ID   PLSB_SHEPW              Reviewed;         807 AA.
AC   B8CUW9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   02-SEP-2026, entry version 82.
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=swp_4820;
OS   Shewanella piezotolerans (strain WP3 / JCM 13877).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Alteromonadales; Shewanellaceae; Shewanella.
OX   NCBI_TaxID=225849;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WP3 / JCM 13877;
RX   PubMed=18398463; DOI=10.1371/journal.pone.0001937;
RA   Wang F., Wang J., Jian H., Zhang B., Li S., Wang F., Zeng X., Gao L.,
RA   Bartlett D.H., Yu J., Hu S., Xiao X.;
RT   "Environmental adaptation: genomic analysis of the piezotolerant and
RT   psychrotolerant deep-sea iron reducing bacterium Shewanella piezotolerans
RT   WP3.";
RL   PLoS ONE 3:E1937-E1937(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=sn-glycerol 3-phosphate + an acyl-CoA = 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; CP000472; ACJ31445.1; -; Genomic_DNA.
DR   RefSeq; WP_020914775.1; NC_011566.1.
DR   AlphaFoldDB; B8CUW9; -.
DR   SMR; B8CUW9; -.
DR   STRING; 225849.swp_4820; -.
DR   KEGG; swp:swp_4820; -.
DR   eggNOG; COG2937; Bacteria.
DR   HOGENOM; CLU_015407_0_0_6; -.
DR   OrthoDB; 335193at2; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000000753; 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:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:TreeGrafter.
DR   CDD; cd07993; LPLAT_DHAPAT-like; 1.
DR   HAMAP; MF_00393; Glyc3P_acyltrans; 1.
DR   InterPro; IPR022284; GPAT/DHAPAT.
DR   InterPro; IPR045520; GPAT/DHAPAT_C.
DR   InterPro; IPR041728; GPAT/DHAPAT_LPLAT.
DR   InterPro; IPR028354; GPAT_PlsB.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   InterPro; IPR060304; PlsB_N.
DR   NCBIfam; TIGR03703; plsB; 1.
DR   NCBIfam; NF003441; PRK04974.1; 1.
DR   PANTHER; PTHR12563:SF17; DIHYDROXYACETONE PHOSPHATE ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR12563; GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   Pfam; PF19277; GPAT_C; 1.
DR   Pfam; PF27464; PlsB_N; 1.
DR   PIRSF; PIRSF500064; GPAT; 1.
DR   PIRSF; PIRSF000437; GPAT_DHAPAT; 1.
DR   SMART; SM00563; PlsC; 1.
DR   SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 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..807
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_1000123097"
FT   MOTIF           308..313
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   807 AA;  91556 MW;  361887D638795347 CRC64;
     MSKKDSLWFK SLRWIQKKLV HTIVVPHDPF DDLNLDPSKP LVYVMKTESV SDIAALSEMT
     GTLGLPSPYD DLEVNGVSAP RVVCLEGSKP LFGERESAEQ YLHCFKRLLS VHKQNAELDI
     QLVPVSLYWG RTPGKEDDTM RAAVLERQNP TWLRKCLMIL FLGRHNFVQF SNAVSLRYMA
     DEHGTDKRIA QKLARVARVH FQRQRKVMTG PQLPKRQALF HALLKSDSIT KAIKEEAASK
     KISETEARAK AMEYLDEVAA DYSDSLVRIA ERFLTWLWNK LYKGINIKGA EQIRQLHHDG
     HEIVYVPCHR SHMDYLLISY ILYYQGMVPP HIAAGINLNF WPAGPMFRRG GAFFIRRSFR
     GNKLYTAVFR EYLDQLFTKG YSVEYFTEGG RSRTGRLLAP KTGMIAMTLN SVLRGVERPV
     TLVPVYLGYD HVMEVATYHK ELSGKKKKKE SVWQVFGAIR KLGNFGQGYV NFGKPITLHN
     FLNDEVPNWR EDIAQDPEQK PTWLTPAVNT LASQVMTNIN DAAAVSSVTL TSLVLLASEQ
     NALERSQLEK QLDLYLTLLK ELPYTEYTSV PEGSGKDLVS QGLELKKVQI ESDALGDIIS
     IDDSIAITMT YYRNNIIHLL VVPSLIAACL LRKERCTRDD VVCVVNDFYP LLQAELFMGI
     EDPKVYADSI LDIFVAQGLV IENGHFEVAD DKVNQLLLLS GTIDETMQRY AILFNLLAVK
     PNMERSELER DSHRLAQRLG ALHGITAPEF YDKKLYATLS VKLKELGHLT DSEGCSDIKR
     IKDRANLLLR SSVRQTIVDS VNAEQKD
//