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Database: UniProt
Entry: A0A1V3SGZ7_9BURK
LinkDB: A0A1V3SGZ7_9BURK
Original site: A0A1V3SGZ7_9BURK 
ID   A0A1V3SGZ7_9BURK        Unreviewed;       664 AA.
AC   A0A1V3SGZ7;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Glucans biosynthesis glucosyltransferase H {ECO:0000256|ARBA:ARBA00020585};
GN   ORFNames=B0E41_02720 {ECO:0000313|EMBL:OOG88279.1};
OS   Hydrogenophaga sp. A37.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Hydrogenophaga.
OX   NCBI_TaxID=1945864 {ECO:0000313|EMBL:OOG88279.1, ECO:0000313|Proteomes:UP000189189};
RN   [1] {ECO:0000313|EMBL:OOG88279.1, ECO:0000313|Proteomes:UP000189189}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A37 {ECO:0000313|EMBL:OOG88279.1,
RC   ECO:0000313|Proteomes:UP000189189};
RA   Lycus P., Bothun K.L., Bergaust L., Shapleigh J.P., Bakken L.R.,
RA   Frostegard A.;
RT   "Phenotypic and genotypic richness of denitrifiers revealed by a novel
RT   isolation strategy.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Glycan metabolism; osmoregulated periplasmic glucan (OPG)
CC       biosynthesis. {ECO:0000256|ARBA:ARBA00005001}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. OpgH
CC       subfamily. {ECO:0000256|ARBA:ARBA00009337}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OOG88279.1}.
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DR   EMBL; MUNZ01000056; OOG88279.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V3SGZ7; -.
DR   STRING; 1945864.B0E41_02720; -.
DR   OrthoDB; 9775281at2; -.
DR   Proteomes; UP000189189; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR   CDD; cd04191; Glucan_BSP_MdoH; 1.
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|ARBA:ARBA00022519};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189189};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OOG88279.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        88..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        125..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        443..469
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        489..510
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        517..536
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        570..595
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        601..624
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          273..497
FT                   /note="Glycosyltransferase 2-like"
FT                   /evidence="ECO:0000259|Pfam:PF13632"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   664 AA;  72645 MW;  B635782FD991F8C7 CRC64;
     MDTPTLARVT PATSGRSRLR EERHPNAVTA PPVRRGSMVP QPWRGFWKSI GANVLSVVSA
     CLPGQAQAQT VRGPRPMAWE TAGQRRRTVF TVLTVLSTLL AASLYHRAQP DGENTWLQMS
     QLALFVLLSA WVVTGFVTAL MGFWVMLRGD RHTLTAASVR DHAMNPEART ALIMPICNED
     VATVFAGLRA TCESLIGTGH AGQFDVFVLS DSYDPAIAAA ERQAWEALRA ALAEQTGQPP
     IEVYYRLRSR RTHRKAGNVA DFCRRWGKDY RYMVVLDADS VMSGSCLVSL TQLMEANPRA
     GIIQTATQAI GHATLHARAQ QFGSRVTGQL FTLGMQFWQL GESHYWGHNA IIRVAPFMKH
     CALAPIKGKG GMSGGIMSHD FVEAALMRRA GYHVWLVSDL TGSYEQQPPD LLSELQRDRR
     WCQGNLQNSR LIAEPGIHRV HRFMFGIGAM SYLAAPLWLA FMALGTALVL SHPDPLASLH
     SVSDERLVLW GWTLCLLFLP RLLGLLAVFL KGEQKRFGGV GNLLVSAGLE SALALIQAPI
     RMVAHSLFVL VAVTGIQLDW KSPPREANGV AWRGAAAQLA PIAAVVGLML VGVAALNPDA
     LLWMLPVTLP LVLAVPFTVA TGHVELGGWM RARGALLIPE ESWSPAVLRR AWRHASRLSL
     LKLA
//
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