(data stored in SCRATCH zone)

SWISSPROT: A5GRU6_SYNR3

ID   A5GRU6_SYNR3            Unreviewed;       289 AA.
AC   A5GRU6;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 70.
DE   RecName: Full=Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase {ECO:0000256|HAMAP-Rule:MF_01147, ECO:0000256|SAAS:SAAS01134355};
DE            EC=2.5.1.145 {ECO:0000256|HAMAP-Rule:MF_01147, ECO:0000256|SAAS:SAAS01134353};
GN   Name=lgt {ECO:0000256|HAMAP-Rule:MF_01147,
GN   ECO:0000313|EMBL:CAK27605.1};
GN   OrderedLocusNames=SynRCC307_0702 {ECO:0000313|EMBL:CAK27605.1};
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278 {ECO:0000313|EMBL:CAK27605.1, ECO:0000313|Proteomes:UP000001115};
RN   [1] {ECO:0000313|EMBL:CAK27605.1, ECO:0000313|Proteomes:UP000001115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307 {ECO:0000313|Proteomes:UP000001115};
RA   Genoscope;
RL   Submitted (MAY-2006) 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
CC       cysteine of a prolipoprotein, the first step in the formation of
CC       mature lipoproteins. {ECO:0000256|HAMAP-Rule:MF_01147,
CC       ECO:0000256|SAAS:SAAS01134350}.
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-
CC         COMP:14680, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:57685, ChEBI:CHEBI:64716, ChEBI:CHEBI:140658;
CC         EC=2.5.1.145; Evidence={ECO:0000256|HAMAP-Rule:MF_01147,
CC         ECO:0000256|SAAS:SAAS01134354};
CC   -!- PATHWAY: Protein modification; lipoprotein biosynthesis
CC       (diacylglyceryl transfer). {ECO:0000256|HAMAP-Rule:MF_01147,
CC       ECO:0000256|SAAS:SAAS00704521}.
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|HAMAP-
CC       Rule:MF_01147, ECO:0000256|SAAS:SAAS00704541}.
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DR   EMBL; CT978603; CAK27605.1; -; Genomic_DNA.
DR   RefSeq; WP_011935120.1; NC_009482.1.
DR   STRING; 316278.SynRCC307_0702; -.
DR   EnsemblBacteria; CAK27605; CAK27605; SynRCC307_0702.
DR   KEGG; syr:SynRCC307_0702; -.
DR   eggNOG; ENOG4105C3B; Bacteria.
DR   eggNOG; COG0682; LUCA.
DR   HOGENOM; HOG000098668; -.
DR   KO; K13292; -.
DR   OMA; AIRWYGL; -.
DR   OrthoDB; 435911at2; -.
DR   BioCyc; SSP316278:G1GJL-693-MONOMER; -.
DR   UniPathway; UPA00664; -.
DR   Proteomes; UP000001115; 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;
DR   PRODOM; A5GRU6.
DR   SWISS-2DPAGE; A5GRU6.
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01147};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01147,
KW   ECO:0000256|SAAS:SAAS00704533};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001115};
KW   Glycosyltransferase {ECO:0000313|EMBL:CAK27605.1};
KW   Lipoprotein {ECO:0000313|EMBL:CAK27605.1};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01147,
KW   ECO:0000256|SAAS:SAAS00704538};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001115};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01147,
KW   ECO:0000256|SAAS:SAAS00704540, ECO:0000313|EMBL:CAK27605.1};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01147,
KW   ECO:0000256|SAAS:SAAS00704539};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01147,
KW   ECO:0000256|SAAS:SAAS00704519}.
FT   TRANSMEM     27     46       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01147}.
FT   TRANSMEM     58     81       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01147}.
FT   TRANSMEM    101    118       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01147}.
FT   TRANSMEM    125    143       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01147}.
FT   TRANSMEM    185    204       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01147}.
FT   TRANSMEM    213    234       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01147}.
FT   TRANSMEM    254    277       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01147}.
FT   BINDING     144    144       Lipid substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01147}.
SQ   SEQUENCE   289 AA;  32079 MW;  1E3B29450221FC3E CRC64;
     MLNAVLLTPA VFQSPGPMVF EFGPLAVRWY GLLIALAVLL GLWISTQLAK SRGLDGGLIA
     DLLPILVLCA VLGARIYYVL FEWRQYQINW LEAVQIWRGG IAIHGALLGG LLAVIGFTRW
     KRLSFWQLMD VLVPSVALGQ AIGRWGNFFN SEAFGLPTDL PWKLFIPAMS RPEQYLSEQY
     FHPTFLYESI WDLALFVLLV VLFTRRNSQG EPLLANGAIT CLYALIYSLG RFWIEGLRLD
     PLCLFGTLAD GNCIRIAQVV SILLAAAGVA GLAWLYAVGR ELPDPGRPQ
//

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