PLSB_SALTY
ID PLSB_SALTY Reviewed; 806 AA.
AC Q8ZKH9;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=STM4235;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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; AE006468; AAL23059.1; -; Genomic_DNA.
DR RefSeq; NP_463100.1; NC_003197.2.
DR RefSeq; WP_000017360.1; NC_003197.2.
DR AlphaFoldDB; Q8ZKH9; -.
DR SMR; Q8ZKH9; -.
DR STRING; 99287.STM4235; -.
DR PaxDb; Q8ZKH9; -.
DR EnsemblBacteria; AAL23059; AAL23059; STM4235.
DR GeneID; 1255761; -.
DR KEGG; stm:STM4235; -.
DR PATRIC; fig|99287.12.peg.4455; -.
DR HOGENOM; CLU_015407_0_0_6; -.
DR OMA; EVIYVPC; -.
DR PhylomeDB; Q8ZKH9; -.
DR BioCyc; SENT99287:STM4235-MON; -.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IBA:GO_Central.
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 GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IBA:GO_Central.
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..806
FT /note="Glycerol-3-phosphate acyltransferase"
FT /id="PRO_0000195232"
FT MOTIF 306..311
FT /note="HXXXXD motif"
SQ SEQUENCE 806 AA; 91227 MW; 9D6FE34757B8F9ED CRC64;
MSGWPRIYYK LLNLPLSILV KSKSIPAEPA QELGLDTSRP IMYVLPYNSK ADLLTLRAQC
LAHDLPDPLE PLEIDGALLP RYVFIHGGPR VFTYYTPKEE SVKLFHDYLD LHRSNPALDV
QMVPVSVMFG RAPGREKGED NPPLRMLNGV QKFFAISWLG RDSFVRFSPS VSLRRMADEH
GTDKIIAQKL ARVARMHFAR QRLAAVGPRL PARQDLFNKL LASKAIARAV EDEARSKKIS
HEKAQQNAIA LMEEIAANFS YEMIRLTDRI LGFTWNRLYQ GINVHNAERV RQLAHDGHEI
VYVPCHRSHM DYLLLSYVLY HQGLVPPHIA AGINLNFWPA GPIFRRLGAF FIRRTFKGNK
LYSTVFREYL GELFSRGYSV EYFVEGGRSR TGRLLDPKTG TLSMTIQAML RGGTRPITLV
PIYIGYEHVM EVGTYAKELR GATKEKESLP QMLKGLSKLR NLGQGYVNFG EPMPLMTYLN
QHVPEWRESI DPIEAIRPAW LTPTVNSIAA DLMVRINNAG AANAMNLCCT ALLASRQRSL
TREQLTEQLD CYLDLMRNVP YSTDSTVPAA SAGELIAHAL QMNKFEVEKD TIGDIIILPR
EQAVLMTYYR NNIAHMLIMP SLMAAIITQH RRISRDALQQ HVEALYPMLK AELFLRWERE
ELASVIDALA SEMQRQGLIT LQDDELHINP THSRTLQLLA AGARETLQRY AITFWLLSAN
PSINRSTLEK ESRTVAQRLS VLHGINAPEF FDKAVFSSLV LTLRDEGYIS DTGDAEPAET
MKIYQMLADL ITSDVRLTIE SATQGE
