ID PLSB_ESCF3 Reviewed; 806 AA.
AC B7LL13;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
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=EFER_4132;
OS Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS 14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585054;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 / JCM
RC 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928158; CAQ91554.1; -; Genomic_DNA.
DR RefSeq; WP_000017352.1; NC_011740.1.
DR AlphaFoldDB; B7LL13; -.
DR SMR; B7LL13; -.
DR GeneID; 75059282; -.
DR KEGG; efe:EFER_4132; -.
DR HOGENOM; CLU_015407_0_0_6; -.
DR OrthoDB; 335193at2; -.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000000745; 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; IPR045520; GPAT/DHAPAT_C.
DR InterPro; IPR041728; GPAT/DHAPAT_LPLAT.
DR InterPro; IPR028354; GPAT_PlsB.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR NCBIfam; TIGR03703; plsB; 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 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; Transferase.
FT CHAIN 1..806
FT /note="Glycerol-3-phosphate acyltransferase"
FT /id="PRO_1000123083"
FT MOTIF 305..310
FT /note="HXXXXD motif"
SQ SEQUENCE 806 AA; 91239 MW; 52FE9199DC5BE54C CRC64;
MSGWPRIYYK LLNLPLSILV KSKSIPADPA PELGLDTSRP IMYVLPYNSK ADLLTLRAQC
LAHDLPDPLD PLEIDGTLLP RYVFIHGGPR VFTYYTPKEE SIKLFHDYLD LHRSNPNLDV
QMVPVSVMFG RSPGREKGEV NPPLRMLNGV QKFFAVLWLG RDSFVRFSPS VSLRHMADEH
GTDKTIAQKL ARVARMHFAR QRLAAVGPRL PARQDLFNKL LASRAIAKAV EDEARSKKIS
HEKAQQNAVA LMEEIAANFS YEMIRLTDRI LGFTWNRLYQ GINVHNAERV RQLAHDGHEI
VYVPCHRSHM DYLLLSYVLY HQGLVPPHIA AGINLNFWPA GPIFRRLGAF FIRRTFKGNK
LYSTVFREYL GELFSRGYSV EYFVEGGRSR TGRLLDPKTG TLSMTIQAML RGGTRPITLV
PIYIGYEHVM EVGTYAKELR GATKEKENMA QMLRGLSKLR NLGQGYVNFG EPIPLMTYLN
QHVPEWRESI DPIEAVRPAW LTPTVNNIAA DLMVRINNAG AANAMNLCCT ALLASRQRSL
TREQLTEQLD CYLDLLRNVP YSPDATVPSA SASELIDHAL QMNKFEVEKD TIGDIIILPR
EQAVLMTYYR NNIAHMLVLP SLMAAIVTQH RHISREALLH HVEVLYPMLK AELFLRWDRD
ELPDVIDALA REMARQGLIT LQNDELQINP SHSRTLQLLA AGARETLQRY AITFWLLSAN
PAINRSSLEK ESRTVAQRLS VLHGINAPEF FDKAVFSSLV LTLRDEGYIS DSGDAEPAET
LKVYQMLAEL ITSDVRLTIE SATQGE
//
