ID A0A157SG83_9BORD Unreviewed; 367 AA.
AC A0A157SG83;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=O-antigen biosynthesis glycosyltransferase {ECO:0000313|EMBL:SAI69458.1};
DE EC=2.7.8.33 {ECO:0000313|EMBL:SAI69458.1};
GN Name=wecA_2 {ECO:0000313|EMBL:SAI69458.1};
GN ORFNames=SAMEA3906487_01800 {ECO:0000313|EMBL:SAI69458.1};
OS Bordetella trematum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=123899 {ECO:0000313|EMBL:SAI69458.1, ECO:0000313|Proteomes:UP000076825};
RN [1] {ECO:0000313|EMBL:SAI69458.1, ECO:0000313|Proteomes:UP000076825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H044680328 {ECO:0000313|EMBL:SAI69458.1,
RC ECO:0000313|Proteomes:UP000076825};
RG Pathogen Informatics;
RL Submitted (APR-2016) 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; LT546645; SAI69458.1; -; Genomic_DNA.
DR RefSeq; WP_025513099.1; NZ_UYIW01000004.1.
DR AlphaFoldDB; A0A157SG83; -.
DR STRING; 123899.SAMEA3906487_01800; -.
DR GeneID; 56590919; -.
DR KEGG; btrm:SAMEA390648701800; -.
DR PATRIC; fig|123899.6.peg.1787; -.
DR eggNOG; COG0472; Bacteria.
DR OrthoDB; 9783652at2; -.
DR Proteomes; UP000076825; Chromosome 1.
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; cd06912; GT_MraY_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 Reference proteome {ECO:0000313|Proteomes:UP000076825};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SAI69458.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 47..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 72..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 102..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 132..153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 160..179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 185..203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 215..233
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 300..322
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 328..347
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 154
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT BINDING 214
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ SEQUENCE 367 AA; 40001 MW; ACE1DF835B2B187E CRC64;
MTWLYICVVA FMVGGLIVAS ERWHGAFTGD SDLSKPQASH TRATPRVGGL AVLAGSLAGL
LVLGPSNMTL NWLWPALFMA SLPVFVAGLL EDITKDIGAS KRLLAAFASA AIAWWLLGGV
SRVGIAPVDW VLSFWPVSLL FTVFAVGGCT HALNIVDGMN GLAGMIATLM AVSIGLVALQ
VGDVPIFMIS AALASATLGF LVWNFPFGRV FLGDGGAYFL GFMLAELAVL LVVRNPSVSP
FYALAVLFYP VFETGFSIWR RRFKRGVPVD QPDALHLHQL VFRRLVRVTF SRRSRHAVPA
LCNALASPYM WVLALIGLVP ATIWWDNAWV LCASLLVFAL VYTWLYVRLV SWRRPGWLLL
PSVLRTP
//
