ID F9HJ38_9STRE Unreviewed; 386 AA.
AC F9HJ38;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Glycosyltransferase, group 4 family {ECO:0000313|EMBL:EGP66842.1};
DE EC=2.7.8.- {ECO:0000313|EMBL:EGP66842.1};
GN ORFNames=HMPREF9182_0922 {ECO:0000313|EMBL:EGP66842.1};
OS Streptococcus sp. oral taxon 056 str. F0418.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=904294 {ECO:0000313|EMBL:EGP66842.1, ECO:0000313|Proteomes:UP000004514};
RN [1] {ECO:0000313|Proteomes:UP000004514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0418 {ECO:0000313|Proteomes:UP000004514};
RA Durkin A.S., Kim M., Radune D., Hostetler J., Torralba M., Gillis M.,
RA Methe B., Sutton G., Nelson K.E.;
RT "Complete sequence of Bifidobacterium breves ACS-071-V-Sch8b.";
RL Submitted (MAY-2011) 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:EGP66842.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AFQU01000001; EGP66842.1; -; Genomic_DNA.
DR RefSeq; WP_009754438.1; NZ_AFQU01000001.1.
DR AlphaFoldDB; F9HJ38; -.
DR eggNOG; COG0472; Bacteria.
DR Proteomes; UP000004514; 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 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:UP000004514};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EGP66842.1};
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..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 51..73
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 85..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 114..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 144..163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 175..194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 200..217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 224..245
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 251..275
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 296..324
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 330..350
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 386 AA; 42426 MW; AF224B7DFF38427C CRC64;
MVTFPLKFII VLLATFFIGI FLTPLVRLLA FKIDAVDYPN ARRINKKPMP SAGGLAVVSA
FSIATLIFMP MIVQVSLHGK TYFEYVWPVV VGGGAIALTG LIDDVKELAP LPKLIGMIIA
ASLIWFLTDF HLSDFKFPFG GPHLFFPPWL SFILTIIWIV SITNAVNLMD GLDGLVSGVS
IISLLTMGIV SYFFLPDHNL FLTLTIFVLV AAIAGFFPYN YHPAIIYGGD TGALFIGFMI
SVLSLQGLKN ATAVAVVTPM IILGVPIADT FLAIVRRKLS GKKIYQPDRG HLHHRLLSLG
LTHRGTVLVI YGISLIFATI SLLLNISSRV GGVLLVIGLL FGVELLAELI EVLGPNRTPL
LNLLRFIGNS SYREEVRQRW KNKKHK
//