ID C9KX17_9BACE Unreviewed; 378 AA.
AC C9KX17;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Glycosyltransferase, group 4 family {ECO:0000313|EMBL:EEX45393.1};
DE EC=2.7.8.- {ECO:0000313|EMBL:EEX45393.1};
GN ORFNames=BACFIN_06859 {ECO:0000313|EMBL:EEX45393.1};
OS Bacteroides finegoldii DSM 17565.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=483215 {ECO:0000313|EMBL:EEX45393.1, ECO:0000313|Proteomes:UP000003768};
RN [1] {ECO:0000313|EMBL:EEX45393.1, ECO:0000313|Proteomes:UP000003768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17565 {ECO:0000313|EMBL:EEX45393.1,
RC ECO:0000313|Proteomes:UP000003768};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2009) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEX45393.1}.
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DR EMBL; ABXI02000041; EEX45393.1; -; Genomic_DNA.
DR RefSeq; WP_007753124.1; NZ_GG688323.1.
DR AlphaFoldDB; C9KX17; -.
DR GeneID; 61622189; -.
DR eggNOG; COG0472; Bacteria.
DR HOGENOM; CLU_023982_1_1_10; -.
DR Proteomes; UP000003768; 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:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IEA:InterPro.
DR CDD; cd06853; GT_WecA_like; 1.
DR InterPro; IPR000715; Glycosyl_transferase_4.
DR InterPro; IPR018480; PNAcMuramoyl-5peptid_Trfase_CS.
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.
DR PROSITE; PS01348; MRAY_2; 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:EEX45393.1};
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..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 50..73
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 117..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 146..163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 201..219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 231..249
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 311..334
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 340..358
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 167
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT BINDING 230
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ SEQUENCE 378 AA; 42953 MW; AFA65C27E4A6B5ED CRC64;
MIIAYLAGIF LLSILLATVI IPRILFISYK KRLFDVPDSR KVHKTPIPRL GGLSFLPVIL
IALCSVTGIR YYTNHPVDML WASDLFIQYL FLIVGLTLLY LVGVADDLVG VGYRYKFVIQ
ILAALLFPLS GLWINDLGGL LGLHEIPAYI GMPLTVFLTV YITNAINLID GIDGLASGLS
CIALGLLIIV CALVGQWTHA FLAAATLGVV ITFYYYNVFS VSGRKLFMGD AGSLTLGYIL
SFLVLHFWQK TQLWDPFTMN LNMVTVSTLL IPLLDVVRVF YSRVSEGRNP FTPDKNHIHH
RLLRTGMKVR TVMITLLMLS LFFVVSNFIL SFYINTTFML LLDLAFWLTT HFIIRYFIMK
HETATGRKWY KTYRNFFW
//
