterization, and mutagenesis of
RT   a lysophosphatidic acid acyltransferase.";
RL   Mol. Microbiol. 18:401-412(1995).
CC   -!- FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid
CC       by incorporating acyl moiety at the 2 position.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC         sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC         ChEBI:CHEBI:58608; EC=2.3.1.51;
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC       diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein.
CC   -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and
CC       may constitute the binding site for the phosphate moiety of the
CC       glycerol-3-phosphate. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC       acyltransferase family. {ECO:0000305}.
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DR   EMBL; U21806; AAB40877.1; -; Genomic_DNA.
DR   PIR; S70545; S70545.
DR   AlphaFoldDB; Q59601; -.
DR   SMR; Q59601; -.
DR   BRENDA; 2.3.1.51; 3590.
DR   UniPathway; UPA00557; UER00613.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR004552; AGP_acyltrans.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   SMART; SM00563; PlsC; 1.
DR   TIGRFAMs; TIGR00530; AGP_acyltrn; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cell inner membrane; Cell membrane; Lipid biosynthesis;
KW   Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW   Phospholipid metabolism; Transferase.
FT   CHAIN           1..255
FT                   /note="1-acyl-sn-glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_0000208174"
FT   MOTIF           78..83
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   255 AA;  27830 MW;  833F080361A5CE88 CRC64;
     MSSNKASFFT RLRRLCRLTV WLFKTGKNLR GIDGGCPKSR NRAVIALGKG ALAALDIGLE
     VGRPAPEHPN GVLVAANHVS WLDIFAMSAV YPSSFIAKQE IKSWPVLGKM GQNAGTVFIN
     RNSRRDIEPI NRAVCETLQR GQNVSFFPEA RTSSGLGLLP FKAALFQSAI DAGAKVLAVA
     LRYYDETGKR TARPSYADVG LPTCLWRIVS MKKLTIKVDF VCVADAAESE DRYALKDKIE
     ESIRAVVADD ADIAV