PLSB_MYCBT
ID PLSB_MYCBT Reviewed; 789 AA.
AC C1AEU7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 60.
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=JTY_2494;
OS Mycobacterium bovis (strain BCG / Tokyo 172 / ATCC 35737 / TMC 1019).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=561275;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCG / Tokyo 172 / ATCC 35737 / TMC 1019;
RX PubMed=19200449; DOI=10.1016/j.vaccine.2009.01.034;
RA Seki M., Honda I., Fujita I., Yano I., Yamamoto S., Koyama A.;
RT "Whole genome sequence analysis of Mycobacterium bovis bacillus Calmette-
RT Guerin (BCG) Tokyo 172: a comparative study of BCG vaccine substrains.";
RL Vaccine 27:1710-1716(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 membrane {ECO:0000255|HAMAP-Rule:MF_00393};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00393};
CC 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; AP010918; BAH26776.1; -; Genomic_DNA.
DR RefSeq; WP_003901413.1; NZ_CP014566.1.
DR AlphaFoldDB; C1AEU7; -.
DR SMR; C1AEU7; -.
DR KEGG; mbt:JTY_2494; -.
DR HOGENOM; CLU_015407_1_0_11; -.
DR OMA; EVIYVPC; -.
DR UniPathway; UPA00557; UER00612.
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.
PE 3: Inferred from homology;
KW Acyltransferase; Cell membrane; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Phospholipid biosynthesis; Phospholipid metabolism; Transferase.
FT CHAIN 1..789
FT /note="Glycerol-3-phosphate acyltransferase"
FT /id="PRO_1000192406"
FT MOTIF 275..280
FT /note="HXXXXD motif"
SQ SEQUENCE 789 AA; 88368 MW; B78D7D9A9796EA22 CRC64;
MTKPAADASA VLTAEDTLVL ASTATPVEME LIMGWLGQQR ARHPDSKFDI LKLPPRNAPP
AALTALVEQL EPGFASSPQS GEDRSIVPVR VIWLPPADRS RAGKVAALLP GRDPYHPSQR
QQRRILRTDP RRARVVAGES AKVSELRQQW RDTTVAEHKR DFAQFVSRRA LLALARAEYR
ILGPQYKSPR LVKPEMLASA RFRAGLDRIP GATVEDAGKM LDELSTGWSQ VSVDLVSVLG
RLASRGFDPE FDYDEYQVAA MRAALEAHPA VLLFSHRSYI DGVVVPVAMQ DNRLPPVHMF
GGINLSFGLM GPLMRRSGMI FIRRNIGNDP LYKYVLKEYV GYVVEKRFNL SWSIEGTRSR
TGKMLPPKLG LMSYVADAYL DGRSDDILLQ GVSICFDQLH EITEYAAYAR GAEKTPEGLR
WLYNFIKAQG ERNFGKIYVR FPEAVSMRQY LGAPHGELTQ DPAAKRLALQ KMSFEVAWRI
LQATPVTATG LVSALLLTTR GTALTLDQLH HTLQDSLDYL ERKQSPVSTS ALRLRSREGV
RAAADALSNG HPVTRVDSGR EPVWYIAPDD EHAAAFYRNS VIHAFLETSI VELALAHAKH
AEGDRVAAFW AQAMRLRDLL KFDFYFADST AFRANIAQEM AWHQDWEDHL GVGGNEIDAM
LYAKRPLMSD AMLRVFFEAY EIVADVLRDA PPDIGPEELT ELALGLGRQF VAQGRVRSSE
PVSTLLFATA RQVAVDQELI APAADLAERR VAFRRELRNI LRDFDYVEQI ARNQFVAREF
KARQGRDRI