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OPGH_XANEU
ID   OPGH_XANEU              Reviewed;         643 AA.
AC   Q83Z42;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Glucans biosynthesis glucosyltransferase H;
DE            EC=2.4.1.-;
GN   Name=opgH;
OS   Xanthomonas euvesicatoria.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=456327;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Isolate 91-118;
RA   Minsavage G.V., Jones J.B., Stall R.E., Mudgett M.B.;
RT   "Role of the Xanthomonas campestris pv. vesicatoria OpgH in host-parasite
RT   interactions.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the biosynthesis of osmoregulated periplasmic
CC       glucans (OPGs). {ECO:0000250}.
CC   -!- PATHWAY: Glycan metabolism; osmoregulated periplasmic glucan (OPG)
CC       biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. OpgH
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AY248747; AAP13869.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q83Z42; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
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..643
FT                   /note="Glucans biosynthesis glucosyltransferase H"
FT                   /id="PRO_0000210369"
FT   TRANSMEM        62..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        99..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        417..439
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        466..488
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        554..576
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        581..603
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   643 AA;  70008 MW;  8E1E08BE9C40F214 CRC64;
     MDGTVTPSPT TTAMPPVSAL DAGTPTLPPE APLAMPEQNL REGSLQVRHQ RTSPPGIGVR
     RFYLIGGTFA TTAIAVWVML SVLWPDGISV LEGCLLGLFV LLFAWIAMSF ASAVAGFVTV
     VARAGRKLGI DPEQPLPTLR SRTALLMPTY NEDPRRLLAG LQAIYESVAE TGQLEHFDFF
     VLSDTTREHI GRAEELVYNE LCDRVDGHGR IFYRRRADNA ARKAGNVADW VRRFGGSYPQ
     MLILDADSVM TGDTIVRLVA GMENNPDVGL IQTLPAVVNG QTLFARMQQF GGRVYGPIIA
     FGVALLHGAE SNYWGHNAII RTQAFADHAG LPSLRGRKPF GGHVLSHDFV EAALMRRGGW
     AMHMVPYLQG SYEEGPPTLT DLLIRDRRWC QGNLQHAKVV SAKGLHWISR MHMLIGIGHY
     FTAPMWGLLM LIGIGIPLAG GGIDLAGDLP FSPARYWHGS SQGNAIWIFI CTMFVLLAPK
     LLGYIALLLN PRELRACGGA FRAAVSILLE TVLAALMAPV VMYLQSRGVF EVLAGKDSGW
     DAQVRDDGKL SWPALFRSYG GLTVFGLFMG AVAYAVSPAL AAWMGPVIVG MALSIPVVAL
     TSLRRTGMAL RRAGIFCIPK NSTRPRCWCV PPSCAAPLRW NRR
 
 
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