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Database: UniProt
Entry: A0A1J0A6K0_9ENTE
LinkDB: A0A1J0A6K0_9ENTE
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ID   A0A1J0A6K0_9ENTE        Unreviewed;       272 AA.
AC   A0A1J0A6K0;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=BHY08_06770 {ECO:0000313|EMBL:APB31556.1};
OS   Vagococcus teuberi.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Vagococcus.
OX   NCBI_TaxID=519472 {ECO:0000313|EMBL:APB31556.1, ECO:0000313|Proteomes:UP000191200};
RN   [1] {ECO:0000313|EMBL:APB31556.1, ECO:0000313|Proteomes:UP000191200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21459 {ECO:0000313|EMBL:APB31556.1,
RC   ECO:0000313|Proteomes:UP000191200};
RA   Wullschleger S., Seifert C., Baumgartner S., Lacroix C., Bonfoh B.,
RA   Stevens M.J., Meile L.;
RT   "Vagococcus teuberi sp. nov., isolated from the Malian artisanal sour milk
RT   fene.";
RL   Submitted (SEP-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}.
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DR   EMBL; CP017267; APB31556.1; -; Genomic_DNA.
DR   RefSeq; WP_071457148.1; NZ_CP017267.1.
DR   AlphaFoldDB; A0A1J0A6K0; -.
DR   STRING; 519472.BHY08_06770; -.
DR   KEGG; vte:BHY08_06770; -.
DR   OrthoDB; 871140at2; -.
DR   UniPathway; UPA00664; -.
DR   Proteomes; UP000191200; Chromosome.
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:APB31556.1};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01147};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191200};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01147, ECO:0000313|EMBL:APB31556.1};
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        53..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT   TRANSMEM        91..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT   TRANSMEM        176..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT   TRANSMEM        206..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT   TRANSMEM        233..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT   BINDING         134
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   272 AA;  31344 MW;  D4CFDE11BDD8A91A CRC64;
     MIAAINPTAF HIFGIGIQWY AIIIVSGIVL VSWLATKEAV RVGLKEDDVI DMMLWALPIS
     IIGARLYYVI FEWQYYSQNP IEIFAIRNGG LAIYGGLIAG GLVLYFYTRH HFINTWTFLD
     VAAPSVLLAQ AIGRWGNFMN HEAFGEITTK GFLMKLHLPN FIIENMYIDG AYRQPTFLYE
     SSWNVLGFII IILLRRKEHF FKQGEIALTY VLWYSFGRFF IEGMRTDSLM FFGGLRVSQI
     LSAVLFIGAM ILIAIRRRNK ELPYYNRSYS IK
//
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