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Database: UniProt
Entry: A0A286H4M3_9ACTN
LinkDB: A0A286H4M3_9ACTN
Original site: A0A286H4M3_9ACTN 
ID   A0A286H4M3_9ACTN        Unreviewed;       315 AA.
AC   A0A286H4M3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=SAMN06272739_3677 {ECO:0000313|EMBL:SOE02701.1};
OS   Blastococcus haudaquaticus.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Blastococcus.
OX   NCBI_TaxID=1938745 {ECO:0000313|EMBL:SOE02701.1, ECO:0000313|Proteomes:UP000219482};
RN   [1] {ECO:0000313|Proteomes:UP000219482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44270 {ECO:0000313|Proteomes:UP000219482};
RA   Varghese N., Submissions S.;
RL   Submitted (SEP-2017) 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; OCNK01000005; SOE02701.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A286H4M3; -.
DR   UniPathway; UPA00664; -.
DR   Proteomes; UP000219482; 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:SOE02701.1};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01147};
KW   Reference proteome {ECO:0000313|Proteomes:UP000219482};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01147, ECO:0000313|EMBL:SOE02701.1};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01147};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01147}.
FT   TRANSMEM        25..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT   TRANSMEM        55..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT   TRANSMEM        95..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT   TRANSMEM        126..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT   TRANSMEM        193..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT   TRANSMEM        217..236
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT   TRANSMEM        248..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT   REGION          281..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        301..315
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         145
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   315 AA;  33808 MW;  1745E7098F8F9917 CRC64;
     MTVVDHLAAI PSPTQGVWEL GPLPIRAYAL CIVAGIVAAV LLTERRWVAR GGAPGDVLDI
     AVWAVPFGII GGRIYHVISS PRAYFGEGGD PMRAFAIWEG GLGIWGAIAL GGVGAWIACR
     RRGIPLPAFA DALAPGLLVA QAIGRLGNWF NNELYGGPTD LPWALTIHEW SGGRAVVDPD
     GAPVVLGTFH PTFLYELLWN LAAAAFVIWA DRRFRLGHGR AFAVYVVSYC VGRLWIELMR
     TDPAETLFGV RINVFTAIIV GLLALAYFVW QRGRPREVIT RGGQAGAPGT AAPVEEPATD
     PGLVRQEEHR PAEPG
//
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