ID   PLSC_BACSU              Reviewed;         199 AA.
AC   O07584; Q796X1;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase;
DE            Short=1-AGP acyltransferase;
DE            Short=1-AGPAT;
DE            Short=1-acyl-G3P acyltransferase;
DE            EC=2.3.1.n4;
DE   AltName: Full=Lysophosphatidic acid acyltransferase;
DE            Short=LPAAT;
DE   AltName: Full=Phosphatidic acid synthase;
DE            Short=PA synthase;
GN   Name=plsC; Synonyms=yhdO; OrderedLocusNames=BSU09540;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9579061; DOI=10.1099/00221287-144-4-859;
RA   Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H.,
RA   Venema G., Bron S.;
RT   "The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus
RT   subtilis chromosome contains several dysfunctional genes, the glyB marker,
RT   many genes encoding transporter proteins, and the ubiquitous hit gene.";
RL   Microbiology 144:859-875(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   SUBCELLULAR LOCATION.
RX   PubMed=15743965; DOI=10.1128/jb.187.6.2163-2174.2005;
RA   Nishibori A., Kusaka J., Hara H., Umeda M., Matsumoto K.;
RT   "Phosphatidylethanolamine domains and localization of phospholipid
RT   synthases in Bacillus subtilis membranes.";
RL   J. Bacteriol. 187:2163-2174(2005).
RN   [4]
RP   FUNCTION IN THE BIOSYNTHESIS OF PHOSPHOLIPID AND AS A ACYLTRANSFERASE,
RP   DISRUPTION PHENOTYPE, AND SUBSTRATE SPECIFICITY.
RX   PubMed=17557823; DOI=10.1128/jb.00602-07;
RA   Paoletti L., Lu Y.-J., Schujman G.E., de Mendoza D., Rock C.O.;
RT   "Coupling of fatty acid and phospholipid synthesis in Bacillus subtilis.";
RL   J. Bacteriol. 189:5816-5824(2007).
CC   -!- FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid
CC       (PA) by incorporating an acyl moiety at the 2 position. This enzyme
CC       utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
CC       {ECO:0000269|PubMed:17557823}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acyl-sn-glycero-3-phosphate + a fatty acyl-[ACP] = a 1,2-
CC         diacyl-sn-glycero-3-phosphate + holo-[ACP]; Xref=Rhea:RHEA:42296,
CC         Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:14125, ChEBI:CHEBI:57970,
CC         ChEBI:CHEBI:58608, ChEBI:CHEBI:64479, ChEBI:CHEBI:138651;
CC         EC=2.3.1.n4;
CC   -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}. Note=Localized in
CC       the septal membrane. {ECO:0000269|PubMed:15743965}.
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   -!- DISRUPTION PHENOTYPE: Cells lacking this gene cease to produce
CC       phospholipid and accumulate fatty acids arising from the
CC       dephosphorylation of 1-acylglycerol-3-P. {ECO:0000269|PubMed:17557823}.
CC   -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC       acyltransferase family. {ECO:0000305}.
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DR   EMBL; Y14082; CAA74499.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12793.1; -; Genomic_DNA.
DR   PIR; E69826; E69826.
DR   RefSeq; NP_388835.1; NC_000964.3.
DR   RefSeq; WP_003233335.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; O07584; -.
DR   SMR; O07584; -.
DR   STRING; 224308.BSU09540; -.
DR   PaxDb; O07584; -.
DR   PRIDE; O07584; -.
DR   EnsemblBacteria; CAB12793; CAB12793; BSU_09540.
DR   GeneID; 936269; -.
DR   KEGG; bsu:BSU09540; -.
DR   PATRIC; fig|224308.179.peg.1027; -.
DR   eggNOG; COG0204; Bacteria.
DR   InParanoid; O07584; -.
DR   OMA; GASPMEF; -.
DR   PhylomeDB; O07584; -.
DR   BioCyc; BSUB:BSU09540-MON; -.
DR   UniPathway; UPA00085; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006654; P:phosphatidic acid biosynthetic process; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Acyltransferase; Cell membrane; Lipid biosynthesis; Lipid metabolism;
KW   Membrane; Phospholipid biosynthesis; Phospholipid metabolism;
KW   Reference proteome; Transferase.
FT   CHAIN           1..199
FT                   /note="1-acyl-sn-glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_0000389440"
FT   MOTIF           39..44
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   199 AA;  21923 MW;  913FBA09BA2714CD CRC64;
     MYKFCANALK VILSLRGGVK VYNKENLPAD SGFVIACTHS GWVDVITLGV GILPYQIHYM
     AKKELFQNKW IGSFLKKIHA FPVDRENPGP SSIKTPIKLL KEGEIVGIFP SGTRTSEDVP
     LKRGAVTIAQ MGKAPLVPAA YQGPSSGKEL FKKGKMKLII GEPLHQADFA HLPSKERLAA
     MTEALNQRIK ELENKLDQL