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Database: UniProt
Entry: A0A1C0A7Z1_9FIRM
LinkDB: A0A1C0A7Z1_9FIRM
Original site: A0A1C0A7Z1_9FIRM 
ID   A0A1C0A7Z1_9FIRM        Unreviewed;       277 AA.
AC   A0A1C0A7Z1;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   13-SEP-2023, entry version 23.
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=U472_10050 {ECO:0000313|EMBL:OCL26340.1};
OS   Orenia metallireducens.
OC   Bacteria; Bacillota; Clostridia; Halanaerobiales; Halobacteroidaceae;
OC   Orenia.
OX   NCBI_TaxID=1413210 {ECO:0000313|EMBL:OCL26340.1, ECO:0000313|Proteomes:UP000093514};
RN   [1] {ECO:0000313|Proteomes:UP000093514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Z6 {ECO:0000313|Proteomes:UP000093514};
RA   Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:OCL26340.1, ECO:0000313|Proteomes:UP000093514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Z6 {ECO:0000313|EMBL:OCL26340.1,
RC   ECO:0000313|Proteomes:UP000093514};
RA   Maxim B.I., Kenneth K., Flynn T.M., Oloughlin E.J., Locke R.A., Weber J.R.,
RA   Egan S.M., Mackie R.I., Cann I.K.;
RT   "Orenia metallireducens sp. nov. strain Z6, a Novel Metal-reducing
RT   Firmicute from the Deep Subsurface.";
RL   Submitted (AUG-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: 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:OCL26340.1}.
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DR   EMBL; LWDV01000009; OCL26340.1; -; Genomic_DNA.
DR   RefSeq; WP_068718067.1; NZ_LWDV01000009.1.
DR   AlphaFoldDB; A0A1C0A7Z1; -.
DR   OrthoDB; 871140at2; -.
DR   UniPathway; UPA00664; -.
DR   Proteomes; UP000093514; 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.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01147};
KW   Lipoprotein {ECO:0000313|EMBL:OCL26340.1};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01147};
KW   Reference proteome {ECO:0000313|Proteomes:UP000093514};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01147, ECO:0000313|EMBL:OCL26340.1};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01147};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01147}.
FT   TRANSMEM        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT   TRANSMEM        45..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT   TRANSMEM        86..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT   TRANSMEM        117..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT   TRANSMEM        159..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT   TRANSMEM        187..205
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        256..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT   BINDING         131
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   277 AA;  31239 MW;  D6244AA9AB872B51 CRC64;
     MQTILFRLGP FSISLFGTFI ALGIAAGFYI LNLEAKREQL DQDEVFNLAL YSIVAAIIGA
     RLYYLLVFNP AYYLKNPSEI IMIQQGGLSI QGGLIGAILV AWFYVKKKKL NFWKLADAFA
     PAIILGQAIG RIGCDVFGVA MKKAYPWGVK IGQQILHPAQ AYEIILNYIL FAILWNLRDK
     VKYHGQLFLW YIIGFSINRG IVEFFRSNPL VFKPFTVAHL TSLVIVLVAG IIMSLIKDKI
     KNRPIEAKAI SLKVKLRDNL IILVATAFSL LTYYSFY
//
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