GenomeNet

Database: UniProt
Entry: U2MA19_9FIRM
LinkDB: U2MA19_9FIRM
Original site: U2MA19_9FIRM 
ID   U2MA19_9FIRM            Unreviewed;       363 AA.
AC   U2MA19;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 45.
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=RUMCAL_01487 {ECO:0000313|EMBL:ERJ96153.1};
OS   Ruminococcus callidus ATCC 27760.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=411473 {ECO:0000313|EMBL:ERJ96153.1, ECO:0000313|Proteomes:UP000016662};
RN   [1] {ECO:0000313|EMBL:ERJ96153.1, ECO:0000313|Proteomes:UP000016662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27760 {ECO:0000313|EMBL:ERJ96153.1,
RC   ECO:0000313|Proteomes:UP000016662};
RA   Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA   O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA   Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL   Submitted (JUL-2013) 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:ERJ96153.1}.
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; AWVF01000183; ERJ96153.1; -; Genomic_DNA.
DR   RefSeq; WP_021682958.1; NZ_KI260451.1.
DR   AlphaFoldDB; U2MA19; -.
DR   STRING; 411473.RUMCAL_01487; -.
DR   GeneID; 78475997; -.
DR   PATRIC; fig|411473.3.peg.1204; -.
DR   eggNOG; COG0682; Bacteria.
DR   HOGENOM; CLU_013386_0_0_9; -.
DR   OrthoDB; 871140at2; -.
DR   UniPathway; UPA00664; -.
DR   Proteomes; UP000016662; 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.
DR   PROSITE; PS01311; LGT; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01147};
KW   Lipoprotein {ECO:0000313|EMBL:ERJ96153.1};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01147};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01147, ECO:0000313|EMBL:ERJ96153.1};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01147};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01147}.
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT   TRANSMEM        69..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT   TRANSMEM        111..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT   TRANSMEM        135..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT   TRANSMEM        210..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT   TRANSMEM        268..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT   REGION          320..363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        328..351
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         154
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   363 AA;  40146 MW;  6777D01E0ABD47A4 CRC64;
     MATETIGTLD YNEIVFPKLG IDLHVNSTAF SIGGLDIQWY GILITLGLVL AMIYAFTQVK
     KYGLNPDRVL DCIIGGIIGG VVGARAYYVL LNWSDYAGDW KSIFNIRGGG LAIYGGIIGS
     LLVGFLVAKI RKVKFLPLLD IVGIGFLLGQ GIGRWGNFFN QEAFGCNTDS LFGMSGGRIQ
     EWITDQYPST TYFANFGTTL DASQPVHPCF LYESLWCLLG FVLLAIFAKK IRRYDGQIFL
     IYICWYGAER AVVESLRTDS LVIGNVRVSQ ILAITCVVIS IILQIAIGTK VKRMGVDYRM
     YKDTNESKQM LAEYEAAKFV KEPEDDTNED TASTDEVAET DTTDSSESDE TPAETDTNQT
     EKE
//
DBGET integrated database retrieval system