OPGH_XYLFT
ID OPGH_XYLFT Reviewed; 638 AA.
AC Q87CC5;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 91.
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}; Synonyms=mdoH;
GN OrderedLocusNames=PD_1156;
OS Xylella fastidiosa (strain Temecula1 / ATCC 700964).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=183190;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Temecula1 / ATCC 700964;
RX PubMed=12533478; DOI=10.1128/jb.185.3.1018-1026.2003;
RA Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y.,
RA Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., Takita M.A.,
RA Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., Goldman M.H.S.,
RA Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M., Carrer H.,
RA Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L.,
RA Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., Marino C.L.,
RA Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., Baia G.S.,
RA Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., da Cunha A.F.,
RA Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., Leoni S.G.,
RA Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., de Souza A.A.,
RA Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., Civerolo E.L.,
RA Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., Kitajima J.P.;
RT "Comparative analyses of the complete genome sequences of Pierce's disease
RT and citrus variegated chlorosis strains of Xylella fastidiosa.";
RL J. Bacteriol. 185:1018-1026(2003).
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; AE009442; AAO29011.1; -; Genomic_DNA.
DR AlphaFoldDB; Q87CC5; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR EnsemblBacteria; AAO29011; AAO29011; PD_1156.
DR KEGG; xft:PD_1156; -.
DR HOGENOM; CLU_015730_1_0_6; -.
DR OMA; TAGLHYW; -.
DR UniPathway; UPA00637; -.
DR Proteomes; UP000002516; Chromosome.
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..638
FT /note="Glucans biosynthesis glucosyltransferase H"
FT /id="PRO_0000210371"
FT TRANSMEM 57..79
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01072"
FT TRANSMEM 94..116
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01072"
FT TRANSMEM 415..437
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01072"
FT TRANSMEM 464..486
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01072"
FT TRANSMEM 499..521
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01072"
FT TRANSMEM 578..600
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01072"
SQ SEQUENCE 638 AA; 70395 MW; A3042127015D365D CRC64;
MQALMEMQIG ASEVVQVLDT GCAVLPPESP LPMPEQSLRK GRLHVPRQRT APLGIGLRRF
YLIGGTMSMS LIATWVMLAV MWPGGINVLE GCLLVLFMFL FAWVTMSFAS ALAGFFCMVF
GGGRKLGIDP QMPLPDLHTY TALLVPTYQE DPCRLLAGLQ AIYESLSETG QLEHFEFFVL
SDSRREEFGL AEEREYAALC ERLGAHGRIF YRRRADNTGR KAGNIADWVR RFGGAYQQML
ILDADSVMTG DTVVRLVAAM ESNPDVGLIQ SLPVVVGGRT LFARMQQFGA CVYGPIIAYG
VAWWHGAESN YWGHNAVIRT KAFADHAGLP ALPGRKPFGG HVLSHDFVEA ALIRRGGWAT
HMVPYLQGSY EEGPPTLTDL LIRDRRWCQG NLQHAKIVTA AGLHWISRMH MLIGIGHYFT
APMWGLLMLV GIAIPLVGDG IDLTAGMHFS PAHYWHGRTD GDVLWIFTFT MFVLLAPKLL
AYFALLFKPY ERRACGGALR VLLSILLESI LAALMAPIVM YLQSRGVFEV LAGKDSGWDA
QQRDDGKLSW SVLLRSYGGL SVLGVLIGAL AYTVSPPLAM WMSPVVLGMA FSVPVVALTS
HRLVGAVLRR WGIFLIPEET APSKVLIRVA ELRRARQP