ID H2IWY4_RAHAC Unreviewed; 289 AA.
AC H2IWY4;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
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 OrderedLocusNames=Rahaq2_0891 {ECO:0000313|EMBL:AEX50796.1};
OS Rahnella aquatilis (strain ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 /
OS NCIMB 13365 / CIP 78.65).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Rahnella.
OX NCBI_TaxID=745277 {ECO:0000313|EMBL:AEX50796.1, ECO:0000313|Proteomes:UP000009010};
RN [1] {ECO:0000313|EMBL:AEX50796.1, ECO:0000313|Proteomes:UP000009010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 /
RC CIP 78.65 {ECO:0000313|Proteomes:UP000009010};
RX PubMed=22582378; DOI=10.1128/JB.00380-12;
RA Martinez R.J., Bruce D., Detter C., Goodwin L.A., Han J., Han C.S.,
RA Held B., Land M.L., Mikhailova N., Nolan M., Pennacchio L., Pitluck S.,
RA Tapia R., Woyke T., Sobecky P.A.;
RT "Complete Genome Sequence of Rahnella aquatilis CIP 78.65.";
RL J. Bacteriol. 194:3020-3021(2012).
RN [2] {ECO:0000313|Proteomes:UP000009010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 /
RC CIP 78.65 {ECO:0000313|Proteomes:UP000009010};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Held B., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sobecky P.,
RA Martinez R., Woyke T.;
RT "Complete sequence of chromosome of Rahnella aquatilis CIP 78.65.";
RL Submitted (JAN-2012) 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 inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_01147}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01147}.
CC -!- SIMILARITY: Belongs to the Lgt family. {ECO:0000256|ARBA:ARBA00007150,
CC ECO:0000256|HAMAP-Rule:MF_01147}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003244; AEX50796.1; -; Genomic_DNA.
DR RefSeq; WP_015696064.1; NZ_JMPO01000130.1.
DR AlphaFoldDB; H2IWY4; -.
DR STRING; 745277.Rahaq2_0891; -.
DR GeneID; 61511006; -.
DR KEGG; raq:Rahaq2_0891; -.
DR PATRIC; fig|745277.3.peg.839; -.
DR eggNOG; COG0682; Bacteria.
DR HOGENOM; CLU_013386_1_0_6; -.
DR OrthoDB; 871140at2; -.
DR UniPathway; UPA00664; -.
DR Proteomes; UP000009010; 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 inner membrane {ECO:0000256|HAMAP-Rule:MF_01147};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01147};
KW Lipoprotein {ECO:0000313|EMBL:AEX50796.1};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_01147};
KW Reference proteome {ECO:0000313|Proteomes:UP000009010};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01147, ECO:0000313|EMBL:AEX50796.1};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01147};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01147}.
FT TRANSMEM 23..40
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 100..118
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 130..148
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 200..218
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 225..242
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 262..281
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT BINDING 143
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 289 AA; 32526 MW; FA7DA1310DB7884B CRC64;
MSNSYLAFPQ FDPVIFSIGP VSLHWYGLMY LVGFVFAMWL AVRRANKPGS GWTKDEVENL
LYAGFLGVFL GGRIGYVFFY NLPLFLDNPL YLFKVWDGGM SFHGGLIGVI VVMLIFAHRT
KRNFFQVSDF IAPLIPFGLG AGRLGNFING ELWGRVTTDV PWAMLFPGSR QEDIAIAAAD
PKWQPLLNQY GVLPRHPSQL YELLLEGVVL FIILNVFIRK SRPMGAVSGL FLIGYGLFRI
IVEHFRQPDA QLGLFDGIIS MGQVLSIPMV VIGLIVMVWA YRRPQKQLS
//
