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Database: UniProt
Entry: A0A1H9YMZ6_9BACI
LinkDB: A0A1H9YMZ6_9BACI
Original site: A0A1H9YMZ6_9BACI 
ID   A0A1H9YMZ6_9BACI        Unreviewed;       279 AA.
AC   A0A1H9YMZ6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase {ECO:0000256|HAMAP-Rule:MF_01147};
DE            EC=2.5.1.145 {ECO:0000256|HAMAP-Rule:MF_01147};
GN   Name=lgt {ECO:0000256|HAMAP-Rule:MF_01147};
GN   ORFNames=SAMN05421676_101230 {ECO:0000313|EMBL:SES70463.1};
OS   Salinibacillus kushneri.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Salinibacillus.
OX   NCBI_TaxID=237682 {ECO:0000313|EMBL:SES70463.1, ECO:0000313|Proteomes:UP000199095};
RN   [1] {ECO:0000313|EMBL:SES70463.1, ECO:0000313|Proteomes:UP000199095}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.3566 {ECO:0000313|EMBL:SES70463.1,
RC   ECO:0000313|Proteomes:UP000199095};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_01147}.
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:0000256|HAMAP-Rule:MF_01147};
CC   -!- PATHWAY: Protein modification; lipoprotein biosynthesis (diacylglyceryl
CC       transfer). {ECO:0000256|HAMAP-Rule:MF_01147}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01147};
CC       Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01147}.
CC   -!- SIMILARITY: Belongs to the Lgt family. {ECO:0000256|ARBA:ARBA00007150,
CC       ECO:0000256|HAMAP-Rule:MF_01147}.
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DR   EMBL; FOHJ01000001; SES70463.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9YMZ6; -.
DR   STRING; 237682.SAMN05421676_101230; -.
DR   OrthoDB; 871140at2; -.
DR   UniPathway; UPA00664; -.
DR   Proteomes; UP000199095; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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   NCBIfam; TIGR00544; lgt; 1.
DR   PANTHER; PTHR30589:SF0; PHOSPHATIDYLGLYCEROL--PROLIPOPROTEIN DIACYLGLYCERYL TRANSFERASE; 1.
DR   PANTHER; PTHR30589; PROLIPOPROTEIN DIACYLGLYCERYL TRANSFERASE; 1.
DR   Pfam; PF01790; LGT; 1.
DR   PROSITE; PS01311; LGT; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01147};
KW   Lipoprotein {ECO:0000313|EMBL:SES70463.1};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01147};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01147, ECO:0000313|EMBL:SES70463.1};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01147};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01147}.
FT   TRANSMEM        20..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT   TRANSMEM        51..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT   TRANSMEM        91..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT   TRANSMEM        119..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT   TRANSMEM        182..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT   TRANSMEM        211..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT   BINDING         138
FT                   /ligand="1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol)"
FT                   /ligand_id="ChEBI:CHEBI:64716"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
SQ   SEQUENCE   279 AA;  31877 MW;  E85A064E44D554DC CRC64;
     MLFNIQPYDR VFIELGPISI YWYGVIIATG AALGLWLATR ESKRLGLKED IFVDLLIFAI
     PAAIICARIY YVTFEWDRYV GEPWWKVFAV WEGGIAIHGA LIGAVLTAFL FAKVKEISFF
     TLADIAAPSL LVGQAIGRWG NFMNQEAHGG PVSEEAYNHF IQYIPDFITN QMIIDGVMYQ
     PTFLYESVWN ILGLLVLLYM RKVNPRRGEI FFSYLIWYSF GRFFIEGLRT DSLYVMGTDI
     RVAQLISVLL IVISILAMVY RRKKGLANVH YNGQLPSEK
//
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