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Database: UniProt
Entry: A4BXV7_9FLAO
LinkDB: A4BXV7_9FLAO
Original site: A4BXV7_9FLAO 
ID   A4BXV7_9FLAO            Unreviewed;       242 AA.
AC   A4BXV7;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Phospholipid/glycerol acyltransferase domain-containing protein {ECO:0000259|SMART:SM00563};
GN   ORFNames=PI23P_04852 {ECO:0000313|EMBL:EAR13798.1};
OS   Polaribacter irgensii 23-P.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=313594 {ECO:0000313|EMBL:EAR13798.1, ECO:0000313|Proteomes:UP000003053};
RN   [1] {ECO:0000313|EMBL:EAR13798.1, ECO:0000313|Proteomes:UP000003053}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=23-P {ECO:0000313|EMBL:EAR13798.1,
RC   ECO:0000313|Proteomes:UP000003053};
RA   Murray A., Staley J., Ferriera S., Johnson J., Kravitz S., Halpern A.,
RA   Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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:EAR13798.1}.
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DR   EMBL; AAOG01000001; EAR13798.1; -; Genomic_DNA.
DR   RefSeq; WP_004569596.1; NZ_CH724148.1.
DR   AlphaFoldDB; A4BXV7; -.
DR   STRING; 313594.PI23P_04852; -.
DR   eggNOG; COG0204; Bacteria.
DR   HOGENOM; CLU_027938_6_4_10; -.
DR   OrthoDB; 9803035at2; -.
DR   Proteomes; UP000003053; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003053};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          75..194
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   242 AA;  27358 MW;  E8417351D34B2279 CRC64;
     MKILSFLVSP IFMLVFFLVL IVFHPLQWIG LHGFGYKGHK FIVDTMNFLL VKSLLIIGVT
     VTVKNEEELP NGVPLVFVSN HQGLFDIPPI IWAFRKYHPK FVSKTELGRG IPSISYNLRH
     GGAVLIDRND PKQAIGALVN FSKRIQDNTW SAVIFPEGTR SRNGVPKSFA SNGVKIITKY
     NKESYVVPLT INNSWKVFKY GKFPFGMGSP ITITVHTPMK IGSLPFEELF EKTETIIKKH
     IN
//
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