ID   PLSB_MYCMM              Reviewed;         788 AA.
AC   B2HNJ0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 68.
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=MMAR_3833;
OS   Mycobacterium marinum (strain ATCC BAA-535 / M).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=216594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-535 / M;
RX   PubMed=18403782; DOI=10.1101/gr.075069.107;
RA   Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA   Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA   Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA   Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA   Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA   Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT   "Insights from the complete genome sequence of Mycobacterium marinum on the
RT   evolution of Mycobacterium tuberculosis.";
RL   Genome Res. 18:729-741(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 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; CP000854; ACC42243.1; -; Genomic_DNA.
DR   RefSeq; WP_012395433.1; NC_010612.1.
DR   AlphaFoldDB; B2HNJ0; -.
DR   SMR; B2HNJ0; -.
DR   STRING; 216594.MMAR_3833; -.
DR   EnsemblBacteria; ACC42243; ACC42243; MMAR_3833.
DR   KEGG; mmi:MMAR_3833; -.
DR   eggNOG; COG2937; Bacteria.
DR   HOGENOM; CLU_015407_1_0_11; -.
DR   OMA; EVIYVPC; -.
DR   OrthoDB; 580383at2; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000001190; 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.
PE   3: Inferred from homology;
KW   Acyltransferase; Cell membrane; Lipid biosynthesis; Lipid metabolism;
KW   Membrane; Phospholipid biosynthesis; Phospholipid metabolism;
KW   Reference proteome; Transferase.
FT   CHAIN           1..788
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_1000123085"
FT   REGION          104..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           271..276
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   788 AA;  88236 MW;  4367AF048DA614E3 CRC64;
     MTKPVADTSA VLTSEDTLVL ASMGSPVEMQ LIMDWLGEQR ARTPGAKFDV LKLPPRNAPT
     AALTALVEQL ESGSEAGADR SIVPVQVFWQ PPADRSRLAK VAGLLPGRDP YHPNPRQQRR
     ILRSDPQRAR VMAGESATVS ELRKQWRDNT VGEDQHDFAH FVARRAILAL ARAEYRILGP
     QYKSPRLVKP EMLASARFRA GLEKIPGATV EEAGKMLDEL ATGWSQASVD VFSVLGRLIS
     RGFDPEFDYD EYQVAAMRTA LEAHPAVLLF SHRSYIDGAV VPVAMQDNRL PPVHMFGGVN
     LSFGVMGPLM RRAGMIFIRR NIAGDPLYKY VLKEYVGYVV EKRFNLSWSI EGTRSRTGKM
     LPPKLGLMSY VADAYLDGRS DDILLQGVSI CFDQLHEIAE YAAYARGAEK TPEGFSWLYN
     FIKAQGERNY GKIYVRFPEA VSMRQYLGVP HGPITHDLAA KRLALQKMSF EVAWRILRAT
     PMTATGLVCA LLLTARGTAL TLGQLHHTLQ DSLDYLERKQ TPMSTSALRL RSREGVRAAV
     DALSNAHPVT RVDSGREPVW YIAPEDELAA AFYRNSVIHA FLETSIVELA LAHARHAEGD
     RMAAFWDQVM RLRDLLKFDF YFADSAAFRA NIAEEMAWHR DWESQVAAGG DQIDAILYAK
     RPLISDAMLR VFFEAYAIVA DVLRDAPANI KQKDLTDLAL GLGRQYVAQA RVRSSEPVST
     LLFATARQVV DDQHLIEPAP DLTERRSAFL AELRNILRDF DYVGKIARNR FVARELKARQ
     ERLEQQAQ