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Database: UniProt
Entry: A0A2M9JPV0_9ACTN
LinkDB: A0A2M9JPV0_9ACTN
Original site: A0A2M9JPV0_9ACTN 
ID   A0A2M9JPV0_9ACTN        Unreviewed;       453 AA.
AC   A0A2M9JPV0;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphate transferase {ECO:0000313|EMBL:PJN08886.1};
GN   ORFNames=CG723_25680 {ECO:0000313|EMBL:PJN08886.1};
OS   Streptomyces sp. CB01635.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2020326 {ECO:0000313|EMBL:PJN08886.1, ECO:0000313|Proteomes:UP000232157};
RN   [1] {ECO:0000313|Proteomes:UP000232157}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB01635 {ECO:0000313|Proteomes:UP000232157};
RA   Pan G., Xu Z., Guo Z., Ma M., Yang D., Zhou H., Gansemans Y., Zhu X.,
RA   Zhao L.-X., Jiang Y., Cheng J., van Nieuwerburgh F., Suh J.W., Duan Y.,
RA   Shen B.;
RT   "Discovery of the Leinamycin Family of Natural Products by Mining
RT   Actinobacterial Genomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 114:0-0(2017).
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:PJN08886.1}.
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DR   EMBL; NNBL01000011; PJN08886.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2M9JPV0; -.
DR   OrthoDB; 9783652at2; -.
DR   Proteomes; UP000232157; 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:UP000232157};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PJN08886.1};
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..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        225..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        265..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          392..453
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   453 AA;  48826 MW;  F46FEE2B1775EF6A CRC64;
     MREYLLTLCI TAAVTYLLTG PVRKFAIVAG AMPEIRARDV HREPTPRLGG IAMFFGLCAG
     LLVADHLTNL SPVFEMSNEP RALLSGAALI WLIGVLDDKF EIDALIKLGG QMIAAGVMVM
     QGLTILWLPI PGVGTVSLTQ WQGTLLTVAL VVISINAVNF VDGLDGLASG MVCIAASAFF
     LYSYRLWYGY GIEAAAPATL FAAILIGMCL GFLPHNMHPA RIFMGDSGSM LIGLVLSAGA
     ISITGQVDPS LMKLNFGGTR DATHAMIPVF IPLLMPLTII AIPFADLVLA IVRRTWKGQS
     PFAADRGHLH HRLLEIGHSH SRAVLIMYFW SALFAFGAVA YSVHSTSMWI VLAIVALSFV
     GLVLLLLPRF TPRAPRWAEA FVPPRYRRRR AARASAEVPE TSPSYAAQEE AEAAEDAPEG
     EGSRTPMPAG VNGATAIGPR SRFLDRRKAH SSR
//
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