ID Q0BTH0_GRABC Unreviewed; 719 AA.
AC Q0BTH0;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 89.
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 OrderedLocusNames=GbCGDNIH1_0984 {ECO:0000313|EMBL:ABI61882.1};
OS Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Granulibacter.
OX NCBI_TaxID=391165 {ECO:0000313|EMBL:ABI61882.1, ECO:0000313|Proteomes:UP000001963};
RN [1] {ECO:0000313|EMBL:ABI61882.1, ECO:0000313|Proteomes:UP000001963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1260 / CGDNIH1 {ECO:0000313|Proteomes:UP000001963};
RX PubMed=17827295; DOI=10.1128/JB.00793-07;
RA Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E.,
RA Kupko J.J.III., Barbian K.D., Babar A., Dorward D.W., Holland S.M.;
RT "Genome sequence analysis of the emerging human pathogenic acetic acid
RT bacterium Granulibacter bethesdensis.";
RL J. Bacteriol. 189:8727-8736(2007).
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 inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_01072}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01072}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC membrane protein {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; CP000394; ABI61882.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0BTH0; -.
DR STRING; 391165.GbCGDNIH1_0984; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR KEGG; gbe:GbCGDNIH1_0984; -.
DR eggNOG; COG2943; Bacteria.
DR HOGENOM; CLU_015730_1_0_5; -.
DR UniPathway; UPA00637; -.
DR Proteomes; UP000001963; Chromosome.
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, ECO:0000256|HAMAP-
KW Rule:MF_01072}; Cell membrane {ECO:0000256|HAMAP-Rule:MF_01072};
KW Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01072,
KW ECO:0000313|EMBL:ABI61882.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01072};
KW Reference proteome {ECO:0000313|Proteomes:UP000001963};
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 49..68
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01072"
FT TRANSMEM 80..105
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01072"
FT TRANSMEM 409..430
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01072"
FT TRANSMEM 458..483
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01072"
FT TRANSMEM 495..518
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01072"
FT TRANSMEM 574..596
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01072"
FT DOMAIN 234..445
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF13632"
SQ SEQUENCE 719 AA; 78422 MW; 024BF6614593E80B CRC64;
MDAVIMSAIG SPPFLPSESP IDMPVQRLDS PATGPLAGQR PLTAPRGLAL RRLFVFLGTV
LLTIGAAYEM NRVLNASVTT TLGVVLVVLF VILFAWIALS FMSALGGFAS MLGRDGGLGL
GVHRDGPLPE LHHRTAILMP CYNESPARVT AGLQGIYESL QATGRMAAFD VFILSDTTDP
DVWIEEEQAF LALRQRVGGG ENIYYRRRAK NIERKAGNIG EWVRRWGGAY RQMLVLDADS
VMEGDTIVRM TAAMEQHDRI GLIQTLPVIV NGRTLFARMQ QFAGRVYGPL IAHGIAWWHG
SEGNYWGHNA VIRTKAFAEQ AGLPHLSGRK PFGGHVLSHD FVEAALMRRG GWAIHMLPAL
AGSYEESPPS LTDIAIRDRR WCQGNLQHAK ILPARDLHWI SRVHMAMGIG SYITAPLWLL
FLVLGILISL ESIFVRPEYF PHQGRALFPH WPSVDPVLAM YVFIGTMGLL LAPKVLGCIV
TMLNGSERRG CGGAIRLVLS MLIETVIGGL IAPIAMLIQS MGVASILAGR DSGWNAQRRD
DGSIPLRVVI QTYWQHTVFG LVLGGAAMLV SFPLFLWMTP VVVGMALAIP LVSLTGNRAA
GMALRRLGLL LIPEECNPPR ALVRAGEIYH SLADAPEMEA VIRLRTDQTL LAAHRAMLPP
PRRPRIDPVD ANILVARVKI AEADTLTHAL TSLSRAEKSA ALNDVDALDG LVSLPDRQS
//
