ID   PLSB_BAUCH              Reviewed;         821 AA.
AC   Q1LU65;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 80.
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}; OrderedLocusNames=BCI_0020;
OS   Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia.
OX   NCBI_TaxID=374463;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA   Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H.,
RA   Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.;
RT   "Metabolic complementarity and genomics of the dual bacterial symbiosis of
RT   sharpshooters.";
RL   PLoS Biol. 4:1079-1092(2006).
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 membrane {ECO:0000255|HAMAP-Rule:MF_00393};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00393};
CC       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; CP000238; ABF13834.1; -; Genomic_DNA.
DR   RefSeq; WP_011520232.1; NC_007984.1.
DR   STRING; 374463.BCI_0020; -.
DR   EnsemblBacteria; ABF13834; ABF13834; BCI_0020.
DR   KEGG; bci:BCI_0020; -.
DR   HOGENOM; CLU_015407_0_0_6; -.
DR   OMA; EVIYVPC; -.
DR   OrthoDB; 580383at2; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000002427; 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 membrane; Lipid biosynthesis; Lipid metabolism;
KW   Membrane; Phospholipid biosynthesis; Phospholipid metabolism;
KW   Reference proteome; Transferase.
FT   CHAIN           1..821
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_1000049428"
FT   MOTIF           310..315
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   821 AA;  95185 MW;  64771BE4E3CE7524 CRC64;
     MFNWRAIYNK ILYLLLKIVV RSHIIPPKLL AEICLDIQEP MMYVLPYNSK CDLLTLRILC
     IQYQLPDPLK PIFIXGVRFP RYLFIDQSCH IRSDVTKQQQ YGRILHNFIT LYRHNSCSNI
     QILPVWVMFG RCPGKESYKN KKTTSIQFFC LLKKIINVIW LGRDSFIYFS PIGSIPISYI
     ANSNYTINSI MILKLFRLGR IHFLRQKRIA IGPSLLVRKH LFEKLLASQT ITKLVEDEAR
     SKKISIKQAQ QKALVIIEEI AADFSYETIR LSDRVLSWIW NMLYQGLYVC NADRVRKLAE
     KGHEIIYLPC HRSHMDYLLL SYILYHEGLV IPYIAAGINL NFWPAGQIFR KLGAFFIHRT
     FKGHQKLYSA IFREYLYQLF NGGYSVAYFL EGSRSRTGRL QAPKTGTLTI TIQSMLHLGK
     KKPIILVPVY ISYEHVIEVA SYTKELYGVV KKKEGLIHMI SGLRNLRNLG RGYINFGEPL
     PLLTWLNQQV PQWQDDINSI EGNRPNWLAL TVDYLAVTIM TRINNAVAVN AMNLCSSIIL
     ASRQYSCSSI VITRTRLLSQ LKCYLELLRN VPYDAEVTVP NVTPEDLFQH LITLNQFTIK
     NNSIIYVSSE KTALITYYRN NIQHLFILPS LLAIIIIAQP GISRKLIHQK LLSLYPLLKV
     ELFMRFSYQE LPHVIDLMIT ELHRQDILYE QQTKIYPVPK RMDELQLLAA SGGRETLYRY
     AITFSLLCSY TRINRYSLEK QSIIIAQHLS KIHSIYALEF IDKTIFSTLI TTLRHEGYLS
     DSGEIHASQA KEIYKFLSAL ISPEIQTSIT NALYHIKTVV N