ID A0A1E5SLF3_9BACT Unreviewed; 375 AA.
AC A0A1E5SLF3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=BFP71_10465 {ECO:0000313|EMBL:OEJ99958.1};
OS Roseivirga misakiensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Roseivirgaceae;
OC Roseivirga.
OX NCBI_TaxID=1563681 {ECO:0000313|EMBL:OEJ99958.1, ECO:0000313|Proteomes:UP000095552};
RN [1] {ECO:0000313|EMBL:OEJ99958.1, ECO:0000313|Proteomes:UP000095552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK-8 {ECO:0000313|EMBL:OEJ99958.1,
RC ECO:0000313|Proteomes:UP000095552};
RA Wong S.-K., Hamasaki K., Yoshizawa S.;
RT "Draft genome of Fabibacter sp. strain SK-8.";
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:OEJ99958.1}.
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DR EMBL; MDGQ01000005; OEJ99958.1; -; Genomic_DNA.
DR RefSeq; WP_069835421.1; NZ_MDGQ01000005.1.
DR AlphaFoldDB; A0A1E5SLF3; -.
DR STRING; 1563681.BFP71_10465; -.
DR OrthoDB; 871140at2; -.
DR UniPathway; UPA00664; -.
DR Proteomes; UP000095552; 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 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:UP000095552};
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..42
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 54..75
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 95..116
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 313..330
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 350..369
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT BINDING 156
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 375 AA; 43190 MW; DEB174B5E5D7B996 CRC64;
MLLHIVWDPM REIIKDIQPP VWYSLLFASG FIIGYQIMVK IFKKEGKDPL NVDTLTVHMV
LATIVGARLG HLVFYEPKRF LADPLMFFRT WEGGLASHGA AFGILAALYL YSHYFVDANW
SPFRFKFRKQ RRVGQSYLWI VDRIVITVAL AAVFIRFGNF VNSEIIGKPT GSDYGVVFAR
VAEEIIEDSD LGIESAEASK SDSDERLEPG IVPIDLTITF ENRQLSEQDA RKIAESRIKS
ILTRYSNINE HYAEPAGPLN YEFKLVERKP TLVVRTWGIV RHPAQLYESG TSLILFFILL
GIWIRYKDRT PEGLLIGIFL VWIFALRWFH ETFKENQVDF ENDMTYNMGQ LLSIPLLALG
VFILIRVFIK SRKPE
//
