(data stored in ACNUC7421 zone)

SWISSPROT: A4AWN1_MARSH

ID   A4AWN1_MARSH            Unreviewed;       320 AA.
AC   A4AWN1;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 67.
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   OrderedLocusNames=FB2170_01756 {ECO:0000313|EMBL:EAQ99645.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAQ99645.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAQ99645.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
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; CP002157; EAQ99645.1; -; Genomic_DNA.
DR   RefSeq; WP_013305044.1; NC_014472.1.
DR   STRING; 313603.FB2170_01756; -.
DR   EnsemblBacteria; EAQ99645; EAQ99645; FB2170_01756.
DR   KEGG; fbc:FB2170_01756; -.
DR   eggNOG; ENOG4107QZC; Bacteria.
DR   eggNOG; COG0682; LUCA.
DR   HOGENOM; HOG000098666; -.
DR   OMA; HQYLFFI; -.
DR   OrthoDB; 435911at2; -.
DR   BioCyc; MSP313603:G1GNS-612-MONOMER; -.
DR   UniPathway; UPA00664; -.
DR   Proteomes; UP000001602; 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.
PE   3: Inferred from homology;
DR   PRODOM; A4AWN1.
DR   SWISS-2DPAGE; A4AWN1.
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:UP000001602};
KW   Lipoprotein {ECO:0000313|EMBL:EAQ99645.1};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01147,
KW   ECO:0000256|SAAS:SAAS00704538};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001602};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01147,
KW   ECO:0000256|SAAS:SAAS00704540, ECO:0000313|EMBL:EAQ99645.1};
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     24     44       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01147}.
FT   TRANSMEM     56     76       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01147}.
FT   TRANSMEM    110    132       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01147}.
FT   TRANSMEM    144    165       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01147}.
FT   TRANSMEM    231    250       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01147}.
FT   TRANSMEM    259    277       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01147}.
FT   TRANSMEM    297    313       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01147}.
FT   BINDING     160    160       Lipid substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01147}.
SQ   SEQUENCE   320 AA;  37099 MW;  301ABC639350EAC9 CRC64;
     MHFLGFIWNP NETLFKIGFL QIKYYNLLWI IAFALGWYIM KRVFNNEKKS VEQLDSLFIH
     AVLATMLGAR LGHVFFYDWP YYKNHIAEIL LPIRENAGET LFGIINGYEF TGFTGLASHG
     AAIGVIIGMY LYTRKFPEFK LLWVLDRVVI PVAIGAFCVR LGNFFNSEIN GKVTDESFIF
     ATKFIRDSDD MHPSKALGVT KEKTVNAAYD AIQNNTQFSE YLAQIPYRHP AQLYEGVCYI
     FVFLLLYYLY WKTDKKNKLG YLFGLFLVLL WTIRFFVEFV KKSQGGFEES LGLLSTGQWL
     SIPFILIGLY FMFRPSTKKS
//

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