ID   OPGH_CUPPJ              Reviewed;         861 AA.
AC   Q46TZ4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=Reut_B4034;
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS   (strain JMP 134)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMP134 / LMG 1197;
RX   PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA   Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA   Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA   Kyrpides N.C.;
RT   "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT   versatile pollutant degrader.";
RL   PLoS ONE 5:E9729-E9729(2010).
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; CP000091; AAZ63390.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q46TZ4; -.
DR   STRING; 264198.Reut_B4034; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   EnsemblBacteria; AAZ63390; AAZ63390; Reut_B4034.
DR   KEGG; reu:Reut_B4034; -.
DR   eggNOG; COG2943; Bacteria.
DR   HOGENOM; CLU_015730_0_0_4; -.
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; PF00535; Glycos_transf_2; 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..861
FT                   /note="Glucans biosynthesis glucosyltransferase H"
FT                   /id="PRO_1000064614"
FT   TRANSMEM        181..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01072"
FT   TRANSMEM        208..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01072"
FT   TRANSMEM        532..552
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01072"
FT   TRANSMEM        589..609
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01072"
FT   TRANSMEM        616..636
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01072"
FT   TRANSMEM        698..718
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01072"
FT   REGION          65..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          101..129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   861 AA;  95873 MW;  AE6647C28A8FD21F CRC64;
     MELHLTPRLK QRPAQAAACE RYVDRLPVSS ELRSELLADP SMPASAGISI DPRDAQAAIE
     QLQSRLSARE PAKGETPEPG GSTYGSVGRR FSLAYGNPQV AGEPLLKRRP DGTVHVDTGP
     EPQRSSMVPR QWPPHIVTGW VRNTWRRMLG RPPVPETWDT LHDGPDAEGK WHPAGSHRRW
     FLLGLVVAQT TLATYFMTKV LPYHGADLLE IAILVLFAVL FSWVSAGFWT AMMGFLVLAK
     GGDRHLISRS AAPDAPLAPD ARTAVIMPIC NEDVTRVFAG LRATYESLGR TGHLANFDFI
     VLSDSGNPDL RTAEVDAWME VCRAVGGFGR IFYRWRRHRV KRKTGNVADF CRRWGSKYRY
     MVVLDADSVM SGDCLATLVR LMEANPGAGI IQTSPLAVGR ETLYARVQQF ATRVYGPLFT
     AGLHYWQLGE SHYWGHNAII RVKPFMEHCA LAPLPGRGPL SGEILSHDFV EAALMRRAGW
     GVWIAYDLHG SYEELPPNLL DEVKRDRRWC QGNLMNFRLW LKQGFHMVHR AVFLTGIMAY
     LSAPLWFLFL LLSTAMLARH ALVPPEYFTQ PYQLFPTWPE WHPEKALALF SATATLLFLP
     KVASILLLVR QARQYGGLPR LVMSMLIEVV LSALLAPTRM LFHTKFVIAA YSGWGISWKS
     PPREDAETTW GEAVRRHGSH TLLGLAWGAL VYWLNPSFVL WLLPIVGSLA LSIPLSVMLS
     RVSFGRASRE AGLFMIPEEA LPPREIVETQ QHVEQATETP NFVDAVVDPV TNALMCATAS
     ARVVQPASAK ERHAALVQHA LTGGPRALTA SQRHILLGDP FALSKLHELV WGSPLADAGW
     KNIRLLVRRA PNVLPLRPRV A