ID   C1CUS8_DEIDV            Unreviewed;       377 AA.
AC   C1CUS8;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=Putative MurG (UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase) (Cell envelope biogenesis) {ECO:0000313|EMBL:ACO45945.1};
GN   OrderedLocusNames=Deide_10540 {ECO:0000313|EMBL:ACO45945.1};
OS   Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=546414 {ECO:0000313|EMBL:ACO45945.1, ECO:0000313|Proteomes:UP000002208};
RN   [1] {ECO:0000313|EMBL:ACO45945.1, ECO:0000313|Proteomes:UP000002208}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115
RC   {ECO:0000313|Proteomes:UP000002208};
RX   PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA   de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA   Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA   Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT   "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT   bacterium Deinococcus deserti.";
RL   PLoS Genet. 5:E1000434-E1000434(2009).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC       {ECO:0000256|ARBA:ARBA00006962}.
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DR   EMBL; CP001114; ACO45945.1; -; Genomic_DNA.
DR   RefSeq; WP_012693068.1; NC_012526.1.
DR   AlphaFoldDB; C1CUS8; -.
DR   STRING; 546414.Deide_10540; -.
DR   CAZy; GT28; Glycosyltransferase Family 28.
DR   PaxDb; 546414-Deide_10540; -.
DR   KEGG; ddr:Deide_10540; -.
DR   eggNOG; COG0707; Bacteria.
DR   HOGENOM; CLU_028367_0_1_0; -.
DR   OrthoDB; 9815663at2; -.
DR   Proteomes; UP000002208; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016758; F:hexosyltransferase activity; IEA:InterPro.
DR   GO; GO:0009247; P:glycolipid biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
DR   InterPro; IPR009695; Diacylglyc_glucosyltr_N.
DR   InterPro; IPR007235; Glyco_trans_28_C.
DR   PANTHER; PTHR43025; MONOGALACTOSYLDIACYLGLYCEROL SYNTHASE; 1.
DR   PANTHER; PTHR43025:SF3; MONOGALACTOSYLDIACYLGLYCEROL SYNTHASE 1, CHLOROPLASTIC; 1.
DR   Pfam; PF04101; Glyco_tran_28_C; 1.
DR   Pfam; PF06925; MGDG_synth; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002208};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACO45945.1}.
FT   DOMAIN          23..188
FT                   /note="Diacylglycerol glucosyltransferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06925"
FT   DOMAIN          217..365
FT                   /note="Glycosyl transferase family 28 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04101"
SQ   SEQUENCE   377 AA;  41553 MW;  654E8314CD73783B CRC64;
     MKKSSQQGPL RALFVSASIG SGHHQAQMAV QQALEARGVP LETRQGDAVA YLGPTERVWT
     VDLYAFELRY APWLYAWFYH GTDHDRPFSL IVSFCRWVGL RGMQRDLEQT LPELVVSSYW
     SSVPLADTVR RRTGLSFVQA LVVTDYRAHR HWIRPEAELT MVASEETAQQ MVERGADPAK
     IFVTGIPIHA RFRQLIGADR AALREKHGLR ADLPLLLVSG GGNGDYRALN ELLSELSNLG
     RRVQVLLLAG ARGRGVKQSG SATIHRLGHT TDFAELLAAS DLVVGKAGGL TVAEATALGV
     PMVVFGPIPG QEEHNADFLE RHGAGVWVRQ RRDLRGAVLR ALDEDERERM SQCARAVGRP
     DAADQVAEVL LRHLGRA
//