ID A0A3S8WT14_9ACTN Unreviewed; 442 AA.
AC A0A3S8WT14;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphate transferase {ECO:0000313|EMBL:AZM60014.1};
GN ORFNames=DLM49_10945 {ECO:0000313|EMBL:AZM60014.1};
OS Streptomyces sp. WAC 01438.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2203204 {ECO:0000313|EMBL:AZM60014.1, ECO:0000313|Proteomes:UP000271045};
RN [1] {ECO:0000313|EMBL:AZM60014.1, ECO:0000313|Proteomes:UP000271045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WAC 01438 {ECO:0000313|EMBL:AZM60014.1,
RC ECO:0000313|Proteomes:UP000271045};
RA Waglechner N., Wright G.D.;
RT "Evolution of GPA BGCs.";
RL Submitted (MAY-2018) 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; CP029601; AZM60014.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S8WT14; -.
DR OrthoDB; 9783652at2; -.
DR Proteomes; UP000271045; Chromosome.
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:UP000271045};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AZM60014.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 80..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 108..129
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 194..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 267..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 349..367
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 393..424
FT /note="Disordered"
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 226
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ SEQUENCE 442 AA; 47317 MW; C028174E12FB1A87 CRC64;
MREYLLTLCI TAAVTYLLTG PVRKFAIVAG AMPEIRARDV HREPTPRLGG IAMFFGLCAG
LLVADHLTNL NQLFEKSNEP RALLSGAALI WLIGVLDDKF EIDALIKLGG QMIAAGVMVM
QGLTILWLPI PGVGSVALTQ WQGTLLTVAL VVITINAVNF VDGLDGLAAG MVCIAAAAFF
LYAYRIWYSY GIEAAAPATL FSAILMGMCL GFLPHNMHPA RIFMGDSGSM LIGLVLAAGA
ISITGQVDPD ALQLFAGSEK EAVHQTVPVY IPLLLPLTII AVPAADLILA IVRRTWRGQS
PFAADRGHLH HRLLEIGHSH SRAVLIMYFW SALIGFGALT YSVNSASMWI VLSVVILSTL
GLILLLLPRF TPRAPRWAEA VVPPRYRRRR AAAAAPAAEA ADRAPEEAAR EERTPVAAGV
AGVNGATAVG PRARLADRSR SR
//
