ID A0A1W6YS86_9BORD Unreviewed; 844 AA.
AC A0A1W6YS86;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=CAL12_26065 {ECO:0000313|EMBL:ARP83937.1};
OS Bordetella genomosp. 8.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1416806 {ECO:0000313|EMBL:ARP83937.1, ECO:0000313|Proteomes:UP000194151};
RN [1] {ECO:0000313|EMBL:ARP83937.1, ECO:0000313|Proteomes:UP000194151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU19157 {ECO:0000313|EMBL:ARP83937.1,
RC ECO:0000313|Proteomes:UP000194151};
RA Spilker T., LiPuma J.;
RT "Complete and WGS of Bordetella genogroups.";
RL Submitted (MAY-2017) 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; CP021108; ARP83937.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W6YS86; -.
DR STRING; 1416806.CAL12_26065; -.
DR OrthoDB; 9775281at2; -.
DR UniPathway; UPA00637; -.
DR Proteomes; UP000194151; 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; PF00535; Glycos_transf_2; 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 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 156..173
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01072"
FT TRANSMEM 189..216
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01072"
FT TRANSMEM 507..535
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01072"
FT TRANSMEM 562..586
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01072"
FT TRANSMEM 598..619
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01072"
FT TRANSMEM 675..695
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01072"
FT DOMAIN 241..421
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF00535"
FT REGION 822..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 844 AA; 94834 MW; AF8720909AF29610 CRC64;
MNLKPNNSLP GADAVEDYLE RLALPPETRA ATQERAATAA EDGRSALDAV HRSLAGDDTL
GGDPVLASGM ERLRVAEGDD PDIAGMARQL PDSGVCLASA PPLNRTAMSP EPWVPNPMAR
FWRRLRGQGP HMSDDYMATA PRMDPRWRQA GSRRRMCLVT MVALQTVIAT YYMKGVLPYQ
GKQILEVGIL FLFALLFCWV SAGFWTAMMG FLQLLIGRDR YSISARSTED APIDRSARTA
IVMPICNEDV SRVFAGLRAT YESLAQTDAM DHFDIFVLSD SYKADICVAE QRAWVDLCKA
VKGFGRIFYR RRRRRVKRKS GNIDDFCRRW GGNYRYMIVL DADSVMTGEC LKRLVQLMEA
SPDAGIIQSA PQASGMDSLY ARIQQFATRV YGPLFTAGMH YWQLGESHYW GHNAIIRLAP
FMRHCVLAPL PGKGAFAGAI LSHDFVEAAL MRRAGWGVWI AYDLPGSYEE LPPNLLEELQ
RDQRWCHGNL MNFRLFFIQG FHPVHRAVFL TGVMSYLSAP LWFLFLLLST ALLAVHTLTE
PQYFVEPRQL FPIWPQWHPD KAIALFSTTA VLLFLPKVLG VLLVWARGAR LFGGRQKALS
SMLMEVLFSM LLAPVRMLFH TRFVVAAFLG LSAKWISPAR DNDQTTWGDA FKRHGSQTLL
GICWAGLVAW LNPVFLFWMA PILAALLLII PLSVYSSRVD LGRRAYLARF FRIPEETQPP
TELQATRRYT AQNRSGQHVP DFEDAVVDPG VNALACAMAT ARHKPNALNE AFRRQQVEHV
MEYGVDALSE PQKIKLLDDP VVLSHVHEAI WRSREEHAVQ LRERTAPRDT PAATLESVET
APAL
//
