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Database: UniProt
Entry: A0A0U1QLF3_9BACL
LinkDB: A0A0U1QLF3_9BACL
Original site: A0A0U1QLF3_9BACL 
ID   A0A0U1QLF3_9BACL        Unreviewed;       198 AA.
AC   A0A0U1QLF3;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Acyl-phosphate glycerol 3-phosphate acyltransferase {ECO:0000313|EMBL:KLI01648.1};
GN   ORFNames=SINU_12215 {ECO:0000313|EMBL:KLI01648.1};
OS   Sporolactobacillus inulinus CASD.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Sporolactobacillaceae;
OC   Sporolactobacillus.
OX   NCBI_TaxID=1069536 {ECO:0000313|EMBL:KLI01648.1, ECO:0000313|Proteomes:UP000035553};
RN   [1] {ECO:0000313|EMBL:KLI01648.1, ECO:0000313|Proteomes:UP000035553}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CASD {ECO:0000313|EMBL:KLI01648.1,
RC   ECO:0000313|Proteomes:UP000035553};
RX   PubMed=21952540; DOI=10.1128/JB.05934-11;
RA   Yu B., Su F., Wang L., Xu K., Zhao B., Xu P.;
RT   "Draft genome sequence of Sporolactobacillus inulinus strain CASD, an
RT   efficient D-lactic acid-producing bacterium with high-concentration lactate
RT   tolerance capability.";
RL   J. Bacteriol. 193:5864-5865(2011).
CC   -!- FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid
CC       by incorporating acyl moiety at the 2 position.
CC       {ECO:0000256|ARBA:ARBA00037183}.
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         Evidence={ECO:0000256|ARBA:ARBA00001141};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KLI01648.1}.
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DR   EMBL; AFVQ02000180; KLI01648.1; -; Genomic_DNA.
DR   RefSeq; WP_010024481.1; NZ_AFVQ02000180.1.
DR   AlphaFoldDB; A0A0U1QLF3; -.
DR   STRING; 1069536.SINU_12215; -.
DR   OrthoDB; 9803035at2; -.
DR   Proteomes; UP000035553; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   CDD; cd07989; LPLAT_AGPAT-like; 1.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   PANTHER; PTHR10434; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR10434:SF60; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE LPAT1, CHLOROPLASTIC; 1.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   SMART; SM00563; PlsC; 1.
DR   SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000313|EMBL:KLI01648.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035553};
KW   Transferase {ECO:0000313|EMBL:KLI01648.1}.
FT   DOMAIN          35..148
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   198 AA;  22038 MW;  6B78B129814B1DC8 CRC64;
     MNLYSIGKPL VALYLRFGFK IQVIGRENVP DQGGALICCN HLSNFDPPLV GTVLSRPLSF
     VAKEELFKIP LFGAVLRRLN AFPIRRGTGD RGAIRLAMKL LREGHALLIF PEGHRNLKHT
     KMQHAYSGAG FFALKTNAVV VPCAIIGRYK FRGKMKIVFG NPLNMEELKD RKLKSSEVTA
     IIMKHIEQLI ATHTSSTA
//
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