PLSB_ECOSM
ID PLSB_ECOSM Reviewed; 827 AA.
AC B1LPK6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, 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};
GN OrderedLocusNames=EcSMS35_4503;
OS Escherichia coli (strain SMS-3-5 / SECEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=439855;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMS-3-5 / SECEC;
RX PubMed=18708504; DOI=10.1128/jb.00661-08;
RA Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA Ravel J., Stepanauskas R.;
RT "Insights into the environmental resistance gene pool from the genome
RT sequence of the multidrug-resistant environmental isolate Escherichia coli
RT SMS-3-5.";
RL J. Bacteriol. 190:6779-6794(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; CP000970; ACB18864.1; -; Genomic_DNA.
DR AlphaFoldDB; B1LPK6; -.
DR SMR; B1LPK6; -.
DR EnsemblBacteria; ACB18864; ACB18864; EcSMS35_4503.
DR KEGG; ecm:EcSMS35_4503; -.
DR HOGENOM; CLU_015407_0_0_6; -.
DR OMA; EVIYVPC; -.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000007011; 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..827
FT /note="Glycerol-3-phosphate acyltransferase"
FT /id="PRO_1000123082"
FT MOTIF 325..330
FT /note="HXXXXD motif"
SQ SEQUENCE 827 AA; 93724 MW; AFAE24FC9859B824 CRC64;
MTFCYPCRAF ALLTRGFTSF MSGWPRIYYK LLNLPLSILV KSKSIPADPA PELGLDTSRP
IMYVLPYNSK ADLLTLRAQC LAHDLPDPLE PLEIDGTLLP RYVFIHGGPR VFTYYTPKEE
SIKLFHDYLD LHRSNPNLDV QMVPVSVMFG RAPGREKGEV NPPLRMLNGV QKFFAVLWLG
RDSFVRFSPS VSLRRMADEH GTDKTIAQKL ARVARMHFAR QRLAAVGPRL PARQDLFNKL
LASRAIAKAV EDEARSKKIS HEKAQQNAIV LMEEIAANFS YEMIRLTDRI LGFTWNRLYQ
GINVHNAERV RQLAHDGHEL VYVPCHRSHM DYLLLSYVLY HQGLVPPHIA AGINLNFWPA
GPIFRRLGAF FIRRTFKGNK LYSTVFREYL GELFSRGYSV EYFVEGGRSR TGRLLDPKTG
TLSMTIQAML RGGTRPITLI PIYIGYEHVM EVGTYAKELR GATKEKESLP QMLRGLSKLR
NLGQGYVNFG EPMPLMTYLN QHVPDWRESI DPIEAVRPAW LTPTVNNIAA DLMVRINNAG
AANAMNLCCT ALLASRQRSL TREQLTEQLN CYLDLMRNVP YSTDSTVPSA SASELIDHAL
QMNKFEVEKD TIGDIIILPR EQAVLMTYYR NNIAHMLVLP SLMAAIVTQH RHISRDVLME
HVNVLYPMLK AELFLRWDRD ELPDVIDALA NEMQRQGLIT LQDDELHINP AHSRTLQLLA
AGARETLQRY AITFWLLSAN PSINRGTLEK ESRTVAQRLS VLHGINAPEF FDKAVFSSLV
LTLRDEGYIS DSGDAEPAET MKVYQLLAEL ITSDVRLTIE SATQGEG