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Database: UniProt
Entry: A0A161LIS2_9ACTN
LinkDB: A0A161LIS2_9ACTN
Original site: A0A161LIS2_9ACTN 
ID   A0A161LIS2_9ACTN        Unreviewed;       502 AA.
AC   A0A161LIS2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=UDP-phosphate alpha-N-acetylglucosaminyl 1-phosphate transferase {ECO:0000313|EMBL:GAT65417.1};
GN   ORFNames=PS9374_01050 {ECO:0000313|EMBL:GAT65417.1};
OS   Planomonospora sphaerica.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Planomonospora.
OX   NCBI_TaxID=161355 {ECO:0000313|EMBL:GAT65417.1, ECO:0000313|Proteomes:UP000077701};
RN   [1] {ECO:0000313|EMBL:GAT65417.1, ECO:0000313|Proteomes:UP000077701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 9374 {ECO:0000313|EMBL:GAT65417.1,
RC   ECO:0000313|Proteomes:UP000077701};
RA   Dohra H., Suzuki T., Inoue Y., Kodani S.;
RT   "Draft Genome Sequence of Planomonospora sphaerica JCM9374, a Rare
RT   Actinomycete.";
RL   Genome Announc. 4:e00779-16(2016).
RN   [2] {ECO:0000313|Proteomes:UP000077701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 9374 {ECO:0000313|Proteomes:UP000077701};
RA   Suzuki T., Dohra H., Kodani S.;
RT   "Planomonospora sphaerica JCM9374 whole genome shotgun sequence.";
RL   Submitted (APR-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:GAT65417.1}.
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DR   EMBL; BDCX01000002; GAT65417.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A161LIS2; -.
DR   STRING; 161355.PS9374_01050; -.
DR   Proteomes; UP000077701; 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:UP000077701};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:GAT65417.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        78..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        107..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        135..156
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..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        226..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        257..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        312..331
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        337..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          362..407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          429..502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        429..467
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         160
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT   BINDING         227
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ   SEQUENCE   502 AA;  51579 MW;  00D1CCE82091D366 CRC64;
     MALVAAAVTY LLVPGVRVFA IRIGAMPEVR DRDVHTTPTP RLGGLAMYGG LVAGLLVARS
     LPYAGGRLAD AEVADGNVVL ALILAGGLIT LTGFLDDWWG MDAFIKLAGQ IGAAGVLVAF
     GVSLPWLPLP SDMGGAYVLG STLGPVITIM IVVVMINAVN FVDGLDGLAA GIVGIAAMAT
     WTYSIILSTD NGDTTINVTA AVASVLIGVC LGFLPHNFHP AKIFMGDTGA MLIGLVLAST
     MITITPLDSS TINDFPVVLP LLIPIAILVL PLLDLIMAVI RRTSNGLSPF APDRGHLHHR
     LLDIGHSHRS SVLIMYAWTV LFAFAVVAMS VVGVPLLLFL LTVLLAIGGL ALVALPRWRS
     RRNGGGRGAH AAGRRARPDE GPAEQVARAV PAPPAAQETW TPSASAPVAF PQPLAAPVAP
     EGVPRFPAAP AVPEASPRSP AAPAAGPVPS PQPPRSPRSP AAPAVPPAAE PGDDTAVLSI
     VPELPGPSRS ATRGPAARFP NP
//
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