ID   PLSX_CLOPE              Reviewed;         339 AA.
AC   Q8XJN6;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 2.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Putative phosphate acyltransferase;
DE            EC=2.3.1.274 {ECO:0000255|HAMAP-Rule:MF_00019};
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=CPE1720;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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.
CC       {ECO:0000255|HAMAP-Rule:MF_00019}.
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};
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 {ECO:0000255|HAMAP-Rule:MF_00019}.
CC       Note=Associated with the membrane possibly through PlsY.
CC       {ECO:0000255|HAMAP-Rule:MF_00019}.
CC   -!- SIMILARITY: Belongs to the PlsX family. {ECO:0000255|HAMAP-
CC       Rule:MF_00019}.
CC   -!- CAUTION: Could be the product of a pseudogene. Resulting from
CC       truncation by frameshift mutation. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB81426.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; BA000016; BAB81426.1; ALT_FRAME; Genomic_DNA.
DR   AlphaFoldDB; Q8XJN6; -.
DR   SMR; Q8XJN6; -.
DR   STRING; 195102.gene:10490984; -.
DR   EnsemblBacteria; BAB81426; BAB81426; BAB81426.
DR   KEGG; cpe:CPE1720; -.
DR   HOGENOM; CLU_039379_2_0_9; -.
DR   OMA; HGKSNAR; -.
DR   UniPathway; UPA00085; -.
DR   Proteomes; UP000000818; 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   5: Uncertain;
KW   Cytoplasm; Lipid biosynthesis; Lipid metabolism; Phospholipid biosynthesis;
KW   Phospholipid metabolism; Reference proteome; Transferase.
FT   CHAIN           1..339
FT                   /note="Putative phosphate acyltransferase"
FT                   /id="PRO_0000189869"
SQ   SEQUENCE   339 AA;  36956 MW;  7D8EB40260CF8A90 CRC64;
     MRVAVDGMGG DHSPSAVVKG CVQALEEFKD IEIYITGPED ILKEAFSKFK YDKERVTFID
     AKEVISTNEH PAMAVKKKKD SSLVKALRLV KDNQCEAVIS AGSTGAFLTG CTLIVGRIKG
     VERPALAPVM PGKNGPFMII DAGANVDSKP SYLVQFAKMG EVYFKSVMDV NNPKVGLVNI
     GEEEEKGNDL TKATYKLLKE ERDINFIGNV EPREVSTGDV DVLVCDGFVG NTVLKMYEGV
     ASTILSMIKS EVKSSFLAKL GVPFLAPALM NLKKKMDYKE YGGAPFLGVK GICVKAHGSS
     DAKAFKNAIR QARKFHENDL IGKLSEEITK KSFDNQKNI