PLSC_STRR6
ID PLSC_STRR6 Reviewed; 264 AA.
AC Q8DNY1;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase;
DE Short=1-AGP acyltransferase;
DE Short=1-AGPAT;
DE Short=1-acyl-G3P acyltransferase;
DE EC=2.3.1.n4 {ECO:0000269|PubMed:16949372};
DE AltName: Full=Lysophosphatidic acid acyltransferase;
DE Short=LPAAT;
DE AltName: Full=Phosphatidic acid synthase;
DE Short=PA synthase;
GN Name=plsC; OrderedLocusNames=spr1465;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16949372; DOI=10.1016/j.molcel.2006.06.030;
RA Lu Y.-J., Zhang Y.-M., Grimes K.D., Qi J., Lee R.E., Rock C.O.;
RT "Acyl-phosphates initiate membrane phospholipid synthesis in Gram-positive
RT pathogens.";
RL Mol. Cell 23:765-772(2006).
CC -!- FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid
CC (PA) by incorporating an acyl moiety at the 2 position. This enzyme
CC utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
CC {ECO:0000269|PubMed:16949372}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + a fatty acyl-[ACP] = a 1,2-
CC diacyl-sn-glycero-3-phosphate + holo-[ACP]; Xref=Rhea:RHEA:42296,
CC Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:14125, ChEBI:CHEBI:57970,
CC ChEBI:CHEBI:58608, ChEBI:CHEBI:64479, ChEBI:CHEBI:138651;
CC EC=2.3.1.n4; Evidence={ECO:0000269|PubMed:16949372};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphate + hexadecanoyl-[ACP] =
CC 1,2-dihexadecanoyl-sn-glycero-3-phosphate + holo-[ACP];
CC Xref=Rhea:RHEA:54972, Rhea:RHEA-COMP:9652, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:57518, ChEBI:CHEBI:64479, ChEBI:CHEBI:72859,
CC ChEBI:CHEBI:78483; Evidence={ECO:0000269|PubMed:16949372};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54973;
CC Evidence={ECO:0000269|PubMed:16949372};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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:0000250}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000305}.
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DR EMBL; AE007317; AAL00269.1; -; Genomic_DNA.
DR PIR; H98054; H98054.
DR RefSeq; NP_359058.1; NC_003098.1.
DR AlphaFoldDB; Q8DNY1; -.
DR SMR; Q8DNY1; -.
DR STRING; 171101.spr1465; -.
DR SwissLipids; SLP:000001800; -.
DR EnsemblBacteria; AAL00269; AAL00269; spr1465.
DR KEGG; spr:spr1465; -.
DR PATRIC; fig|171101.6.peg.1584; -.
DR eggNOG; COG0204; Bacteria.
DR HOGENOM; CLU_027938_4_3_9; -.
DR OMA; GASPMEF; -.
DR BioCyc; MetaCyc:MON-14088; -.
DR UniPathway; UPA00085; -.
DR Proteomes; UP000000586; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IBA:GO_Central.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..264
FT /note="1-acyl-sn-glycerol-3-phosphate acyltransferase"
FT /id="PRO_0000389441"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 57..62
FT /note="HXXXXD motif"
SQ SEQUENCE 264 AA; 30768 MW; B6BC663F196D4AEC CRC64;
MIRYNNNKKT IEGDRMFYTY LRGLVVLLLW SINGNAHYHN TDKIPNQDEN YILVAPHRTW
WDPVYMAFAT KPKQFIFMAK KELFTNRIFG WWIRMCGAFP IDRENPSASA IKYPINVLKK
SDRSLIMFPS GSRHSNDVKG GAALIAKMAK VRIMPVTYTG PMTLKGLISR ERVDMNFGNP
IDISDIKKMN DEGIETVANR IQTEFQRLDE ETKQWHNDKK PNPLWWFIRI PALILAIILA
ILTIIFSFIA SFIWNPDKKR EELA
