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Database: UniProt
Entry: A0A1S2LMY8_9BACI
LinkDB: A0A1S2LMY8_9BACI
Original site: A0A1S2LMY8_9BACI 
ID   A0A1S2LMY8_9BACI        Unreviewed;       363 AA.
AC   A0A1S2LMY8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphate transferase {ECO:0000313|EMBL:OIJ13047.1};
GN   ORFNames=BKP37_11045 {ECO:0000313|EMBL:OIJ13047.1};
OS   Anaerobacillus alkalilacustris.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anaerobacillus.
OX   NCBI_TaxID=393763 {ECO:0000313|EMBL:OIJ13047.1, ECO:0000313|Proteomes:UP000179524};
RN   [1] {ECO:0000313|EMBL:OIJ13047.1, ECO:0000313|Proteomes:UP000179524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18345 {ECO:0000313|EMBL:OIJ13047.1,
RC   ECO:0000313|Proteomes:UP000179524};
RA   Bassil N.M., Lloyd J.R.;
RT   "Draft genome sequences of four alkaliphilic bacteria belonging to the
RT   Anaerobacillus genus.";
RL   Submitted (OCT-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}.
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:OIJ13047.1}.
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DR   EMBL; MLQR01000029; OIJ13047.1; -; Genomic_DNA.
DR   RefSeq; WP_071309644.1; NZ_MLQR01000029.1.
DR   AlphaFoldDB; A0A1S2LMY8; -.
DR   OrthoDB; 9783652at2; -.
DR   Proteomes; UP000179524; 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:OIJ13047.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        5..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        45..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        68..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        97..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        123..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        154..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        178..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        208..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        231..252
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        283..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        307..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   BINDING         147
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT   BINDING         207
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ   SEQUENCE   363 AA;  40241 MW;  84331009784D210D CRC64;
     MIFLISFICF LASILVTPVV IKLAKLINAV DLPNGRKVHR KATPLLGGLS IYLGFIIGIL
     WFHPENHFIW PIIIGATVIV LTGMIDDMIQ LKPRWKFVGQ SIAAISVISG GLFIEFINLP
     FETIWELGFL GIPLTYLWIV AITNAINLID GLDGLAAGVS IIVLTAISII SIMAGNFFIS
     LLTLILISST LGFLFFNFHP AKIFMGDTGS LFLGFMISVI SILGFKSITL FTLIVPIILL
     AVPLSDSIFA IIRRIVHKKS IVTPDKSHLH HCLMKIGFTH KGTVLLIYGL SAFFAVCAML
     LTKSTFMGGF IITLIIIITI ELTVEIVGLI NGNYRPMLNF ISRFKRIGKS QYFSKQNKDW
     FKH
//
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