ID   PGLL1_ACIAD             Reviewed;         568 AA.
AC   Q6FFS6;
DT   16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=General O-oligosaccharyltransferase {ECO:0000303|PubMed:25727908};
DE            Short=General O-OTase {ECO:0000303|PubMed:25727908};
DE            EC=2.4.-.- {ECO:0000305|PubMed:25727908};
GN   Name=pglL1 {ECO:0000305}; Synonyms=pglL {ECO:0000303|PubMed:25727908};
GN   OrderedLocusNames=ACIAD0103 {ECO:0000312|EMBL:CAG67081.1};
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=25727908; DOI=10.1111/mmi.12986;
RA   Harding C.M., Nasr M.A., Kinsella R.L., Scott N.E., Foster L.J.,
RA   Weber B.S., Fiester S.E., Actis L.A., Tracy E.N., Munson R.S. Jr.,
RA   Feldman M.F.;
RT   "Acinetobacter strains carry two functional oligosaccharyltransferases, one
RT   devoted exclusively to type IV pilin, and the other one dedicated to O-
RT   glycosylation of multiple proteins.";
RL   Mol. Microbiol. 96:1023-1041(2015).
CC   -!- FUNCTION: Catalyzes the O-glycosylation of multiple protein targets. Is
CC       responsible for general protein glycosylation within A.baylyi ADP1.
CC       Does not act as an O-antigen ligase. {ECO:0000269|PubMed:25727908}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene lose the ability to
CC       glycosylate substrate proteins and their glycoproteome is highly
CC       affected. {ECO:0000269|PubMed:25727908}.
CC   -!- SIMILARITY: Belongs to the PglL O-oligosaccharyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; CR543861; CAG67081.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6FFS6; -.
DR   SMR; Q6FFS6; -.
DR   STRING; 62977.ACIAD0103; -.
DR   EnsemblBacteria; CAG67081; CAG67081; ACIAD0103.
DR   KEGG; aci:ACIAD0103; -.
DR   eggNOG; COG3307; Bacteria.
DR   HOGENOM; CLU_031791_1_0_6; -.
DR   OMA; GAICLIM; -.
DR   BioCyc; ASP62977:ACIAD_RS00480-MON; -.
DR   Proteomes; UP000000430; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016757; F:glycosyltransferase activity; IMP:UniProtKB.
DR   GO; GO:0006486; P:protein glycosylation; IMP:UniProtKB.
DR   InterPro; IPR007016; O-antigen_ligase-related.
DR   InterPro; IPR031726; PglL_A.
DR   InterPro; IPR021797; Wzy_C_2.
DR   Pfam; PF15864; PglL_A; 1.
DR   Pfam; PF04932; Wzy_C; 1.
DR   Pfam; PF11846; Wzy_C_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Glycosyltransferase; Membrane; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..568
FT                   /note="General O-oligosaccharyltransferase"
FT                   /id="PRO_0000433786"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        78..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        101..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        132..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        214..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        251..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        349..369
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        376..396
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        397..417
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        429..449
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   568 AA;  64866 MW;  414D9556CF1C3A9F CRC64;
     MAGSPRVYNS QHCGFSVAVM RFLLLLLTAV LISLAWLSPD HSYPWLTFAS EMLSFAAFLS
     LLALFLNRPL ELPRVQLLAL PVVFIPMIQW GFGLVVDFSS ALLSSAYLLG FWLTMLLGYN
     LSRSSADRER MFTLSSYLLF AVALLTSLIA CIQWLNLESH VPGVMNLYSH RPYANFAQPN
     NMSTFLILGL LGCLYLAEKQ KLKQYYIWPV AALIVFAITL SQSRTAWVFG LFFIIYWTYK
     SWRYPTHLKR YAVLLWAIGF FAVGLLFPRF TRLIQKLKEG NVVQTSSVVE RASAGHERLG
     IWQQMLDAIH QKPWTGYGWN QTSIAELSSM SSNTIHVWFT SAHNVVLDLL VWNGWLLGGL
     ITICILIWIC WLNVHAKTTE SIIACLMVSA VWIHTLLEYP LQYAYFLLPV GFLMGLIQAQ
     TPDQTARSVP VSVIRSIWVI GIMLLALIWR DYNLYKVNSL RILKNQPANI EIWGSSKILV
     LTEFDQRLYW LKLSPVAPLT STELDQIEKM VQNKATPYNL QKYAQLLLAN HQFEKAQQQI
     AYLNRLHKKD YTLQDLQQAN ASAVESSK