ID   A0A2R3JLF0_9LACO        Unreviewed;       204 AA.
AC   A0A2R3JLF0;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   13-NOV-2019, entry version 7.
DE   RecName: Full=Glycerol-3-phosphate acyltransferase {ECO:0000256|HAMAP-Rule:MF_01043};
DE   AltName: Full=Acyl-PO4 G3P acyltransferase {ECO:0000256|HAMAP-Rule:MF_01043};
DE   AltName: Full=Acyl-phosphate--glycerol-3-phosphate acyltransferase {ECO:0000256|HAMAP-Rule:MF_01043};
DE   AltName: Full=G3P acyltransferase {ECO:0000256|HAMAP-Rule:MF_01043};
DE            Short=GPAT {ECO:0000256|HAMAP-Rule:MF_01043};
DE            EC=2.3.1.275 {ECO:0000256|HAMAP-Rule:MF_01043};
DE   AltName: Full=Lysophosphatidic acid synthase {ECO:0000256|HAMAP-Rule:MF_01043};
DE            Short=LPA synthase {ECO:0000256|HAMAP-Rule:MF_01043};
GN   Name=plsY {ECO:0000256|HAMAP-Rule:MF_01043};
GN   ORFNames=C5Z25_00835 {ECO:0000313|EMBL:AVK60409.1};
OS   Lactobacillus sp. CBA3605.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus; unclassified Lactobacillus.
OX   NCBI_TaxID=2099788 {ECO:0000313|EMBL:AVK60409.1, ECO:0000313|Proteomes:UP000239036};
RN   [1] {ECO:0000313|EMBL:AVK60409.1, ECO:0000313|Proteomes:UP000239036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBA3605 {ECO:0000313|EMBL:AVK60409.1,
RC   ECO:0000313|Proteomes:UP000239036};
RA   Jung M.Y.;
RT   "Complete genome sequence of Lactobacillus sp. CBA3605.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the transfer of an acyl group from acyl-
CC       phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form
CC       lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate
CC       as fatty acyl donor, but not acyl-CoA or acyl-ACP.
CC       {ECO:0000256|HAMAP-Rule:MF_01043}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-
CC         sn-glycero-3-phosphate + phosphate; Xref=Rhea:RHEA:34075,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57597, ChEBI:CHEBI:57970,
CC         ChEBI:CHEBI:59918; EC=2.3.1.275; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01043};
CC   -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC       {ECO:0000256|HAMAP-Rule:MF_01043, ECO:0000256|SAAS:SAAS00702448}.
CC   -!- SUBUNIT: Probably interacts with PlsX. {ECO:0000256|HAMAP-
CC       Rule:MF_01043, ECO:0000256|SAAS:SAAS00702495}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01043}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01043}.
CC   -!- SIMILARITY: Belongs to the PlsY family. {ECO:0000256|HAMAP-
CC       Rule:MF_01043, ECO:0000256|SAAS:SAAS00702497}.
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DR   EMBL; CP027190; AVK60409.1; -; Genomic_DNA.
DR   UniPathway; UPA00085; -.
DR   Proteomes; UP000239036; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043772; F:acyl-phosphate glycerol-3-phosphate acyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01043; PlsY; 1.
DR   InterPro; IPR003811; G3P_acylTferase_PlsY.
DR   PANTHER; PTHR30309; PTHR30309; 1.
DR   Pfam; PF02660; G3P_acyltransf; 1.
DR   SMART; SM01207; G3P_acyltransf; 1.
DR   TIGRFAMs; TIGR00023; TIGR00023; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000313|EMBL:AVK60409.1};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01043,
KW   ECO:0000256|SAAS:SAAS00702469};
KW   Complete proteome {ECO:0000313|Proteomes:UP000239036};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01043,
KW   ECO:0000256|SAAS:SAAS00702478};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01043,
KW   ECO:0000256|SAAS:SAAS00702441};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01043,
KW   ECO:0000256|SAAS:SAAS00702479};
KW   Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01043,
KW   ECO:0000256|SAAS:SAAS00702501};
KW   Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_01043,
KW   ECO:0000256|SAAS:SAAS00702488};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01043,
KW   ECO:0000256|SAAS:SAAS00702475, ECO:0000313|EMBL:AVK60409.1};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01043,
KW   ECO:0000256|SAAS:SAAS00702474};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01043,
KW   ECO:0000256|SAAS:SAAS00702429}.
FT   TRANSMEM      6     27       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01043}.
FT   TRANSMEM     47     68       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01043}.
FT   TRANSMEM     80     99       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01043}.
FT   TRANSMEM    111    133       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01043}.
FT   TRANSMEM    153    174       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01043}.
SQ   SEQUENCE   204 AA;  22241 MW;  1C96B2E9E62B53F4 CRC64;
     MEIILMLIVA YFLGAIPSGV IIGKLFFHTD IRQAGSGNIG TTNTYRVLGP TAGTIVMAMD
     ILKGTLAAAQ PALFHLPVNA LLIGLGAIVG HTFSVFIGFK GGKAVATSAG ILLAYNWHFF
     LIASAIMFTL VYLTSMVSVA SMTSLTLVSL IAIFYYQDWI LSVIAVILTI FIFYRHRANI
     KRILAGTESL VHFGLGWRHY QRKQ
//