ID   PLSX_HERAR              Reviewed;         357 AA.
AC   A4G6T3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Phosphate acyltransferase {ECO:0000255|HAMAP-Rule:MF_00019};
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=HEAR2078;
OS   Herminiimonas arsenicoxydans.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herminiimonas.
OX   NCBI_TaxID=204773;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ULPAs1;
RX   PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA   Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA   Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA   Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M., Leize E.,
RA   Lieutaud A., Lievremont D., Makita Y., Mangenot S., Nitschke W., Ortet P.,
RA   Perdrial N., Schoepp B., Siguier P., Simeonova D.D., Rouy Z., Segurens B.,
RA   Turlin E., Vallenet D., van Dorsselaer A., Weiss S., Weissenbach J.,
RA   Lett M.-C., Danchin A., Bertin P.N.;
RT   "A tale of two oxidation states: bacterial colonization of arsenic-rich
RT   environments.";
RL   PLoS Genet. 3:518-530(2007).
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}.
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DR   EMBL; CU207211; CAL62220.1; -; Genomic_DNA.
DR   RefSeq; WP_011871496.1; NC_009138.1.
DR   AlphaFoldDB; A4G6T3; -.
DR   SMR; A4G6T3; -.
DR   STRING; 204773.HEAR2078; -.
DR   EnsemblBacteria; CAL62220; CAL62220; HEAR2078.
DR   KEGG; har:HEAR2078; -.
DR   eggNOG; COG0416; Bacteria.
DR   HOGENOM; CLU_039379_1_0_4; -.
DR   OMA; HGKSNAR; -.
DR   OrthoDB; 631784at2; -.
DR   UniPathway; UPA00085; -.
DR   Proteomes; UP000006697; 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   3: Inferred from homology;
KW   Cytoplasm; Lipid biosynthesis; Lipid metabolism; Phospholipid biosynthesis;
KW   Phospholipid metabolism; Reference proteome; Transferase.
FT   CHAIN           1..357
FT                   /note="Phosphate acyltransferase"
FT                   /id="PRO_1000001770"
SQ   SEQUENCE   357 AA;  38211 MW;  969FF5A3E8E8A870 CRC64;
     MTIKISIDCM GGDHGPAVTI PAAISFVESE PDAELILVGL ADQLWAELKK HKAGEHPRLS
     VVNATEVVTM DDTLEAALRR KKNSSMRVAI NLVKQGQADA CVSAGNTGAL MAISRYVLKT
     LPGVDRPAIC SILPNQKDGP TYMLDLGANV DCEPQHLHQF ALMGSALVSA MEGKPRPTVG
     LLNVGEEDIK GNDIVKQTAV LLRADHERGT LNFYGNVEGN DIFKGTTDIV VCDGFVGNVT
     LKASEGLGRF VKSVLTTEFK RNPLTMLGAL IARSALKAIS QRLNPSRYNG GSLLGLRGLV
     FKSHGGADAY GYQWAIKRAF DAAKYDVLAR ISTKIADLMP QSALTPLPED SVTATEQ