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PLSC_NEIMB
ID   PLSC_NEIMB              Reviewed;         255 AA.
AC   Q9JZ47;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase;
DE            Short=1-AGP acyltransferase;
DE            Short=1-AGPAT;
DE            EC=2.3.1.51;
DE   AltName: Full=Lysophosphatidic acid acyltransferase;
DE            Short=LPAAT;
GN   Name=plsC; OrderedLocusNames=NMB1294;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA   Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA   Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA   Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA   Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA   Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA   Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA   Moxon E.R., Rappuoli R., Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(2000).
CC   -!- FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid
CC       by incorporating acyl moiety at the 2 position. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC         sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC         ChEBI:CHEBI:58608; EC=2.3.1.51;
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC       diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}.
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; AE002098; AAF41670.1; -; Genomic_DNA.
DR   PIR; A81099; A81099.
DR   RefSeq; NP_274314.1; NC_003112.2.
DR   RefSeq; WP_002217072.1; NC_003112.2.
DR   AlphaFoldDB; Q9JZ47; -.
DR   SMR; Q9JZ47; -.
DR   STRING; 122586.NMB1294; -.
DR   PaxDb; Q9JZ47; -.
DR   PRIDE; Q9JZ47; -.
DR   EnsemblBacteria; AAF41670; AAF41670; NMB1294.
DR   KEGG; nme:NMB1294; -.
DR   PATRIC; fig|122586.8.peg.1619; -.
DR   HOGENOM; CLU_027938_0_1_4; -.
DR   OMA; PMLWVSN; -.
DR   UniPathway; UPA00557; UER00613.
DR   Proteomes; UP000000425; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IBA:GO_Central.
DR   GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006654; P:phosphatidic acid biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR004552; AGP_acyltrans.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   SMART; SM00563; PlsC; 1.
DR   TIGRFAMs; TIGR00530; AGP_acyltrn; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cell inner membrane; Cell membrane; Lipid biosynthesis;
KW   Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW   Phospholipid metabolism; Reference proteome; Transferase.
FT   CHAIN           1..255
FT                   /note="1-acyl-sn-glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_0000208176"
FT   MOTIF           78..83
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   255 AA;  27943 MW;  F262C2BE7B2F2AD7 CRC64;
     MSSNKASFFT RLRRLCRLAV WLFKTGKNLR GIDGGCPESR NRAVIELGRG VLAALDIGLE
     VGRPAPEHPN GVLVAANHVS WLDIFAMSAV YPSSFIAKQE IKSWPVLGKM GQNAGTVFIN
     RNSRRDIEPI NRAVCETLQR GQNVSFFPEA RTSSGLGLLP FKAALFQSAI DAGAKVLAVA
     LRYYDETGKR TARPSYADVG LPTCLWRIVS MKKLTIRVDF VCVADAAESE DRYALKDKIE
     ESIRAVVADD ADIAV
 
 
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