ID   PLSB_XYLFM              Reviewed;         863 AA.
AC   B0U229;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 71.
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=Xfasm12_0345;
OS   Xylella fastidiosa (strain M12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=405440;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M12;
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}.
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DR   EMBL; CP000941; ACA11363.1; -; Genomic_DNA.
DR   RefSeq; WP_004085224.1; NC_010513.1.
DR   AlphaFoldDB; B0U229; -.
DR   KEGG; xfm:Xfasm12_0345; -.
DR   HOGENOM; CLU_015407_0_0_6; -.
DR   OMA; EVIYVPC; -.
DR   OrthoDB; 580383at2; -.
DR   UniPathway; UPA00557; UER00612.
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_1000123102"
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;  97699 MW;  E849406B1A976D9B CRC64;
     MPKKNSPLLP KETTTTQSSV DTSGSSNLTW PVSEHSIRRP LWARLLGQML DPWLDLSIEP
     EHSVQYNDGR PIIYVLEDYG LCNTLILDKA CRKTKLPSPL IPLPDNPLQR KRAYLALSRR
     SSSNSLIPNQ RGGKTHSDSL ANLLQAHRIR DTLDVHLVPV SIFIGRTPDR QSGWFAVLFS
     ENWALVGRFR RLLAVLLNGR NTIVCFAPPI SVRQTLNEGL PPERTLRKLQ RVLRTHFRRI
     RETVIGPDLS TRRLLVDNVL ATEAVREAIA AQAKRDGTDL SETWRKAQAY AWEIAADYSS
     PVIRSADFLF SHVWNRIYAG VLIHHVDSFK ETAPGHEVVY VPSHRSHIDY MLLSYCLYQC
     GIVLPHIVAG INLNLPIVGT LLRKCGAFFI RRSIKGNMLY SIVLSEYVAQ LVAGGYSLEY
     FIEGGRSRTG RLLQPKGGMI MMTLQAFLRQ PRRPVLFQPI YIGYEKLIEG TSYLDELSGE
     PKKKESIWRL FWNIPKVLKQ KYGQVVVNFG EPIALNDVLA ELAPEWEGQA LNENEKPAWL
     SSTVNHLARQ IQTRINSAAD VNPINLLALA LLSTPKHAMG EADLIAQITL CKKILLELPY
     SNRVTVTPHT 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