ID B8H6V1_PSECP Unreviewed; 396 AA.
AC B8H6V1;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 97.
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=Achl_1685 {ECO:0000313|EMBL:ACL39672.1};
OS Pseudarthrobacter chlorophenolicus (strain ATCC 700700 / DSM 12829 / CIP
OS 107037 / JCM 12360 / KCTC 9906 / NCIMB 13794 / A6) (Arthrobacter
OS chlorophenolicus).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Pseudarthrobacter.
OX NCBI_TaxID=452863 {ECO:0000313|EMBL:ACL39672.1, ECO:0000313|Proteomes:UP000002505};
RN [1] {ECO:0000313|EMBL:ACL39672.1, ECO:0000313|Proteomes:UP000002505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700700 / DSM 12829 / CIP 107037 / JCM 12360 / KCTC 9906 /
RC NCIMB 13794 / A6 {ECO:0000313|Proteomes:UP000002505};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Goltsman E., Clum A., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Jansson J., Richardson P.;
RT "Complete sequence of chromosome of Arthrobacter chlorophenolicus A6.";
RL Submitted (JAN-2009) 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; CP001341; ACL39672.1; -; Genomic_DNA.
DR RefSeq; WP_015936892.1; NC_011886.1.
DR AlphaFoldDB; B8H6V1; -.
DR STRING; 452863.Achl_1685; -.
DR KEGG; ach:Achl_1685; -.
DR eggNOG; COG0682; Bacteria.
DR HOGENOM; CLU_013386_2_2_11; -.
DR OrthoDB; 871140at2; -.
DR UniPathway; UPA00664; -.
DR Proteomes; UP000002505; 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:ACL39672.1};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_01147};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01147, ECO:0000313|EMBL:ACL39672.1};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01147};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01147}.
FT TRANSMEM 40..61
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 73..91
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 119..136
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 143..161
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 205..222
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 234..250
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT TRANSMEM 270..289
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01147"
FT REGION 298..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 162
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 396 AA; 42420 MW; 774559B035030BE7 CRC64;
MQTLLAAAEL APTLVPASIP SPGWSGFDIP LPWGSLRIHA YALCILAGII AGLWLTSVRW
AKRGAPEGSV WDIVIWAIPF GIIGGRLYHV FSSPDAYFGP GFDGTGDLSL IPQIQRGGLG
IWGAVVLGVI GAWIGCRRSG VKLSAFLDAA APGLLLAQAL GRWGNWFNQE LFGGPTTLPW
GLQIDADNPN FPAGVPADTL FHPTFLYESL WNIAGVVILL VLDRRFNFRR SRLFWLYAMY
YTLGRVWIEA MRIDDAEQVS LFGITTRLNV WTSILVFVVA LAAFILLGLK KRTEPDTVYL
PGRKPADRAV EKPADADATG DATRTDEQVR DADPVVSDSE SRDNLPDNQS GSRPASVPAE
KVQAAPAGSK PDTDAAATGH SGSTATGTAP EAGSSK
//
