ID A0A1A0LY87_9MYCO Unreviewed; 785 AA.
AC A0A1A0LY87;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=A9W99_04525 {ECO:0000313|EMBL:OBA77791.1};
OS Mycobacterium sp. 1164966.3.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1856861 {ECO:0000313|EMBL:OBA77791.1, ECO:0000313|Proteomes:UP000092060};
RN [1] {ECO:0000313|Proteomes:UP000092060}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1164966.3 {ECO:0000313|Proteomes:UP000092060};
RA Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Garcia-Basteiro A.,
RA Lopez-Varela E., Palencia S.;
RL Submitted (JUN-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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:OBA77791.1}.
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DR EMBL; LZSG01000070; OBA77791.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1A0LY87; -.
DR STRING; 1856861.A9W99_04525; -.
DR UniPathway; UPA00664; -.
DR Proteomes; UP000092060; 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:OBA77791.1};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_01147};
KW Reference proteome {ECO:0000313|Proteomes:UP000092060};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01147, ECO:0000313|EMBL:OBA77791.1};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01147};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01147}.
FT TRANSMEM 74..91
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 170..187
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 199..217
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 229..247
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT REGION 259..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..447
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..587
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..745
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 117
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 785 AA; 83793 MW; 2E7498F51D86FA65 CRC64;
MFIIIGIVVA LLISDRRWAA RGGQRGVVYD IALWVVPFGL IGGRLYHLAT DWRTYFAPGG
AGFLAALRIW DGGLGIWGAI ALGVLGGWIA CRRRNIPFPS MLDAVAPGVV LAQAIGRLGN
YFNQELYGRE TTLPWGLEIF YRRDPAGFVD VHSLDGVSTG QLAFVVQPTF LYELIWNVLV
FVALIYLDRR FTLSHGRLFA LYIALYCAGR FWVELLRDDA ATHIAGIRIN SFTSTFVFIG
AVVYIILATK GREEPAILRG TGPVAEKAPE PEPVAEPTPV SADAVPTIAA PAGPGEDDKL
VDFSEVAKSE EGAEPEVAET GSAAAAEAEV IEPEAIEPQA QAATTPEVAE VAQTAPEVVE
PEVAEAAVAQ PEMGGWLRRL RSRRQAQSVE AAEPEVAQAE AAEPESVEPE PAEPDVLEPD
AAEPEVGEPE ATEPEVGEPE ATEPEVLESE VADAGVAEPG PAQTEVAEAG EATVAEAAAA
KGAQVEEVRA AEPEAEEVVA DEEAPPEVAA AAAAEPEVGG WLRRLRSRRQ KARSVEREPE
AAGPDVVEPG PAEPDEVEPE AAEPQVAEPE VAEPEVAEPE VAEPEVAEPE VAEVVAAEPE
ALKGAEPEVE EAEPEVEEAE PEIDEAEVEA AELEPEAEGS EAEAEQAEPE TGESEVEAAE
LEPEAEYSEA EVEEAEPETE VPEVEAAESE PVEPEAEEEH PESEAAEEPV DKAEDFVEEA
EADEKPDTEV DSTEADSEAP AVEKADEDDE DRAAPSSPPP TSGTPGSARE RWRQRMRNLR
SRSGR
//
