PLSX_STRR6
ID PLSX_STRR6 Reviewed; 330 AA.
AC Q8DRN3;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Phosphate acyltransferase {ECO:0000255|HAMAP-Rule:MF_00019};
DE EC=2.3.1.274 {ECO:0000255|HAMAP-Rule:MF_00019, ECO:0000269|PubMed:16949372};
DE AltName: Full=Acyl-ACP phosphotransacylase {ECO:0000255|HAMAP-Rule:MF_00019};
DE AltName: Full=Acyl-[acyl-carrier-protein]--phosphate acyltransferase {ECO:0000255|HAMAP-Rule:MF_00019};
DE AltName: Full=Phosphate-acyl-ACP acyltransferase {ECO:0000255|HAMAP-Rule:MF_00019};
GN Name=plsX {ECO:0000255|HAMAP-Rule:MF_00019}; OrderedLocusNames=spr0037;
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, CATALYTIC ACTIVITY, SUBUNIT, ACTIVITY REGULATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
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: Catalyzes the reversible formation of acyl-phosphate (acyl-
CC PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme
CC utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA. It is active
CC with both saturated and unsaturated acyl-ACP. {ECO:0000255|HAMAP-
CC Rule:MF_00019, ECO:0000269|PubMed:16949372}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-
CC [ACP]; Xref=Rhea:RHEA:42292, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC COMP:14125, ChEBI:CHEBI:43474, ChEBI:CHEBI:59918, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:138651; EC=2.3.1.274; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00019, ECO:0000269|PubMed:16949372};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-[ACP] + phosphate = hexadecanoyl phosphate +
CC holo-[ACP]; Xref=Rhea:RHEA:54964, Rhea:RHEA-COMP:9652, Rhea:RHEA-
CC COMP:9685, ChEBI:CHEBI:43474, ChEBI:CHEBI:64479, ChEBI:CHEBI:78483,
CC ChEBI:CHEBI:138436; Evidence={ECO:0000269|PubMed:16949372};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54965;
CC Evidence={ECO:0000269|PubMed:16949372};
CC -!- ACTIVITY REGULATION: Magnesium ions lead to a slight increase in the
CC catalytic activity. {ECO:0000269|PubMed:16949372}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=140 uM for orthophosphate {ECO:0000269|PubMed:16949372};
CC KM=300 uM for acyl-ACP {ECO:0000269|PubMed:16949372};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism. {ECO:0000255|HAMAP-
CC Rule:MF_00019}.
CC -!- SUBUNIT: Homodimer. Probably interacts with PlsY. {ECO:0000255|HAMAP-
CC Rule:MF_00019}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Associated with the membrane
CC possibly through PlsY. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the PlsX family. {ECO:0000255|HAMAP-
CC Rule:MF_00019}.
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DR EMBL; AE007317; AAK98841.1; -; Genomic_DNA.
DR PIR; E97876; E97876.
DR RefSeq; NP_357631.1; NC_003098.1.
DR RefSeq; WP_000717456.1; NC_003098.1.
DR AlphaFoldDB; Q8DRN3; -.
DR SMR; Q8DRN3; -.
DR STRING; 171101.spr0037; -.
DR SwissLipids; SLP:000001797; -.
DR EnsemblBacteria; AAK98841; AAK98841; spr0037.
DR GeneID; 60232828; -.
DR GeneID; 66805243; -.
DR KEGG; spr:spr0037; -.
DR PATRIC; fig|171101.6.peg.43; -.
DR eggNOG; COG0416; Bacteria.
DR HOGENOM; CLU_039379_1_1_9; -.
DR OMA; HGKSNAR; -.
DR BioCyc; MetaCyc:MON-14086; -.
DR BRENDA; 2.3.1.274; 1960.
DR SABIO-RK; Q8DRN3; -.
DR UniPathway; UPA00085; -.
DR Proteomes; UP000000586; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043811; F:phosphate:acyl-[acyl carrier protein] acyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR HAMAP; MF_00019; PlsX; 1.
DR InterPro; IPR003664; FA_synthesis.
DR InterPro; IPR012281; Phospholipid_synth_PlsX-like.
DR PANTHER; PTHR30100; PTHR30100; 1.
DR Pfam; PF02504; FA_synthesis; 1.
DR PIRSF; PIRSF002465; Phsphlp_syn_PlsX; 1.
DR TIGRFAMs; TIGR00182; plsX; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Lipid biosynthesis; Lipid metabolism; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase.
FT CHAIN 1..330
FT /note="Phosphate acyltransferase"
FT /id="PRO_0000189947"
SQ SEQUENCE 330 AA; 34918 MW; 453C34A40D28957F CRC64;
MKKIAVDAMG GDYAPQAIVE GVNQALSDFS DIEVQLYGDE AKIKQYLTAT ERVSIIHTDE
KIDSDDEPTR AIRNKKNASM VLAAKAVKDG EADAVLSAGN TGALLAAGFF IVGRIKNIDR
PGLMSTLPTV DGKGFDMLDL GANAENTAQH LHQYAVLGSF YAKNVRGIAQ PRVGLLNNGT
ESSKGDPLRK ETYELLAADE SLNFIGNVEA RDLMNGVADV VVADGFTGNA VLKSIEGTAM
GIMGLLKTAI TGGGLRAKLG ALLLKDSLRG LKKQLNYSDV GGAVLFGVKA PVVKTHGSSD
AKAVYSTIRQ IRTMLETDVV AQTAREFSGE
