LGT_BACSU
ID LGT_BACSU Reviewed; 269 AA.
AC O34752; Q9R9E2;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 124.
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};
DE AltName: Full=Spore germination protein GerF;
GN Name=lgt {ECO:0000255|HAMAP-Rule:MF_01147}; Synonyms=gerF;
GN OrderedLocusNames=BSU34990;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Dartois V.A., Hoch J.A.;
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Lazarevic V., Soldo B., Rivolta C., Reynolds S., Mauel C., Karamata D.;
RT "Nucleotide sequence of the 300-304 chromosomal segment of Bacillus
RT subtilis.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9846746; DOI=10.1099/00221287-144-11-3105;
RA Robinson C., Rivolta C., Karamata D., Moir A.;
RT "The product of the yvoC (gerF) gene of Bacillus subtilis is required for
RT spore germination.";
RL Microbiology 144:3105-3109(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [5]
RP CHARACTERIZATION.
RX PubMed=10096076; DOI=10.1046/j.1365-2958.1999.01247.x;
RA Leskelae S., Wahlstroem E., Kontinen V.P., Sarvas M.;
RT "Lipid modification of prelipoproteins is dispensable for growth but
RT essential for efficient protein secretion in Bacillus subtilis:
RT characterization of the Lgt gene.";
RL Mol. Microbiol. 31:1075-1085(1999).
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. Required for spore germination.
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 membrane {ECO:0000255|HAMAP-Rule:MF_01147,
CC ECO:0000305}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01147, ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Lgt family. {ECO:0000255|HAMAP-
CC Rule:MF_01147, ECO:0000305}.
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DR EMBL; U63310; AAD09501.1; -; Genomic_DNA.
DR EMBL; AF017113; AAC67287.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15504.1; -; Genomic_DNA.
DR PIR; C69651; C69651.
DR RefSeq; NP_391379.1; NC_000964.3.
DR RefSeq; WP_003242661.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O34752; -.
DR SMR; O34752; -.
DR STRING; 224308.BSU34990; -.
DR PaxDb; O34752; -.
DR PRIDE; O34752; -.
DR EnsemblBacteria; CAB15504; CAB15504; BSU_34990.
DR GeneID; 936609; -.
DR KEGG; bsu:BSU34990; -.
DR PATRIC; fig|224308.179.peg.3787; -.
DR eggNOG; COG0682; Bacteria.
DR InParanoid; O34752; -.
DR OMA; TDVPWAI; -.
DR PhylomeDB; O34752; -.
DR BioCyc; BSUB:BSU34990-MON; -.
DR UniPathway; UPA00664; -.
DR Proteomes; UP000001570; 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 1: Evidence at protein level;
KW Cell membrane; Germination; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..269
FT /note="Phosphatidylglycerol--prolipoprotein diacylglyceryl
FT transferase"
FT /id="PRO_0000172556"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01147"
FT BINDING 137
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"
FT CONFLICT 31
FT /note="A -> P (in Ref. 1; AAD09501)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 269 AA; 30619 MW; 6D2E00DC07482C68 CRC64;
MNEAIEPLNP IAFQLGPLAV HWYGIIIGLG ALLGLWIAMR ESEKRGLQKD TFIDLVLFAI
PIAIICARIY YVAFEWDYYA AHPGEIIKIW KGGIAIHGGL IGAILTGYVF SRVKNLSFWK
LADIAAPSIL LGQAIGRWGN FMNQEAHGEA VSRAFLENLH LPEFIINQMY INGQYYHPTF
LYESLWSFVG VIVLLLLRRA NLRRGEMFLI YIIWYSIGRY FIEGMRTDSL MLTDSLRIAQ
VISIVLIVLA VAAIIFRRVK GYSKERYAE
