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Database: UniProt
Entry: A0A0Q9PKU5_9GAMM
LinkDB: A0A0Q9PKU5_9GAMM
Original site: A0A0Q9PKU5_9GAMM 
ID   A0A0Q9PKU5_9GAMM        Unreviewed;       367 AA.
AC   A0A0Q9PKU5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=UDP-phosphate N-acetylglucosaminyl-1-phosphate transferase {ECO:0000313|EMBL:KRE88901.1};
GN   ORFNames=ASG87_09770 {ECO:0000313|EMBL:KRE88901.1};
OS   Frateuria sp. Soil773.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Frateuria.
OX   NCBI_TaxID=1736407 {ECO:0000313|EMBL:KRE88901.1, ECO:0000313|Proteomes:UP000051919};
RN   [1] {ECO:0000313|Proteomes:UP000051919}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil773 {ECO:0000313|Proteomes:UP000051919};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRE88901.1, ECO:0000313|Proteomes:UP000051919}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil773 {ECO:0000313|EMBL:KRE88901.1,
RC   ECO:0000313|Proteomes:UP000051919};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KRE88901.1}.
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DR   EMBL; LMSL01000041; KRE88901.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q9PKU5; -.
DR   STRING; 1736407.ASG87_09770; -.
DR   OrthoDB; 9803238at2; -.
DR   Proteomes; UP000051919; 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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KRE88901.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        34..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        91..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        122..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        149..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        173..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        200..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        231..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        282..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        308..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   BINDING         142
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT   BINDING         204
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ   SEQUENCE   367 AA;  39229 MW;  4920963AEDF2D5D6 CRC64;
     MIAALTTAIA IAVLRRFAEP LGLVDRPNER KHHVGHVPLI GGLAIFAGVL AGAFWYGKFG
     PFAKVLLGTS AALALLGALD DRHDLSVRVR LLVQTAAILT VIATTGVYIH SLGHIFGYEL
     ELGWLGIPFT VVAVIGLLNA FNMMDGIDGL AGSLALVSIA AIMLFVGPAP IQGVLALMTL
     LAVAAVPYLI VNLGFTGRKI FMGDAGSMVV GYLLAWTLIR LSEQPQMSLS TVDVLWCVAL
     PVLDTLAVMY RRIRQGKSPF KPDRGHIHHI LMGLRLGPRS TLIALVALAS SIAFLGNVVR
     ALGVGTGLNL VAFCLFAMIY IAVVTRIWSH QQQSSSSLRT QAANDDRIHQ NLTIVRNIRP
     DASQPNG
//
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