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Database: UniProt
Entry: A0A087MJZ1_9GAMM
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ID   A0A087MJZ1_9GAMM        Unreviewed;       298 AA.
AC   A0A087MJZ1;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 37.
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=N788_10940 {ECO:0000313|EMBL:KFL37194.1};
OS   Arenimonas donghaensis DSM 18148 = HO3-R19.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Arenimonas.
OX   NCBI_TaxID=1121014 {ECO:0000313|EMBL:KFL37194.1, ECO:0000313|Proteomes:UP000029085};
RN   [1] {ECO:0000313|Proteomes:UP000029085}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HO3-R19 {ECO:0000313|Proteomes:UP000029085};
RA   Chen F., Wang G.;
RT   "Genome sequencing of Arenimonas donghaensis.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KFL37194.1, ECO:0000313|Proteomes:UP000029085}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HO3-R19 {ECO:0000313|EMBL:KFL37194.1,
RC   ECO:0000313|Proteomes:UP000029085};
RX   PubMed=26380644; DOI=10.1186/s40793-015-0055-4;
RA   Chen F., Wang H., Cao Y., Li X., Wang G.;
RT   "High quality draft genomic sequence of Arenimonas donghaensis DSM
RT   18148(T).";
RL   Stand. Genomic Sci. 10:59-59(2015).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KFL37194.1}.
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DR   EMBL; AVCJ01000006; KFL37194.1; -; Genomic_DNA.
DR   RefSeq; WP_034221680.1; NZ_AVCJ01000006.1.
DR   AlphaFoldDB; A0A087MJZ1; -.
DR   STRING; 1121014.N788_10940; -.
DR   PATRIC; fig|1121014.3.peg.943; -.
DR   OrthoDB; 871140at2; -.
DR   UniPathway; UPA00664; -.
DR   Proteomes; UP000029085; 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   Membrane {ECO:0000256|HAMAP-Rule:MF_01147};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029085};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01147};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01147};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01147}.
FT   TRANSMEM        20..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT   TRANSMEM        59..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT   TRANSMEM        93..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT   TRANSMEM        224..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT   TRANSMEM        261..279
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT   BINDING         142
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   298 AA;  33067 MW;  D2F3A228CE61E38D CRC64;
     MTILHTIDPL ALQLPFWPHG IHWYGLMYAL AFFTAWWLGR RRVRAGRLPG VNEDGFGDLL
     FYGMLGVILG GRIGYVLFYA FQDFLADPMM LFMINQGGMS FHGGLLGVLV AAAWWTRHHR
     LHFFDTMDFV APLVPAGLGF GRLGNYIGGE LWGKPTGGDW GVVFPSSLPA EYAALPAEQL
     RALHASGALD AFARHPSQLY QAALEGLVLG LVLWVYSRRP RPRYAVSGLF ALGYGLFRFA
     VEFVREPDAH LGYLAFDWLT MGQLLSLPLV ALGLFLLWLS RRSPVLAPLP PPPLEGKA
//
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