PGLL2_ACIAD
ID PGLL2_ACIAD Reviewed; 548 AA.
AC Q6F7F9;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=ComP-specific O-oligosaccharyltransferase {ECO:0000303|PubMed:25727908};
DE Short=ComP-specific O-OTase {ECO:0000303|PubMed:25727908};
DE EC=2.4.-.- {ECO:0000305|PubMed:23658772, ECO:0000305|PubMed:25727908};
GN Name=pglL2 {ECO:0000305}; Synonyms=pglL {ECO:0000303|PubMed:23658772};
GN OrderedLocusNames=ACIAD3337 {ECO:0000312|EMBL:CAG70006.1};
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=23658772; DOI=10.1371/journal.pone.0062768;
RA Schulz B.L., Jen F.E., Power P.M., Jones C.E., Fox K.L., Ku S.C.,
RA Blanchfield J.T., Jennings M.P.;
RT "Identification of bacterial protein O-oligosaccharyltransferases and their
RT glycoprotein substrates.";
RL PLoS ONE 8:E62768-E62768(2013).
RN [3]
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: Specifically catalyzes the glycosylation of the pilin-like
CC competence factor ComP. {ECO:0000269|PubMed:23658772}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Loss of glycosylation of the ComP protein.
CC {ECO:0000269|PubMed:23658772, ECO:0000269|PubMed:25727908}.
CC -!- SIMILARITY: Belongs to the PglL O-oligosaccharyltransferase family.
CC {ECO:0000305}.
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DR EMBL; CR543861; CAG70006.1; -; Genomic_DNA.
DR RefSeq; WP_004923783.1; NC_005966.1.
DR AlphaFoldDB; Q6F7F9; -.
DR SMR; Q6F7F9; -.
DR STRING; 62977.ACIAD3337; -.
DR EnsemblBacteria; CAG70006; CAG70006; ACIAD3337.
DR GeneID; 45235534; -.
DR KEGG; aci:ACIAD3337; -.
DR eggNOG; COG3307; Bacteria.
DR HOGENOM; CLU_501210_0_0_6; -.
DR OMA; SWGQFLN; -.
DR OrthoDB; 1897460at2; -.
DR BioCyc; ASP62977:ACIAD_RS15095-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..548
FT /note="ComP-specific O-oligosaccharyltransferase"
FT /id="PRO_0000433787"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 548 AA; 64444 MW; 17EF64AD2DCA3C6E CRC64;
MNSIFKKIKN YTIVSGVFFL GSAFIIPNTS NLSSTLYKEL IAVLGLLILL TVKSFDYKKI
LIPKNFYWFL FVIFIIFIQL IVGEIYFFQD FFFSISFLVI LFLSFLLGFN ERLNGDDLIV
KKIAWIFIIV VQISFLIAIN QKIEIVQNFF LFSSSYNGRS TANLGQPNQF STLILITLFL
LCYLREKNSL NNMVFNILSF CLIFANVMTQ SRSAWISVIL ISLLYLLKFQ KKIELRRVIF
FNIVFWTLVY CVPLLFNLIF FQKNSYSTFD RLTMGSSRFE IWPQLLKAVF HKPFIGYGWG
QTGVAQLETI NKSSTKGEWF TYSHNLFLDL MLWNGFFIGL IISILILCFL IELYSSIKNK
SDLFLFFCVV AFFVHCLLEY PFAYTYFLIP VGFLCGYIST QNIKNSISYF NLSKRKLTLF
LGCCWLGYVA FWVEVLDISK KNEIYARQFL FSNHVKFYNI ENYILDGFSK QLDFQYLDYC
ELKDKYQLLD FKKVAYRYPN ASIVYKYYSI SAEMKMDQKS ANQIIRAYSV IKNQKIIKPK
LKFCSIEY
