ID A0A060R922_9BACT Unreviewed; 319 AA.
AC A0A060R922;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Undecaprenyl-phosphate N-acetylglucosaminyl 1-phosphate transferase {ECO:0000313|EMBL:CDN32032.1};
DE EC=2.7.8.- {ECO:0000313|EMBL:CDN32032.1};
GN ORFNames=BN938_1955 {ECO:0000313|EMBL:CDN32032.1};
OS Mucinivorans hirudinis.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Mucinivorans.
OX NCBI_TaxID=1433126 {ECO:0000313|EMBL:CDN32032.1, ECO:0000313|Proteomes:UP000027616};
RN [1] {ECO:0000313|EMBL:CDN32032.1, ECO:0000313|Proteomes:UP000027616}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3 {ECO:0000313|Proteomes:UP000027616};
RX PubMed=25657285; DOI=10.1128/genomeA.01530-14;
RA Nelson M.C., Bomar L., Graf J.;
RT "Complete Genome Sequence of the Novel Leech Symbiont Mucinivorans
RT hirudinis M3T.";
RL Genome Announc. 3:e01530-e01514(2015).
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; HG934468; CDN32032.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060R922; -.
DR STRING; 1433126.BN938_1955; -.
DR KEGG; rbc:BN938_1955; -.
DR PATRIC; fig|1433126.3.peg.1931; -.
DR eggNOG; COG0472; Bacteria.
DR HOGENOM; CLU_023982_3_0_10; -.
DR OrthoDB; 9783652at2; -.
DR Proteomes; UP000027616; Chromosome I.
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; cd06854; GT_WbpL_WbcO_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:UP000027616};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CDN32032.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 111..128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 135..152
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 167..184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 191..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 218..240
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 261..286
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 292..308
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 129
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT BINDING 194
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ SEQUENCE 319 AA; 36589 MW; A64BA0D839CA7A55 CRC64;
MITLLIILAL LVMTILVYFR IADHYNIIDK PNHRSSHTNI TIRGGGIIFY FGLLFFWIFY
GFHYPWLLMG ASFIAAISFV DDIHPLSPKL RLLVQFLTIG LLLYQCGVWQ WYWFIPALVL
VAGVINIYNF MDGINGITSC YSLVVLAGLW YVDNAKYGQG IDFVDNHIFY TMALSLIVFC
FFNFRKRAKC FAGDVGSVTI AYVLSFLLVN LIVTTGNFAY IIFLAVYGVD AIITIVHRVI
RKEKLTEAHR SHTYQIMANE LKIPHLVVST IYALLQILVT VGLFVFAQYQ CIYFVVAIVL
LVGINLWLRH KYFYLHKAS
//
