ID   PLSB_ACTSZ              Reviewed;         813 AA.
AC   A6VQ68;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 76.
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=Asuc_1763;
OS   Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / CCUG 43843 /
OS   130Z).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=339671;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z;
RX   PubMed=21118570; DOI=10.1186/1471-2164-11-680;
RA   McKinlay J.B., Laivenieks M., Schindler B.D., McKinlay A.A.,
RA   Siddaramappa S., Challacombe J.F., Lowry S.R., Clum A., Lapidus A.L.,
RA   Burkhart K.B., Harkins V., Vieille C.;
RT   "A genomic perspective on the potential of Actinobacillus succinogenes for
RT   industrial succinate production.";
RL   BMC Genomics 11:680-680(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; CP000746; ABR75115.1; -; Genomic_DNA.
DR   RefSeq; WP_012073492.1; NC_009655.1.
DR   AlphaFoldDB; A6VQ68; -.
DR   SMR; A6VQ68; -.
DR   STRING; 339671.Asuc_1763; -.
DR   EnsemblBacteria; ABR75115; ABR75115; Asuc_1763.
DR   KEGG; asu:Asuc_1763; -.
DR   eggNOG; COG2937; Bacteria.
DR   HOGENOM; CLU_015407_0_0_6; -.
DR   OMA; EVIYVPC; -.
DR   OrthoDB; 580383at2; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000001114; 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; Reference proteome; Transferase.
FT   CHAIN           1..813
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_1000072227"
FT   MOTIF           304..309
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   813 AA;  93109 MW;  77EAD4D86CCBB0C6 CRC64;
     MSAFLNLYRN TLSWPLSFLV KDNPIPNNPV EELTLNIEQP IVYVLPYTSQ TDLVVLRKNC
     LSLGLPDPFL DNRIEGKVLP RYVFLDEGHQ FFKSKGAKKE TEKVFKNYLE LHRTSADLDV
     QVVPVSVLWG RSPGREDKGL PKLRLLNGLQ KTIAAIWFGR DTFVRFSQAM SMRYMVNEYG
     EDEKLAQKLP RIAKMHFAKQ RISATGPRLP NRQAMFNKLL QHPAVLQAIE DEARGKNMTK
     EKARKEAEKI LNEIAADTNY SSLRVADRLL GWLWNKLYQG IEVEHADRVR RLALEGHEIV
     YVPCHRSHID YLLLSYVLYH QGLVPPHIAA GINLNFWPVG RIFRSWGAFF IRRTFKGNRL
     YSTLFREYLG ELFHRGYSVE YFIEGGRSRT GRLLTPKTGM MSMTLQALQQ GQTRPISIVP
     VYVGYEHVLE VDTYAKELRG AAKEKENAGL VLRVIKKLRN LGRGFVNFGE PITLSTYLNR
     HFPEWKNEGR DERPLWFNKA VDAVSRQVMV NINKAAAVNA MNLTGTALLS SRQRALSREQ
     LLEQLESYQQ YLLNVSYSDD IIIPSAPPKE LLDHVLGLDR VGILIEKDNF GELVRLERNH
     AVLMTYYRNN IQHLLVLPSL VASIVLHHEA IQKDLVLTSV EKLYPFLKAE LFMHLPPEAL
     REKVERIIAE LHRQQLIKLN ENILSINRPR VRTLQLWSAG MREILQRYLI TVAILLQDPA
     ISRGKLEKES QSIAQRLSVL HGINSPEFFD KAVFSTFIAS LKDNGYFDTS GNADVTKLQG
     MADILEHVIS TEINLTIKSA VETAVDLDEI ESE