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Database: UniProt
Entry: A0A171DN11_9ACTN
LinkDB: A0A171DN11_9ACTN
Original site: A0A171DN11_9ACTN 
ID   A0A171DN11_9ACTN        Unreviewed;       294 AA.
AC   A0A171DN11;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
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=PS9374_06122 {ECO:0000313|EMBL:GAT70440.1};
OS   Planomonospora sphaerica.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Planomonospora.
OX   NCBI_TaxID=161355 {ECO:0000313|EMBL:GAT70440.1, ECO:0000313|Proteomes:UP000077701};
RN   [1] {ECO:0000313|EMBL:GAT70440.1, ECO:0000313|Proteomes:UP000077701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 9374 {ECO:0000313|EMBL:GAT70440.1,
RC   ECO:0000313|Proteomes:UP000077701};
RA   Dohra H., Suzuki T., Inoue Y., Kodani S.;
RT   "Draft Genome Sequence of Planomonospora sphaerica JCM9374, a Rare
RT   Actinomycete.";
RL   Genome Announc. 4:e00779-16(2016).
RN   [2] {ECO:0000313|Proteomes:UP000077701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 9374 {ECO:0000313|Proteomes:UP000077701};
RA   Suzuki T., Dohra H., Kodani S.;
RT   "Planomonospora sphaerica JCM9374 whole genome shotgun sequence.";
RL   Submitted (APR-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:GAT70440.1}.
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DR   EMBL; BDCX01000017; GAT70440.1; -; Genomic_DNA.
DR   RefSeq; WP_068902674.1; NZ_BDCX01000017.1.
DR   AlphaFoldDB; A0A171DN11; -.
DR   STRING; 161355.PS9374_06122; -.
DR   OrthoDB; 871140at2; -.
DR   UniPathway; UPA00664; -.
DR   Proteomes; UP000077701; 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:GAT70440.1};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01147};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077701};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01147, ECO:0000313|EMBL:GAT70440.1};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01147};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01147}.
FT   TRANSMEM        30..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT   TRANSMEM        114..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT   TRANSMEM        202..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT   BINDING         157
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   294 AA;  31736 MW;  AFD660BB011CDD14 CRC64;
     MSPTVSSAVS LAGIPSPSEG VWHLGPLPVR GYTVCIMLGV VVAVVVAERR WRNRGGAPGT
     MVDLVTWGLP FGIVGARLYH VITDWQLYFG PGAPHRPIDA ILVWSDSGPG WRGLGVWGGI
     ALGGVGVWIA CRRRGISVSA VADTVAPAVA IGQAVGRWCN YFNQELFGGP TDLPWGLVIE
     AGRPGTVPGV TTYHPTFLYE SLWNLGLALA LVWIGGRFAL RHGRLFALYV AGYTAGRFWI
     EGLRVDPANE ILGMRLNQWT SIALFLGALA YVHLTRNKRS EESLGDERTP AEVR
//
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