ID   PLSB_XYLF2              Reviewed;         863 AA.
AC   B2I7N1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Glycerol-3-phosphate acyltransferase {ECO:0000255|HAMAP-Rule:MF_00393};
DE            Short=GPAT {ECO:0000255|HAMAP-Rule:MF_00393};
DE            EC=2.3.1.15 {ECO:0000255|HAMAP-Rule:MF_00393};
GN   Name=plsB {ECO:0000255|HAMAP-Rule:MF_00393};
GN   OrderedLocusNames=XfasM23_0310;
OS   Xylella fastidiosa (strain M23).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=405441;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M23;
RX   PubMed=20601474; DOI=10.1128/jb.00651-10;
RA   Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.;
RT   "Whole genome sequences of two Xylella fastidiosa strains (M12 and M23)
RT   causing almond leaf scorch disease in California.";
RL   J. Bacteriol. 192:4534-4534(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-
CC         phosphate + CoA; Xref=Rhea:RHEA:15325, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57597, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342; EC=2.3.1.15;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00393};
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC       diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC       {ECO:0000255|HAMAP-Rule:MF_00393}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00393}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00393}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_00393}.
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:0000255|HAMAP-Rule:MF_00393}.
CC   -!- SIMILARITY: Belongs to the GPAT/DAPAT family. {ECO:0000255|HAMAP-
CC       Rule:MF_00393}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001011; ACB91759.1; -; Genomic_DNA.
DR   RefSeq; WP_004089351.1; NC_010577.1.
DR   AlphaFoldDB; B2I7N1; -.
DR   EnsemblBacteria; ACB91759; ACB91759; XfasM23_0310.
DR   GeneID; 58015870; -.
DR   KEGG; xfn:XfasM23_0310; -.
DR   HOGENOM; CLU_015407_0_0_6; -.
DR   OMA; EVIYVPC; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000001698; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0102420; F:sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd07993; LPLAT_DHAPAT-like; 1.
DR   HAMAP; MF_00393; Glyc3P_acyltrans; 1.
DR   InterPro; IPR022284; GPAT/DHAPAT.
DR   InterPro; IPR041728; GPAT/DHAPAT_LPLAT.
DR   InterPro; IPR045520; GPAT_C.
DR   InterPro; IPR028354; GPAT_PlsB.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   PANTHER; PTHR12563; PTHR12563; 1.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   Pfam; PF19277; GPAT_C; 1.
DR   PIRSF; PIRSF500064; GPAT; 1.
DR   PIRSF; PIRSF000437; GPAT_DHAPAT; 1.
DR   SMART; SM00563; PlsC; 1.
DR   TIGRFAMs; TIGR03703; plsB; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cell inner membrane; Cell membrane; Lipid biosynthesis;
KW   Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW   Phospholipid metabolism; Transferase.
FT   CHAIN           1..863
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_1000123101"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           343..348
FT                   /note="HXXXXD motif"
FT   COMPBIAS        8..29
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   863 AA;  97619 MW;  D700BB120F14ECC6 CRC64;
     MPKKNSPLLP KETTTTQSSV DTSGSSNLTW PVSEHTIRRP LWARLLGQIL DPWLDLSIEP
     EHSVQYNDGR PIIYVLEDYG LCNTLILDKA CRKTKLPSPL IPLSGNPLQR KRAYLALSRR
     SSSNSLIPNQ RGGKTHSDSL ANLLQAHRIR DTLDVHLVPV SIFIGRTPDR QSGWFAVLFS
     ENWALVGRFR RILAILLNGR NTIVCFAPPI SVRQTLNEGL PPERTLRKLQ RVLRTHFRRI
     RETVIGPDLS TRRLLVDNVL ATEAVREAIG AQAKRDGTDL SETWRKAQAY AWEIAADYSS
     PVIRSADFLF SHVWNRIYAG VLVHHVDSFK EISPGHEIVY VPSHRSHMDY LLLSYCLYKC
     SIGLPHIVAG INLNLPVVGT LLRKCGAFFI RRSIKGNMLY SVVLSEYVAQ LVAGGYSLEY
     FIEGGRSRTG RLLQPKGGMI MMTVQAFLRQ PRRPVLFQPI YIGYEKLMEG TSYLDELSGE
     PKKKESIWRV FWNIPKVLKQ KYGQVVVNFG EPIALNDVLA ELAPEWEGQA LNENEKPAWL
     SSTVNHLARQ IQTRINSAAD VNPINLLALA LLSTPKHAMG EADLIAQITL CKKILLELPY
     SNRVTITPHT PERIIAHAEQ INILTRVHHP LGDVLRVDGD NAVLLSYFRN NVLHLFTASA
     WVACCFKNNR RMSRIALIRL GVGMYPFLQA ELFLPWTEDQ FAQHIQQVIE LFVREGLLLS
     AGNEEEDPLT RNTSQTDEVF RLRAISHSLQ QAFERYYITI SILVKNGPGT LSASELESLC
     QLAAQRLSLL YASTAPEFFD KGLFRGFIQK LRELNLVWPD TYSKLLFDER LDTSAKDAQV
     ILGRELRHTI ERISPEATKP APK