ID T2KQ32_FORAG Unreviewed; 382 AA.
AC T2KQ32;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=UDP-N-acetylglucosaminyl 1-phosphate transferase {ECO:0000313|EMBL:CDF80618.1};
DE EC=2.7.8.- {ECO:0000313|EMBL:CDF80618.1};
GN ORFNames=BN863_29060 {ECO:0000313|EMBL:CDF80618.1};
OS Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 /
OS M-2Alg 35-1).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Formosa.
OX NCBI_TaxID=1347342 {ECO:0000313|EMBL:CDF80618.1, ECO:0000313|Proteomes:UP000016160};
RN [1] {ECO:0000313|EMBL:CDF80618.1, ECO:0000313|Proteomes:UP000016160}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901
RC {ECO:0000313|Proteomes:UP000016160};
RX PubMed=23995932; DOI=10.1128/AEM.01937-13;
RA Mann A.J., Hahnke R.L., Huang S., Werner J., Xing P., Barbeyron T.,
RA Huettel B., Stueber K., Reinhardt R., Harder J., Gloeckner F.O.,
RA Amann R.I., Teeling H.;
RT "The genome of the alga-associated marine flavobacterium Formosa agariphila
RT KMM 3901T reveals a broad potential for degradation of algal
RT polysaccharides.";
RL Appl. Environ. Microbiol. 79:6813-6822(2013).
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; HG315671; CDF80618.1; -; Genomic_DNA.
DR RefSeq; WP_051774862.1; NZ_HG315671.1.
DR AlphaFoldDB; T2KQ32; -.
DR STRING; 1347342.BN863_29060; -.
DR PATRIC; fig|1347342.6.peg.2924; -.
DR eggNOG; COG0472; Bacteria.
DR HOGENOM; CLU_023982_1_1_10; -.
DR OrthoDB; 9783652at2; -.
DR Proteomes; UP000016160; 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 InterPro; IPR018480; PNAcMuramoyl-5peptid_Trfase_CS.
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.
DR PROSITE; PS01348; MRAY_2; 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:UP000016160};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CDF80618.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 15..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 60..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 144..165
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 172..190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 228..246
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 258..279
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 311..330
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 336..360
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 165
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 382 AA; 42400 MW; B6A0CBEECCC43ECE CRC64;
MNFITEIIEN GNGTMLLLLP FLLALITAFI AFPTIIFIAH AKQLVDVPDK RSVHSKTVPT
LGGIGIFFAV AIVLTLCGAF LDAKLLMPVV GALIILFFLG VKDDILILSP KKKMLGQIIA
ALMVILITDL RITTFSGILG IESIPYFLSI GFTLFVFILI INAYNLIDGL DGLAGSVGLL
VSLFYGFLFF NMNEMTLTVV SLALVGALIP FLYFNFSKVR KIFMGDTGSM VVGFLLAFQS
IAFININQLN PLAQFHLNAP IIVLAILFFP LLDTLRIFYV RVVILKKHPF SPDKNHIHHH
MLQLGLKHWQ VTLVISIAST SVLICTLLAQ NLSVNIQLLL VVMAGLFMFS LPFFINYSVF
NKRIKLNRLL KKINKTNLSR AK
//
