ID J6IXD0_9RHOB Unreviewed; 742 AA.
AC J6IXD0;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=A33M_0760 {ECO:0000313|EMBL:EJW09945.1};
OS Rhodovulum sp. PH10.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodovulum.
OX NCBI_TaxID=1187851 {ECO:0000313|EMBL:EJW09945.1, ECO:0000313|Proteomes:UP000002930};
RN [1] {ECO:0000313|EMBL:EJW09945.1, ECO:0000313|Proteomes:UP000002930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PH10 {ECO:0000313|EMBL:EJW09945.1,
RC ECO:0000313|Proteomes:UP000002930};
RX PubMed=23105089; DOI=10.1128/JB.01695-12;
RA Khatri I., Nupur, Korpole S., Subramanian S., Pinnaka A.K.;
RT "Draft Genome Sequence of Rhodovulum sp. Strain PH10, a Phototrophic
RT Alphaproteobacterium Isolated from a Soil Sample of Mangrove of Namkhana,
RT India.";
RL J. Bacteriol. 194:6363-6363(2012).
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}.
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:EJW09945.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AKZI01000124; EJW09945.1; -; Genomic_DNA.
DR RefSeq; WP_008390314.1; NZ_AKZI01000124.1.
DR AlphaFoldDB; J6IXD0; -.
DR STRING; 1187851.A33M_0760; -.
DR PATRIC; fig|1187851.3.peg.3843; -.
DR eggNOG; COG2943; Bacteria.
DR OrthoDB; 9775281at2; -.
DR UniPathway; UPA00637; -.
DR Proteomes; UP000002930; Unassembled WGS sequence.
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};
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 Reference proteome {ECO:0000313|Proteomes:UP000002930};
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 59..78
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01072"
FT TRANSMEM 98..123
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01072"
FT TRANSMEM 413..438
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01072"
FT TRANSMEM 467..490
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01072"
FT TRANSMEM 502..526
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01072"
FT TRANSMEM 582..605
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01072"
FT DOMAIN 241..432
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF13632"
SQ SEQUENCE 742 AA; 79622 MW; 1AAECF7FE0F3C3EE CRC64;
MDAVIGTPAE TAGVAPGDRG VAAAAVEALP PECPLAMPEQ SLWDAATAPP GKTAPRFLAL
RRFLVFGATA ALTGLGAYEM YEVLKVAGLT VAEGVLLALF VLLFAWIAFS LVSTLIGFVA
VLAGPDHTLG IDPDAPLPAL SARTAVLLPT YNEDPHRVMA RLEAIRESLV ETGQGDAFDF
FVLSDTTDPN VWILEEAVHR DLVARTGATN VFYRHRADNT ARKAGNISEW TTRFGGAYAH
MLVLDADSLM TGDTIVRMAA AMERHPSVGL IQTFPVIIDG TTPFARIQQF AGRVYGPLIA
RGIAWWHGSD SNYWGHNAII RVAAFAGQAG LPLLPGPKPF GGHILSHDFV EAALMRRGGW
GVHMAPGLSG SYEECPPSLT DYAVRDRRWC QGNLQHLGVL PARGLHWLSR LHLLTGIGSY
ITSPLWLLFL LLGILLSLQA QFIKPEYFPS GFSLFPRWPS VQDPIRAAWV FAGTMGMLIL
PKILGWITVV ARRSERRGCG GVVRSFLGVI FETIVTSLIA PIMMLLQSRS VGEILLGRDA
GWNAQQRKAG EAQLAVLARG YGSHVLLGVL LGAAAWAVSA PLLLWMTPVV VGLVLAIPTV
AFTASERIGA ALRRMGLLLI PEESTPPPIL SRVHEIEAAA YGPPAGGDGL LMLRDDPDLL
DAHCAMLPAK KPRKRGEVDL PLVVGLAKID DAESVADASG LLSPSEKLAV LRDHRAVARL
MALPADARTT PLADETRTLR PN
//
