ID   A0A0A1HX93_9PSED        Unreviewed;       302 AA.
AC   A0A0A1HX93;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=FIG018329: 1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000313|EMBL:CDF94667.1};
GN   ORFNames=BN844_3687 {ECO:0000313|EMBL:CDF94667.1};
OS   Pseudomonas sp. SHC52.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=984195 {ECO:0000313|EMBL:CDF94667.1, ECO:0000313|Proteomes:UP000031550};
RN   [1] {ECO:0000313|EMBL:CDF94667.1, ECO:0000313|Proteomes:UP000031550}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SHC52 {ECO:0000313|EMBL:CDF94667.1,
RC   ECO:0000313|Proteomes:UP000031550};
RA   Van der Voort M., Mendes R., Raaijmakers J.M.;
RT   "Genome mining of the rhizosphere bacterium Pseudomonas sp. SH-C52.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
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:CDF94667.1}.
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DR   EMBL; CBLV010000204; CDF94667.1; -; Genomic_DNA.
DR   RefSeq; WP_041022404.1; NZ_CBLV010000204.1.
DR   AlphaFoldDB; A0A0A1HX93; -.
DR   OrthoDB; 319710at2; -.
DR   Proteomes; UP000031550; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   CDD; cd07990; LPLAT_LCLAT1-like; 1.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   PANTHER; PTHR10983; 1-ACYLGLYCEROL-3-PHOSPHATE ACYLTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR10983:SF16; LYSOCARDIOLIPIN ACYLTRANSFERASE 1; 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:CDF94667.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transferase {ECO:0000313|EMBL:CDF94667.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        123..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          89..231
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   302 AA;  35003 MW;  EBBBCF3F3851FBFC CRC64;
     MLDFLPAPVR GVIASLLLAL NTIACCTPLF IVAIFKLLLP FPAAQRFTDW LMSHIHEAWI
     SNNKAWMNLL RRTRWHLSGL EGLDYQHSYL ITSNHQSWVD IMVLQYVLNR RVRPLKFFLK
     QELIWVPVIG LAWWALGFPF MKRYSKAYLE KHPEKKGKDL ETTRKTCAKF RNNPVGIFNF
     AEGTRFTEGK HAQQQSPFRY LLKPKAGGIA FVLDAMGEQL ESIINVTIHY PGGRPGYWDL
     LCGNVGEVVV HFQELPIPPQ FIGKNYDQDG AYRLEFQGWI NQLWQDKDAL LEQMHREYPG
     KS
//