ID   OPGH_XANOM              Reviewed;         645 AA.
AC   Q2NYU0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Glucans biosynthesis glucosyltransferase H {ECO:0000255|HAMAP-Rule:MF_01072};
DE            EC=2.4.1.- {ECO:0000255|HAMAP-Rule:MF_01072};
GN   Name=opgH {ECO:0000255|HAMAP-Rule:MF_01072}; OrderedLocusNames=XOO3782;
OS   Xanthomonas oryzae pv. oryzae (strain MAFF 311018).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=342109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF 311018;
RA   Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.;
RT   "Genome sequence of Xanthomonas oryzae pv. oryzae suggests contribution of
RT   large numbers of effector genes and insertion sequences to its race
RT   diversity.";
RL   Jpn. Agric. Res. Q. 39:275-287(2005).
CC   -!- FUNCTION: Involved in the biosynthesis of osmoregulated periplasmic
CC       glucans (OPGs). {ECO:0000255|HAMAP-Rule:MF_01072}.
CC   -!- PATHWAY: Glycan metabolism; osmoregulated periplasmic glucan (OPG)
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01072}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01072}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01072}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. OpgH
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01072}.
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DR   EMBL; AP008229; BAE70537.1; -; Genomic_DNA.
DR   RefSeq; WP_011260377.1; NC_007705.1.
DR   AlphaFoldDB; Q2NYU0; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   PRIDE; Q2NYU0; -.
DR   KEGG; xom:XOO3782; -.
DR   PATRIC; fig|291331.8.peg.4442; -.
DR   HOGENOM; CLU_015730_1_0_6; -.
DR   OMA; TAGLHYW; -.
DR   UniPathway; UPA00637; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016758; F:hexosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009250; P:glucan biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.550.10; -; 1.
DR   HAMAP; MF_01072; MdoH_OpgH; 1.
DR   InterPro; IPR023725; Glucans_biosynth_gluTrFase_H.
DR   InterPro; IPR001173; Glyco_trans_2-like.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF13632; Glyco_trans_2_3; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Glycosyltransferase; Membrane;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..645
FT                   /note="Glucans biosynthesis glucosyltransferase H"
FT                   /id="PRO_1000064621"
FT   TRANSMEM        64..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01072"
FT   TRANSMEM        98..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01072"
FT   TRANSMEM        423..443
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01072"
FT   TRANSMEM        465..485
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01072"
FT   TRANSMEM        504..524
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01072"
FT   TRANSMEM        559..579
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01072"
FT   TRANSMEM        580..600
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01072"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   645 AA;  70307 MW;  408DFF6FA9A424A2 CRC64;
     MDGTVTLSST PTAIPPVSAL DAGKPTLPPE APLAMPEQNL REGSLQVRHQ RTSPPGIGMR
     RFYLIGGTFA ATAVAVWVML SVLWPDGISV LEGCLLCLFT LLFAWIAMSF ASAVAGFVTV
     VARAGRKLGI DPEEPLPTLR SRTALLMPTY NEDPRRLLAG LQAIYESVAE TGQLEHFDFF
     VLSDTTREHI GRAEELVYSE LCDRVDGHGR IFYRRRADNA ARKAGNVADW VRRFGGRYPQ
     MLILDADSVM TGDTIVRLVA GMENNPDVGL IQTLPAVVNG QTLFARMQQF GGRVYGPIIA
     FGVAWWHGAE SNYWGHNAII RTHAFADHAG LPSLRGRKPF GGHVLSHDFV EAALMRRGGW
     AMHMVPYLQG SYEEGPPTLT DLLIRDRRWC QGNLQHAKVV SAKGLHWISR MHMLIGIGHY
     FTAPMWGLLM LIGIGIPLAG VGIDLAGDLP FSPARYWHGS SQGNAIWIFI CTMFVLLAPK
     LLGYIALLLN PRELRACGGA FRAAVSILLE TVLAALMAPV VMYLQSRGVF EVLAGKDSGW
     DAQVRDDGKL SWPALLRSYG GLTVFGLFMG AVAYAVSPAL AAWMGPVIVG MALSIPVVAL
     TSLRRTGMAL RRAGIFCIPE ELDPPKVLVR ASELRRAAVL EPSLI