ID PLSX_STRZJ Reviewed; 330 AA.
AC C1CHD4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 01-MAY-2013, entry version 34.
DE RecName: Full=Phosphate acyltransferase;
DE EC=2.3.1.n2;
DE AltName: Full=Acyl-ACP phosphotransacylase;
DE AltName: Full=Acyl-[acyl-carrier-protein]--phosphate acyltransferase;
DE AltName: Full=Phosphate-acyl-ACP acyltransferase;
GN Name=plsX; OrderedLocusNames=SPJ_0061;
OS Streptococcus pneumoniae (strain JJA).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=488222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JJA;
RA Hotopp J.D., Censini S., Masignani V., Covacci A., Tettelin H.;
RT "Complete genome sequence of Streptococcus pneumoniae strain JJA.";
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible formation of acyl-phosphate
CC (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This
CC enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: Acyl-[acyl-carrier-protein] + phosphate =
CC acyl-phosphate + [acyl-carrier-protein].
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC -!- SUBUNIT: Homodimer. Probably interacts with PlsY (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Note=Associated
CC with the membrane possibly through PlsY (By similarity).
CC -!- SIMILARITY: Belongs to the PlsX family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; CP000919; ACO19529.1; -; Genomic_DNA.
DR RefSeq; YP_002735177.1; NC_012466.1.
DR ProteinModelPortal; C1CHD4; -.
DR SMR; C1CHD4; 3-322.
DR STRING; 488222.SPJ_0061; -.
DR EnsemblBacteria; ACO19529; ACO19529; SPJ_0061.
DR GeneID; 7680376; -.
DR KEGG; sjj:SPJ_0061; -.
DR PATRIC; 19695150; VBIStrPne71544_0055.
DR eggNOG; COG0416; -.
DR HOGENOM; HOG000154731; -.
DR KO; K03621; -.
DR OMA; DEKPSQA; -.
DR ProtClustDB; PRK05331; -.
DR UniPathway; UPA00085; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0016747; F:transferase activity, transferring acyl groups other than amino-acyl groups; IEA:EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:HAMAP.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.718.10; -; 1.
DR HAMAP; MF_00019; PlsX; 1; -.
DR InterPro; IPR003664; FA_synthesis.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR InterPro; IPR012281; Phospholipid_synth_PlsX-like.
DR Pfam; PF02504; FA_synthesis; 1.
DR PIRSF; PIRSF002465; Phsphlp_syn_PlsX; 1.
DR TIGRFAMs; TIGR00182; plsX; 1.
PE 3: Inferred from homology;
KW Complete proteome; Cytoplasm; Lipid biosynthesis; Lipid metabolism;
KW Phospholipid biosynthesis; Phospholipid metabolism; Transferase.
FT CHAIN 1 330 Phosphate acyltransferase.
FT /FTId=PRO_1000193149.
SQ SEQUENCE 330 AA; 34849 MW; 448D84A40D29947F 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 ALLLKDSLSG LKKQLNYSDV GGAVLFGVKA PVVKTHGSSD
AKAVYSTIRQ IRTMLETDVV AQTAREFSGE
//