ID   PLSB_PSEF5              Reviewed;         834 AA.
AC   Q4KHJ1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 90.
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=PFL_1161;
OS   Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=220664;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5;
RX   PubMed=15980861; DOI=10.1038/nbt1110;
RA   Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA   Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA   Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA   Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA   Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S. III,
RA   Thomashow L.S., Loper J.E.;
RT   "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT   Pf-5.";
RL   Nat. Biotechnol. 23:873-878(2005).
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; CP000076; AAY90448.1; -; Genomic_DNA.
DR   RefSeq; WP_011059509.1; NC_004129.6.
DR   AlphaFoldDB; Q4KHJ1; -.
DR   SMR; Q4KHJ1; -.
DR   STRING; 220664.PFL_1161; -.
DR   EnsemblBacteria; AAY90448; AAY90448; PFL_1161.
DR   GeneID; 57474165; -.
DR   KEGG; pfl:PFL_1161; -.
DR   PATRIC; fig|220664.5.peg.1193; -.
DR   eggNOG; COG2937; Bacteria.
DR   HOGENOM; CLU_015407_0_0_6; -.
DR   OMA; EVIYVPC; -.
DR   OrthoDB; 580383at2; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000008540; 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; Reference proteome; Transferase.
FT   CHAIN           1..834
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_1000049445"
FT   MOTIF           309..314
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   834 AA;  94862 MW;  81526C3E25F5A784 CRC64;
     MTRSPIRRLV FGTLRRLLYL WVRSETINQS SFTLDLDRSR PVFYVLQNPS LTDLAVVDTE
     CTKAGLPRPV LPVSVGNLLE PAAFFYLTPE PDWLGRQDKR GAPPTLTRLV SALTQNAAED
     AQIIPVSVFW GQSPDSESSP WKLLFADSWA VTGRLRRLLS IMILGRKTRV QFSAPINLRE
     LIEHNKGHER TVRMAQRILR VHFRNLKAAV IGPDISHRRN LVKGLLNQPL VKQAILDEAE
     REKISPEKAK AQALRYGNEI ASDYTYTAIR FLEVVLSWFW NKIYDGIKVN HLEGVQKIAQ
     GHEVIYVPCH RSHIDYLLLS YLLFRNGLTP PHIAAGINLN MPVIGGLLRR GGAFFMRRTF
     KGNPLYTSVF NEYLHTLFTK GFPVEYFVEG GRSRTGRMLQ PKTGMLAITL RSFLRSSRMP
     IVFVPVYIGY ERVLEGRTYL GELRGASKKK ESIFDIFKVI GALKQRFGQV AVNFGEPIKL
     AEFLDQEQPD WRTQELGPQY RPAWLNETTN RLGERVAQHL NEAAAINPVN LVALALLSTT
     RLALDDRAMA RVLDLYLALL RRVPYSPHTT LPEGDGRALI QHVKDMDLLA EQSDALGKIL
     YLDEQNAVLM TYYRNNVLHI FALPALLASF FQSSSRMSRE QILRYTRALY PYLQSELFIR
     WPLDELDAVV DQWLEAFVEQ GLLRFEKDLY QRPAPSSRHF VLLTLLSKSI AQTLQRFYMA
     ISLLLNSGQN SISAEELEDL CTVMAQRLSI LHGLNAPEFF DKSLFRHFIQ TLLDQGVLRR
     DEAGKLSYHE ALGELAEGAA KRVLPAEIRL SIRQVALHRS EDAADQLAAP AQND