ID A0A1J0WLM8_9RHOB Unreviewed; 628 AA.
AC A0A1J0WLM8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Glucans biosynthesis glucosyltransferase H {ECO:0000256|ARBA:ARBA00020585};
GN ORFNames=BOO69_03585 {ECO:0000313|EMBL:APE45273.1};
OS Sulfitobacter alexandrii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=1917485 {ECO:0000313|EMBL:APE45273.1, ECO:0000313|Proteomes:UP000181897};
RN [1] {ECO:0000313|EMBL:APE45273.1, ECO:0000313|Proteomes:UP000181897}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM1-D1 {ECO:0000313|EMBL:APE45273.1,
RC ECO:0000313|Proteomes:UP000181897};
RA Yang Q., Zhang X., Tian X.;
RT "Complete genome sequence of Sulfitobacter sp. AM1-D1, a toxic bacteria
RT associated with marine dinoflagellate Alexandrium minutum in East China
RT Sea.";
RL Submitted (NOV-2016) 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}.
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DR EMBL; CP018076; APE45273.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J0WLM8; -.
DR STRING; 1917485.BOO69_03585; -.
DR KEGG; suam:BOO69_03585; -.
DR OrthoDB; 9775281at2; -.
DR Proteomes; UP000181897; Chromosome.
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 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:APE45273.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 41..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 78..104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 395..414
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 446..470
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 482..503
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 544..573
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 221..410
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF13632"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 628 AA; 68988 MW; 133B74F3127B2475 CRC64;
MTPETPPSAT TMPERAPLSM QPQDFARAPA RRVTASQPRS LGWRIAVFGP ALIGTALLMY
GLYGWLAGSG MTWLEWALLS MIGATFVWVT LSVSTVGVAI AGLLARQNAD ERAPGAVTPL
DVALLVPIYN EVPWDVFGNA AAMLADLHRR KGKHRYALFI LSDTRDDDIA AQERRAFERL
RADAPAGMSV HYRRRTANTD KKVGNLMDWI TGWGAAYEGM IVLDADSLMT GRAIDRLASE
LSADPDAGLI QTFPMLIGAE TLFARVQQFS NIAYGWLLAE GLALWARNEG NYWGHNAIIR
TRAFAESAGL PHLTSGGRDD LILSHDFVEA GLLRRAGWRV RFLPRVTGSF EETPGTLIDY
VVRDRRWCRG NLQHLRLLGT AGLHPVSRFH LFHGAVAYLL SPAWFILLVF WSLLGKDSDT
NVVRYFNQAN PYFPDWPPAM SHIDSAVFLV IMYAMLLTPK LAGAGIIAFS PKAVAVYGGK
RAFVTSFLVE VALSVAYAPI MMIQQTKAVM NAVLTRTEAW APQQRGGKGY PLRTLIGFHW
LETLLGILLL SGLAAGLISL WLVPIVFSLV MAVPLSALSS INLSNLASRG LRMESPNTLR
EPAIVGQARR ARLQIRTHLL APEKIAAE
//
