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Database: UniProt
Entry: A0A1Q6WPQ0_9GAMM
LinkDB: A0A1Q6WPQ0_9GAMM
Original site: A0A1Q6WPQ0_9GAMM 
ID   A0A1Q6WPQ0_9GAMM        Unreviewed;       447 AA.
AC   A0A1Q6WPQ0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=N-acetylglucosaminyltransferase {ECO:0000313|EMBL:OLB15182.1};
GN   ORFNames=AUH10_02365 {ECO:0000313|EMBL:OLB15182.1};
OS   Gammaproteobacteria bacterium 13_2_20CM_66_19.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria.
OX   NCBI_TaxID=1805166 {ECO:0000313|EMBL:OLB15182.1, ECO:0000313|Proteomes:UP000186999};
RN   [1] {ECO:0000313|EMBL:OLB15182.1, ECO:0000313|Proteomes:UP000186999}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27843720;
RA   Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA   Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA   Banfield J.F.;
RT   "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT   heterotrophy are prevalent below the grass root zone.";
RL   PeerJ 4:E2687-E2687(2016).
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family.
CC       {ECO:0000256|ARBA:ARBA00006739}.
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:OLB15182.1}.
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DR   EMBL; MNCZ01000021; OLB15182.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q6WPQ0; -.
DR   STRING; 1805166.AUH10_02365; -.
DR   Proteomes; UP000186999; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   CDD; cd06423; CESA_like; 1.
DR   InterPro; IPR001173; Glyco_trans_2-like.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR43630; POLY-BETA-1,6-N-ACETYL-D-GLUCOSAMINE SYNTHASE; 1.
DR   PANTHER; PTHR43630:SF1; POLY-BETA-1,6-N-ACETYL-D-GLUCOSAMINE SYNTHASE; 1.
DR   Pfam; PF13632; Glyco_trans_2_3; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000313|EMBL:OLB15182.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transferase {ECO:0000313|EMBL:OLB15182.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        33..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        330..357
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        363..388
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        400..420
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          162..382
FT                   /note="Glycosyltransferase 2-like"
FT                   /evidence="ECO:0000259|Pfam:PF13632"
SQ   SEQUENCE   447 AA;  50876 MW;  FBDF9D5BF2FA0A53 CRC64;
     MDAMLTLTGA WLTLLQLLEA VWRSDWIVVA LKFFPFVLMF ELPIQALVML GGVRRYIEGR
     RTARYPLAYH PSVSCVITCY SEGADVQKTV RSLTEQLYAG PIEMLAVVDG AVQNRATLAA
     LRALGPYVNA RKLRRLEIVP KLQRGGRVSS LNQGLALACG EIVMALDGDT SFDNDMVRHA
     VRHFADQNVV AVAGNLRARN ARSSFVTRLQ ALEYALSIHL SRAGLDAFNL VNNISGAFGV
     FRRDFLRRIG GWDSGTAEDL DLTLRIKKYF ARHPDLRIRF EPRAMGHTDV PETFRGFLKQ
     RLRWDGDLSY LYLRKYGHHL RPGLLGLRNF LALVWTGLLF QLALPFVLLT YTIYMLFVYP
     AAVTLGVLAF VYLFYTLLAA LMYAEYWLLY SERRRQDLKL AWLLLAFPGF TFLTRCWNAI
     ATLYELLGNS HLESSMAPSW VLRRTKF
//
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