ID   PLSC_MYCPN              Reviewed;         266 AA.
AC   P75479;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Probable 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; OrderedLocusNames=MPN_299; ORFNames=MP537;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
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   -!- 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}.
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; U00089; AAB96185.1; -; Genomic_DNA.
DR   PIR; S73863; S73863.
DR   RefSeq; NP_109987.1; NC_000912.1.
DR   RefSeq; WP_010874656.1; NC_000912.1.
DR   AlphaFoldDB; P75479; -.
DR   SMR; P75479; -.
DR   STRING; 272634.MPN_299; -.
DR   PRIDE; P75479; -.
DR   EnsemblBacteria; AAB96185; AAB96185; MPN_299.
DR   GeneID; 66609054; -.
DR   KEGG; mpn:MPN_299; -.
DR   PATRIC; fig|272634.6.peg.323; -.
DR   HOGENOM; CLU_027938_6_1_14; -.
DR   OMA; RLMGITM; -.
DR   BioCyc; MPNE272634:G1GJ3-468-MON; -.
DR   UniPathway; UPA00557; UER00613.
DR   Proteomes; UP000000808; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
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; Lipid biosynthesis; Lipid metabolism;
KW   Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW   Transferase.
FT   CHAIN           1..266
FT                   /note="Probable 1-acyl-sn-glycerol-3-phosphate
FT                   acyltransferase"
FT                   /id="PRO_0000208173"
FT   MOTIF           92..97
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   266 AA;  30414 MW;  79D933AD8203927F CRC64;
     MKKLTQAFLR FCLRFLQLLS LVLVLPVFVL MLISSLISAK NYESIPENYP PEIRFKKVYR
     LVSLFLYIKG VKVVIVNPEN VPKKAVLVVA NHKSNLDPLI LIKAFGKTEG VPPLTFIAKI
     ELQDTWLFKI MKLIDCVFID RKNLRQMAAS LEQQQQIIRQ GTALCVFPEG TRVLSRQIGE
     FKSGALKVAY NAFVPIVPLT IVGSMGHMES KKRLQKAQVE RDRGYKIQVI FNTPINPINF
     NQIDSQNVAN NVWREISQTY AQYCQD