LGT_SALTY
ID LGT_SALTY Reviewed; 291 AA.
AC P60959; Q07293;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase {ECO:0000255|HAMAP-Rule:MF_01147};
DE EC=2.5.1.145 {ECO:0000255|HAMAP-Rule:MF_01147, ECO:0000269|PubMed:8051048};
GN Name=lgt {ECO:0000255|HAMAP-Rule:MF_01147, ECO:0000303|PubMed:8344935};
GN OrderedLocusNames=STM3002 {ECO:0000312|EMBL:AAL21878.1};
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=8344935; DOI=10.1016/s0021-9258(19)85453-4;
RA Gan K., Gupta S.D., Sankaran K., Schmid M.B., Wu H.C.;
RT "Isolation and characterization of a temperature-sensitive mutant of
RT Salmonella typhimurium defective in prolipoprotein modification.";
RL J. Biol. Chem. 268:16544-16550(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=8051048; DOI=10.1016/s0021-9258(17)32077-x;
RA Sankaran K., Wu H.C.;
RT "Lipid modification of bacterial prolipoprotein. Transfer of diacylglyceryl
RT moiety from phosphatidylglycerol.";
RL J. Biol. Chem. 269:19701-19706(1994).
RN [4]
RP VARIANT SE5221.
RX PubMed=7592473; DOI=10.1128/jb.177.23.6820-6824.1995;
RA Qi H.Y., Sankaran K., Gan K., Wu H.C.;
RT "Structure-function relationship of bacterial prolipoprotein diacylglyceryl
RT transferase: functionally significant conserved regions.";
RL J. Bacteriol. 177:6820-6824(1995).
CC -!- FUNCTION: Catalyzes the transfer of the diacylglyceryl group from
CC phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine
CC of a prolipoprotein, the first step in the formation of mature
CC lipoproteins. {ECO:0000255|HAMAP-Rule:MF_01147,
CC ECO:0000269|PubMed:8051048}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-
CC cysteinyl-[prolipoprotein] = H(+) + S-1,2-diacyl-sn-glyceryl-L-
CC cysteinyl-[prolipoprotein] + sn-glycerol 1-phosphate;
CC Xref=Rhea:RHEA:56712, Rhea:RHEA-COMP:14679, Rhea:RHEA-COMP:14680,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:57685,
CC ChEBI:CHEBI:64716, ChEBI:CHEBI:140658; EC=2.5.1.145;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01147,
CC ECO:0000269|PubMed:8051048};
CC -!- PATHWAY: Protein modification; lipoprotein biosynthesis (diacylglyceryl
CC transfer). {ECO:0000255|HAMAP-Rule:MF_01147,
CC ECO:0000269|PubMed:8051048}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01147}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01147}.
CC -!- DISRUPTION PHENOTYPE: Mutants accumulate unmodified prolipoprotein due
CC to a defect in the activity of prolipoprotein glyceryl transferase.
CC {ECO:0000269|PubMed:8344935}.
CC -!- SIMILARITY: Belongs to the Lgt family. {ECO:0000255|HAMAP-
CC Rule:MF_01147, ECO:0000305}.
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DR EMBL; L13259; AAA20896.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21878.1; -; Genomic_DNA.
DR PIR; A47354; A47354.
DR RefSeq; NP_461919.1; NC_003197.2.
DR RefSeq; WP_000204645.1; NC_003197.2.
DR AlphaFoldDB; P60959; -.
DR SMR; P60959; -.
DR STRING; 99287.STM3002; -.
DR PaxDb; P60959; -.
DR EnsemblBacteria; AAL21878; AAL21878; STM3002.
DR GeneID; 1254525; -.
DR KEGG; stm:STM3002; -.
DR PATRIC; fig|99287.12.peg.3177; -.
DR HOGENOM; CLU_013386_1_0_6; -.
DR OMA; TDVPWAI; -.
DR PhylomeDB; P60959; -.
DR BioCyc; SENT99287:STM3002-MON; -.
DR UniPathway; UPA00664; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0008961; F:phosphatidylglycerol-prolipoprotein diacylglyceryl transferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042158; P:lipoprotein biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01147; Lgt; 1.
DR InterPro; IPR001640; Lgt.
DR PANTHER; PTHR30589; PTHR30589; 1.
DR Pfam; PF01790; LGT; 1.
DR TIGRFAMs; TIGR00544; lgt; 1.
DR PROSITE; PS01311; LGT; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..291
FT /note="Phosphatidylglycerol--prolipoprotein diacylglyceryl
FT transferase"
FT /id="PRO_0000172668"
FT TOPO_DOM 1..20
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P60955"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TOPO_DOM 42..59
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P60955"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TOPO_DOM 81..95
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P60955"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TOPO_DOM 117..129
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P60955"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TOPO_DOM 151..197
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P60955"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TOPO_DOM 219..224
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P60955"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TOPO_DOM 246..259
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P60955"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TOPO_DOM 281..291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P60955"
FT BINDING 143
FT /ligand="1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol)"
FT /ligand_id="ChEBI:CHEBI:64716"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT VARIANT 249
FT /note="D -> N (in SE5221, temperature-sensitive)"
SQ SEQUENCE 291 AA; 33075 MW; A3A38C4FE0123841 CRC64;
MTSSYLHFPD FDPVIFSIGP VALHWYGLMY LVGFVFAMWL AVRRANRPGS GWTKNEVENL
LYAGFLGVFL GGRIGYVLFY NFPLFLDNPL YLFRVWDGGM SFHGGLIGVI LVMIIFARRT
KRSFFQVSDF IAPLIPFGLG AGRLGNFING ELWGRVDPDF RFAMLFPGSR AEDIALLPSH
PQWQPIFDTY GVLPRHPSQL YELALEGVVL FIILNLFIRK PRPMGAVSGL FLIGYGAFRI
IVEFFRQPDA QFTGAWVQYI SMGQILSIPM IIAGAIMMVW AYRRRPQQHV S
