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Database: UniProt
Entry: Q5LC75_BACFN
LinkDB: Q5LC75_BACFN
Original site: Q5LC75_BACFN 
ID   Q5LC75_BACFN            Unreviewed;       317 AA.
AC   Q5LC75; A0A380Z698;
DT   21-JUN-2005, integrated into UniProtKB/TrEMBL.
DT   21-JUN-2005, sequence version 1.
DT   24-JAN-2024, entry version 84.
DE   SubName: Full=LPS biosynthesis related glycosyltransferase {ECO:0000313|EMBL:CAH08291.1};
DE   SubName: Full=Putative LPS biosynthesis glycosyltransferase {ECO:0000313|EMBL:SUV40270.1};
DE            EC=2.7.8.33 {ECO:0000313|EMBL:SUV40270.1};
GN   Name=wecA_6 {ECO:0000313|EMBL:SUV40270.1};
GN   ORFNames=BF9343_2510 {ECO:0000313|EMBL:CAH08291.1}, NCTC9343_04210
GN   {ECO:0000313|EMBL:SUV40270.1};
OS   Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS   / NCTC 9343 / Onslow).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=272559 {ECO:0000313|EMBL:CAH08291.1, ECO:0000313|Proteomes:UP000006731};
RN   [1] {ECO:0000313|EMBL:CAH08291.1, ECO:0000313|Proteomes:UP000006731}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 /
RC   Onslow {ECO:0000313|Proteomes:UP000006731};
RX   PubMed=15746427; DOI=10.1126/science.1107008;
RA   Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V.,
RA   Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A.,
RA   Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.,
RA   Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J.,
RA   Barrell B.G., Parkhill J.;
RT   "Extensive DNA inversions in the B. fragilis genome control variable gene
RT   expression.";
RL   Science 307:1463-1465(2005).
RN   [2] {ECO:0000313|EMBL:SUV40270.1, ECO:0000313|Proteomes:UP000255401}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC9343 {ECO:0000313|EMBL:SUV40270.1,
RC   ECO:0000313|Proteomes:UP000255401};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR600715-1};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CR626927; CAH08291.1; -; Genomic_DNA.
DR   EMBL; UFTH01000001; SUV40270.1; -; Genomic_DNA.
DR   RefSeq; WP_010993067.1; NZ_UFTH01000001.1.
DR   PaxDb; 272559-BF9343_2510; -.
DR   KEGG; bfs:BF9343_2510; -.
DR   eggNOG; COG0472; Bacteria.
DR   HOGENOM; CLU_023982_3_0_10; -.
DR   OMA; INVQIVR; -.
DR   BioCyc; BFRA272559:G1GHZ-2729-MONOMER; -.
DR   Proteomes; UP000006731; Chromosome.
DR   Proteomes; UP000255401; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0036380; F:UDP-N-acetylglucosamine-undecaprenyl-phosphate N-acetylglucosaminephosphotransferase activity; IEA:UniProtKB-EC.
DR   CDD; cd06854; GT_WbpL_WbcO_like; 1.
DR   InterPro; IPR000715; Glycosyl_transferase_4.
DR   PANTHER; PTHR22926; PHOSPHO-N-ACETYLMURAMOYL-PENTAPEPTIDE-TRANSFERASE; 1.
DR   PANTHER; PTHR22926:SF3; UNDECAPRENYL-PHOSPHATE ALPHA-N-ACETYLGLUCOSAMINYL 1-PHOSPHATE TRANSFERASE; 1.
DR   Pfam; PF00953; Glycos_transf_4; 1.
PE   4: Predicted;
KW   Magnesium {ECO:0000256|PIRSR:PIRSR600715-1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR600715-1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SUV40270.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        39..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        63..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        89..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        112..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        141..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        165..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        188..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        216..238
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        259..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        288..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   BINDING         130
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT   BINDING         191
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ   SEQUENCE   317 AA;  36585 MW;  D07A27EEFD430918 CRC64;
     MYYLIILVLL FLAEFFYFRI ADKCNIIDKP NERSSHTRIT LRGGGIIFYL GALAYFLTNQ
     FEYPWFMLAL TLITFISFVD DIRSTSQGLR LVFHFTAMAL MFYQWGLFSL PWWTILIALI
     VCTGIINAYN FMDGINGITG GYSWVVLLAL AFINVQIVRF VEEDLIYTML CAVLVFNFFN
     FRKKAKCFAG DVGSVSIAFV ILFLIGKLII RTENFSWIVL LVVYGVDSVL TIIHRLMLHE
     NIGLPHRKHL YQLMANELEI PHVVVSLIYM TSQAIIIVGY LLTPGWGYCY LLGTIVILSM
     VYILFMKKYF HLHPAMK
//
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