ID R2PR50_9ENTE Unreviewed; 467 AA.
AC R2PR50;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Glycosyl transferase, group 4 family protein {ECO:0000313|EMBL:EOH86997.1};
GN ORFNames=UAS_01460 {ECO:0000313|EMBL:EOH86997.1};
OS Enterococcus asini ATCC 700915.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1158606 {ECO:0000313|EMBL:EOH86997.1, ECO:0000313|Proteomes:UP000013777};
RN [1] {ECO:0000313|EMBL:EOH86997.1, ECO:0000313|Proteomes:UP000013777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700915 {ECO:0000313|EMBL:EOH86997.1,
RC ECO:0000313|Proteomes:UP000013777};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A.M., Gilmore M.S., Lebreton F., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Enterococcus asini ATCC_700915.";
RL Submitted (FEB-2013) 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:EOH86997.1}.
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DR EMBL; AJAP01000012; EOH86997.1; -; Genomic_DNA.
DR AlphaFoldDB; R2PR50; -.
DR STRING; 57732.RU94_GL000486; -.
DR PATRIC; fig|1158606.3.peg.1416; -.
DR eggNOG; COG0472; Bacteria.
DR HOGENOM; CLU_023982_2_4_9; -.
DR OrthoDB; 9783652at2; -.
DR Proteomes; UP000013777; 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 Reference proteome {ECO:0000313|Proteomes:UP000013777};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EOH86997.1};
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..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 53..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 77..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 108..133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 139..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 219..240
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 246..268
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 289..317
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 323..346
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 372..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..450
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 159
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT BINDING 223
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ SEQUENCE 467 AA; 51550 MW; 972FE9CCB7C831E3 CRC64;
MIVPYFAFTF ILQFFITLIL SLVLTPLVKV LACKIGAVDM PNARRINKKP MPSAGGLAIF
TAFSVSVLFG FREIELFKVT WPIVLGGAIV VVTGLLDDIF ELKPWQKLIG ITLAALEAFF
VAGIEMDSIS FPFFGKWELG WLSLPVTILW ILALTNAVNL IDGLDGLAAG VSIIGLTTLG
IISFFFLLPN DSLYTTIIIF TLVAAIAGFF PYNFFPASIY LGDTGALFLG YMISIVSMTG
LKNATFISIM TPMLILGVPI TDTVYAMIRR KFNKQKISSA DKMHLHHRLI SIGFTHRGAV
LTIYALALVF SFIALLMNYA STTAMILLII ATMVGLELFI EVIGLVGENR QPLITMLKFV
GNRQYRNEVL HREKADEPAD SLPEEKVHEP DELGNTKEFN NEELLQRLKE SLAANKAAVD
VKTAEKTPEQ KETTEAPESG EPEDGKKEAS TPKAPTYATR SERHKNK
//
