LGT_ZYMMO
ID LGT_ZYMMO Reviewed; 285 AA.
AC Q9FDM1; Q5NQT9;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase {ECO:0000255|HAMAP-Rule:MF_01147};
DE EC=2.5.1.145 {ECO:0000255|HAMAP-Rule:MF_01147};
GN Name=lgt {ECO:0000255|HAMAP-Rule:MF_01147}; OrderedLocusNames=ZMO0291;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RA Lee H.J., Kang H.S.;
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
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:0000255|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:0000255|HAMAP-Rule:MF_01147};
CC -!- PATHWAY: Protein modification; lipoprotein biosynthesis (diacylglyceryl
CC transfer). {ECO:0000255|HAMAP-Rule:MF_01147}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01147}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01147}.
CC -!- SIMILARITY: Belongs to the Lgt family. {ECO:0000255|HAMAP-
CC Rule:MF_01147}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG02148.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; AF212041; AAG02148.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE008692; AAV88915.2; -; Genomic_DNA.
DR RefSeq; WP_011240228.1; NZ_CP035711.1.
DR AlphaFoldDB; Q9FDM1; -.
DR SMR; Q9FDM1; -.
DR STRING; 264203.ZMO0291; -.
DR EnsemblBacteria; AAV88915; AAV88915; ZMO0291.
DR GeneID; 58026155; -.
DR KEGG; zmo:ZMO0291; -.
DR eggNOG; COG0682; Bacteria.
DR HOGENOM; CLU_013386_1_0_5; -.
DR OMA; TDVPWAI; -.
DR OrthoDB; 435911at2; -.
DR UniPathway; UPA00664; -.
DR Proteomes; UP000001173; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
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; PTHR30589; 1.
DR Pfam; PF01790; LGT; 1.
DR TIGRFAMs; TIGR00544; lgt; 1.
DR PROSITE; PS01311; LGT; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..285
FT /note="Phosphatidylglycerol--prolipoprotein diacylglyceryl
FT transferase"
FT /id="PRO_0000172724"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT BINDING 160
FT /ligand="1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol)"
FT /ligand_id="ChEBI:CHEBI:64716"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
SQ SEQUENCE 285 AA; 32173 MW; 25F7A75540C16620 CRC64;
MPFAFIEQMK SVIHFDALGL SPIAFDLGVW HLFGLTLHPL IHWYALAYIT GILLAWRYVL
FLLKQPGTPM KPEQTDDLVF WSTLGILVGG RLAYVLFYQP AILENPLEIF KLWEGGMSYH
GGMIGVFLAI WWVKTTNHLS WLRIADYIGC AAPIGLFLGR LANFVNGELW GRPSTMPWAV
IFPQAGALPR HPSQLYEAGL EGILLFAFLN YQFFATKARL HPGKLAGFFL VGYGLSRFIV
EWFREPDVQL GTLSWGLTMG QTLTIPMVIA GLWLIITSKK REISL