ID A0A077EG10_9FLAO Unreviewed; 279 AA.
AC A0A077EG10;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 50.
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=BD94_1738 {ECO:0000313|EMBL:AIL45513.1};
OS Elizabethkingia anophelis NUHP1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Elizabethkingia.
OX NCBI_TaxID=1338011 {ECO:0000313|EMBL:AIL45513.1, ECO:0000313|Proteomes:UP000028933};
RN [1] {ECO:0000313|EMBL:AIL45513.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NUHP1 {ECO:0000313|EMBL:AIL45513.1};
RX PubMed=24012265; DOI=10.1016/S0140-6736(13)61858-9;
RA Teo J., Tan S.Y., Tay M., Ding Y., Kjelleberg S., Givskov M., Lin R.T.,
RA Yang L.;
RT "First case of E anophelis outbreak in an intensive-care unit.";
RL Lancet 382:855-856(2013).
RN [2] {ECO:0000313|EMBL:AIL45513.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NUHP1 {ECO:0000313|EMBL:AIL45513.1};
RX PubMed=26019164; DOI=10.1093/gbe/evv101;
RA Li Y., Liu Y., Chew S.C., Tay M., Salido M.M., Teo J., Lauro F.M.,
RA Givskov M., Yang L.;
RT "Complete Genome Sequence and Transcriptomic Analysis of the Novel Pathogen
RT Elizabethkingia anophelis in Response to Oxidative Stress.";
RL Genome Biol. Evol. 7:1676-1685(2015).
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; CP007547; AIL45513.1; -; Genomic_DNA.
DR RefSeq; WP_024564556.1; NZ_CP007547.1.
DR AlphaFoldDB; A0A077EG10; -.
DR STRING; 1338011.BD94_1738; -.
DR KEGG; eao:BD94_1738; -.
DR eggNOG; COG0682; Bacteria.
DR HOGENOM; CLU_013386_1_0_10; -.
DR UniPathway; UPA00664; -.
DR Proteomes; UP000028933; 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.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01147};
KW Lipoprotein {ECO:0000313|EMBL:AIL45513.1};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_01147};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01147, ECO:0000313|EMBL:AIL45513.1};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01147};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01147}.
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 57..80
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 100..127
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 134..152
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 186..204
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 216..235
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT BINDING 153
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 279 AA; 31738 MW; 6AED3C7392F8C0C7 CRC64;
MSLLYINWDV NPEIVNIGGG FPLKYYGLLF CIGLILCYNL LGKVYKKEQL SEKAHEALFA
YAFIGILVGA RLGHCLFYDF DYYSQHPLEI FLPIQKGEDG AYHFIGYAGL ASHGGVIGLI
IMMIFYARKY KIQFLRIFDI IAIVAPLGGA FIRLGNLMNS EIIGTPSNLP WAFVFRHVDD
VPRHPAQLYE AISYFIIFFS VYFIYQKGIF KAGKGFYFGI SICLIFILRI AVEFIKVDQV
NFEHGMILNM GQILSIPFII LGLFFIIKNL LGMKKLQTS
//
