ID   PLSB_ACTPJ              Reviewed;         824 AA.
AC   B0BQ47;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-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}; OrderedLocusNames=APJL_1126;
OS   Actinobacillus pleuropneumoniae serotype 3 (strain JL03).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=434271;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JL03;
RX   PubMed=18197260; DOI=10.1371/journal.pone.0001450;
RA   Xu Z., Zhou Y., Li L., Zhou R., Xiao S., Wan Y., Zhang S., Wang K., Li W.,
RA   Li L., Jin H., Kang M., Dalai B., Li T., Liu L., Cheng Y., Zhang L., Xu T.,
RA   Zheng H., Pu S., Wang B., Gu W., Zhang X.L., Zhu G.-F., Wang S.,
RA   Zhao G.-P., Chen H.;
RT   "Genome biology of Actinobacillus pleuropneumoniae JL03, an isolate of
RT   serotype 3 prevalent in China.";
RL   PLoS ONE 3:E1450-E1450(2008).
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; CP000687; ABY69682.1; -; Genomic_DNA.
DR   RefSeq; WP_005601572.1; NC_010278.1.
DR   AlphaFoldDB; B0BQ47; -.
DR   EnsemblBacteria; ABY69682; ABY69682; APJL_1126.
DR   KEGG; apj:APJL_1126; -.
DR   HOGENOM; CLU_015407_0_0_6; -.
DR   OMA; EVIYVPC; -.
DR   OrthoDB; 580383at2; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000008547; 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..824
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_1000123072"
FT   MOTIF           302..307
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   824 AA;  94242 MW;  E86CE9730054F4D6 CRC64;
     MSSLLNFYRK VLNVPLSLLV KSRAIPTDPV KELNLNLEQP IIYVLPYTSQ TDLLILQKNC
     LSLNLPDPLQ NNELNGQSLP RYVFLDEGRR FFKSKGAKSE TESIFYRYLD LHRNNESLDV
     QLIPASVLWG RSPGKESEPH LRLMSSFQRI ISMIWFGRDN FVRFSQALSL KYMVAEHGAD
     EGIAQKLARV AKIHFAKQRY SAMGPRLPDR QAMFNKIIQS PAIKAAIEEE AKTKKISIEK
     ARQEAEKIVN EIAADVSHES LRIADRVLSW LWNKLYQGIN VQNGDRVRKL ALEGHEIVYV
     PCHRSHMDYL LLSYLLYHQG LVPPHIAAGI NLNFFPAGPI FRSWGAFFIR RTFKGNRLYS
     TIFREYLAEL FYRGYSVEYF IEGGRSRTGR LLEPKTGMMS MTLQALQRGL TRPISIVPVY
     IGYEHVLEVD TYAKELRGAE KEKENAGLVL RVIKKLKNLG QCYVNFAEPI QVNNYLNQHF
     PEWKESQAED SRPKWLNEAV DSVAHQVMIN INKAAAINAK NLIGSVLLAS RQRALAREQL
     IEQVDSYLQL FKNVSYSDDV IVPNDSAEEM LNHVLTLPRS GVISEKDSFG EMIRLDRESA
     VLMTYYRNNI QHLFVLPSLV ASIILHHESV SKDLIIKTVN RIYPFLKAEL FLHFEENDVR
     NQVEAILTEF SAQRIVKYES DVLQINRARV RALQLHAAGV REILQRYYIS LSILLEHPEI
     SRAALEKESR SIAQRLSILH GINAPEFFDK ALFSTFSASL KAQGYFDSEG NCILEKAKEA
     EEILRSLISV EVQLTIQGAM EKVEEVENTE TVVKTAEAVT EKNE