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Database: UniProt
Entry: A0A1G6VCG9_9BURK
LinkDB: A0A1G6VCG9_9BURK
Original site: A0A1G6VCG9_9BURK 
ID   A0A1G6VCG9_9BURK        Unreviewed;       867 AA.
AC   A0A1G6VCG9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Glucans biosynthesis glucosyltransferase H {ECO:0000256|ARBA:ARBA00020585, ECO:0000256|HAMAP-Rule:MF_01072};
DE            EC=2.4.1.- {ECO:0000256|HAMAP-Rule:MF_01072};
GN   Name=opgH {ECO:0000256|HAMAP-Rule:MF_01072};
GN   ORFNames=SAMN05216345_11084 {ECO:0000313|EMBL:SDD51164.1};
OS   Cupriavidus sp. YR651.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=1855315 {ECO:0000313|EMBL:SDD51164.1, ECO:0000313|Proteomes:UP000198719};
RN   [1] {ECO:0000313|Proteomes:UP000198719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YR651 {ECO:0000313|Proteomes:UP000198719};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the biosynthesis of osmoregulated periplasmic
CC       glucans (OPGs). {ECO:0000256|HAMAP-Rule:MF_01072}.
CC   -!- PATHWAY: Glycan metabolism; osmoregulated periplasmic glucan (OPG)
CC       biosynthesis. {ECO:0000256|ARBA:ARBA00005001, ECO:0000256|HAMAP-
CC       Rule:MF_01072}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01072};
CC       Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01072}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. OpgH
CC       subfamily. {ECO:0000256|ARBA:ARBA00009337, ECO:0000256|HAMAP-
CC       Rule:MF_01072}.
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DR   EMBL; FMYZ01000010; SDD51164.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6VCG9; -.
DR   STRING; 1855315.SAMN05216345_11084; -.
DR   OrthoDB; 9775281at2; -.
DR   UniPathway; UPA00637; -.
DR   Proteomes; UP000198719; Unassembled WGS sequence.
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   CDD; cd04191; Glucan_BSP_MdoH; 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   PANTHER; PTHR43867; CELLULOSE SYNTHASE CATALYTIC SUBUNIT A [UDP-FORMING]; 1.
DR   PANTHER; PTHR43867:SF5; GLUCANS BIOSYNTHESIS GLUCOSYLTRANSFERASE H; 1.
DR   Pfam; PF13632; Glyco_trans_2_3; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01072};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01072};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01072};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198719};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01072};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_01072};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_01072}.
FT   TRANSMEM        186..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01072"
FT   TRANSMEM        219..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01072"
FT   TRANSMEM        537..564
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01072"
FT   TRANSMEM        592..615
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01072"
FT   TRANSMEM        627..648
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01072"
FT   TRANSMEM        704..726
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01072"
FT   DOMAIN          367..560
FT                   /note="Glycosyltransferase 2-like"
FT                   /evidence="ECO:0000259|Pfam:PF13632"
FT   REGION          67..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   867 AA;  96641 MW;  5515A2E9C09FA3B0 CRC64;
     MELHLTPRLK QRPAQAAACE RYVDRLPASP ELRSELLADT PMPPVASVPT DGIEAPSAMI
     QLQTRLAGRD PKDQEGIDFS QRSTPGGATY ASVSRRFSMA YGNPQTDGEP LLQRREDGTV
     RVDTGPEPAR ESMVPRQWPP HVVTGGLRNL WRKMTGRPPI PETWDTLHDG PDAEGKWHPA
     GSHRRWFLLA LVIGQTAVAT YFMAKVLPYH GADPLEIAIL ALFAILFSWV SAGFWTAMMG
     FLVLAKGGDR HLISRSAAPD AAIDPAARTA VIMPICNEDV TRVFAGLRAT YESLERTGEL
     AHFDFFVLSD SGNPDLRTAE HDAWMEICRA VGGFGRIFYR WRRHRVKRKT GNVADFCRRW
     GSKYRYMIVL DADSVMSGDC LATLTRLMEA NPGAGIIQTA PLAVGRDTLY ARVQQFSTRV
     YGPLFTAGLH YWQLGESHYW GHNAIIRIKP FMEHCALAPL PGKGPLSGEI LSHDFVEAAL
     MRRAGWGVWI AYDLPGSFEE LPPNLLDEVK RDRRWCQGNL MNFRLWMKQG FHMVHRAVFL
     TGIMAYLSAP LWLLFLLLST AALAKHALVP PEYFTQPYQL FPTWPEWHPE KALALFSATA
     TLLFLPKLLS VLLLMKDARQ YGGVVRLVIS MLLEMAMSAL LAPTRMLFHT KFVIAAYSGW
     GISWKSPPRE DAETTWGEAF RRHGWHTLLG LVWGGGVYWL SPGFIWWLLP IVGSLALSIP
     LSVMLSRVSL GRAARRAGLF MIPEETIVPR EIVETQQHVE GAQDVPGFVD AVVDPVTNAL
     MCATATARKI QPEPARLQHA SLVQHALTHG PQSLSAAQKH VLLGDPFALS RLHELVWGSP
     LADAAWKETR VLMRRAANVL PLRPRAA
//
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