PLSB_YERPS
ID PLSB_YERPS Reviewed; 834 AA.
AC Q66FG9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 89.
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=YPTB0368;
OS Yersinia pseudotuberculosis serotype I (strain IP32953).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=273123;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP32953;
RX PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA Derbise A., Hauser L.J., Garcia E.;
RT "Insights into the evolution of Yersinia pestis through whole-genome
RT comparison with Yersinia pseudotuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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; BX936398; CAH19608.1; -; Genomic_DNA.
DR RefSeq; WP_011191593.1; NZ_CP009712.1.
DR AlphaFoldDB; Q66FG9; -.
DR SMR; Q66FG9; -.
DR EnsemblBacteria; CAH19608; CAH19608; YPTB0368.
DR GeneID; 66843217; -.
DR KEGG; ypo:BZ17_2202; -.
DR KEGG; yps:YPTB0368; -.
DR PATRIC; fig|273123.14.peg.2331; -.
DR OMA; EVIYVPC; -.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000001011; 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..834
FT /note="Glycerol-3-phosphate acyltransferase"
FT /id="PRO_1000049474"
FT REGION 800..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 304..309
FT /note="HXXXXD motif"
FT COMPBIAS 801..815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 834 AA; 94603 MW; B71C212BDF3E9B05 CRC64;
MSGWRKIYYK LLNLPLKLLV KSKVIPADPV SELGLDPSRP ILYVLPYNSK ADLLTLRAQC
LAQDLPDPLI PLEIDGVQLP SHVFIENGPR VFRYYVPKQE SVKLFHDYLD LHRNNPALDI
QMLPVSVMFG RSPGREGHGT PHLRVLNGVQ KFFAVLWLGR DSFVRFSTTV SLRRMASEHG
TDKTIAHKLA RVARMHFSRQ RLAAVGPSLP ARQDLFKKLL ASKAIEKAVA DEARSKKISH
EKAQQNAITL MEEIAANFSY EAVRLSDRVL SWTWNRLYQG INVHNAERVR QLAQDGHEIV
YVPCHRSHMD YLLLSYVLYH QGLVPPHIAA GINLNFWPAG PIFRRLGAFF IRRTFKGNKL
YSTVFREYLG ELFTRGYSVE YFVEGGRSRT GRLLEPKTGT LSMTIQAMLR GGTRPITLVP
IYIGYEHVME VGTYAKELRG AIKEKENLLQ MLRGLRKLRN LGQGYVNFGE PLPLTTYLNT
HVPQWRDAID PIEAQRPSWL TPAVNDLANQ IMVRINNAAA ANAMNLCSTA LLASRQRSLT
REQLLEQLDC YLQLMRNAPY AKDTTVPDKT PEELLNHALN MNKFEVEKDT IGDIIILPRE
QAVLMTYYRN NIQHLLILPS LIASMVMYHR RITRTELLHK ISMIYPMLKA ELFLHYSKEQ
LPETLDTLID ELARQQLICD KGSELVLNPA RIRPLQLLAA GVRETLQRYA ITLSLLSATP
SINRGALEKE SRIMAQRLSV LHGINAPEFF DKAVFSTLVA TLREEGYISD SGDAIQEHTL
EVYNMLSALM TPEVKLTIES VSMPAETSNQ PEAPETPETP ETPETPEPEG KTES
