ID   PLSC_BORBU              Reviewed;         250 AA.
AC   Q59188;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   25-MAY-2022, entry version 106.
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; OrderedLocusNames=BB_0037;
OS   Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS   (Borrelia burgdorferi).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=224326;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX   PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA   Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA   Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA   van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA   Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA   Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA   Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL   Nature 390:580-586(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 116-250.
RC   STRAIN=212;
RX   PubMed=7812434; DOI=10.1099/13500872-140-11-2931;
RA   Ojaimi C., Davidson B.E., Saint-Girons I., Old I.G.;
RT   "Conservation of gene arrangement and an unusual organization of rRNA genes
RT   in the linear chromosomes of the Lyme disease spirochaetes Borrelia
RT   burgdorferi, B. garinii and B. afzelii.";
RL   Microbiology 140:2931-2940(1994).
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}.
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DR   EMBL; AE000783; AAC66417.1; -; Genomic_DNA.
DR   EMBL; L32861; AAC41407.1; -; Genomic_DNA.
DR   PIR; E70104; E70104.
DR   RefSeq; NP_212171.1; NC_001318.1.
DR   RefSeq; WP_002665505.1; NC_001318.1.
DR   AlphaFoldDB; Q59188; -.
DR   SMR; Q59188; -.
DR   STRING; 224326.BB_0037; -.
DR   EnsemblBacteria; AAC66417; AAC66417; BB_0037.
DR   KEGG; bbu:BB_0037; -.
DR   PATRIC; fig|224326.49.peg.436; -.
DR   HOGENOM; CLU_027938_6_1_12; -.
DR   OMA; RLMGITM; -.
DR   UniPathway; UPA00557; UER00613.
DR   Proteomes; UP000001807; 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..250
FT                   /note="1-acyl-sn-glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_0000208167"
FT   MOTIF           88..93
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   250 AA;  28581 MW;  A730BED7058AD999 CRC64;
     MIIVFMKILR SIITYFNVLL FFLILIFFLF PFYLVCKIFL IERYVVRLSF IMMRACIKIS
     LWLAGIKIIV TGSENIPKKS NVIIMGNHIA AMDPLIFIYT FACPFVILAK HSLLRIPFVN
     IVLIVMGVIF VNRRSIRSAA AAEVKAIKVM REGRSIGIFP EGTRNRGGDT RVFKKGSIKM
     ALKTGTSILP VTLYNTNNFF IKNIIFNSGL SVYIHVHPLI DVLKLSEYEK ENLTSIIRDQ
     IVKKLETIKI