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Database: UniProt
Entry: OPGH_SHEB8
LinkDB: OPGH_SHEB8
Original site: OPGH_SHEB8 
ID   OPGH_SHEB8              Reviewed;         727 AA.
AC   A6WMM7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 78.
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};
GN   OrderedLocusNames=Shew185_1923;
OS   Shewanella baltica (strain OS185).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=402882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS185;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Brettar I., Rodrigues J., Konstantinidis K., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Shewanella baltica OS185.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000753; ABS08066.1; -; Genomic_DNA.
DR   RefSeq; WP_006086416.1; NC_009665.1.
DR   AlphaFoldDB; A6WMM7; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   GeneID; 11772130; -.
DR   KEGG; sbm:Shew185_1923; -.
DR   HOGENOM; CLU_015730_1_0_6; -.
DR   UniPathway; UPA00637; -.
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; Cell membrane; Glycosyltransferase; Membrane;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..727
FT                   /note="Glucans biosynthesis glucosyltransferase H"
FT                   /id="PRO_1000084501"
FT   TRANSMEM        58..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01072"
FT   TRANSMEM        97..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01072"
FT   TRANSMEM        278..298
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01072"
FT   TRANSMEM        408..428
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01072"
FT   TRANSMEM        460..480
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01072"
FT   TRANSMEM        496..516
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01072"
FT   TRANSMEM        572..592
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01072"
FT   REGION          18..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   727 AA;  81031 MW;  F6F3810EC6C73AD9 CRC64;
     MTVSENSVLE TEVLVGGSAM PNERPGAMEP QNLSKMPEGF PRRSTVANGV RSRASRRFLV
     VGGALLLSLF AIYEMGAVFS IGGITPLEYL VLALFAVNFC WIALAFCSGI AGFLILLRKP
     RAKDLQVTEL HTRTAILMPT YNESPDRVFS AVSVMAETLS QTGHGHAFDW FILSDTTDPD
     IALLEEQAFL VLRQETHKHS RVYYRRRRKN VARKAGNVAD FCRRWGSRYD HLLVLDADSL
     MESSTITGLA QRMQADPDAG LIQTIPSLIN GTTLMARLQQ FAARIYGPVI GTGLGWWVQK
     EGNFWGHNAI IRTEAFMTAA GLPNLKGKPP FGGHIMSHDF VEAALIRRAG WSVVIAYDLP
     GSYEECPPSI IDLAVRDRRW CQGNLQHSRI LPTKGLHWVS RLHLLTGIMA YLSSPFWLML
     ILTGLMLALQ AHFIRPEYFT DQFSLFPTWP IMDSDRALRL FYITMGVLFG PKVFGVLLLL
     KDGEFARSVG GRIKAIFSVI FEVILSALIA PIMMFIHCGA VMSILMGRDS GWSPQRRDDG
     SMPWMTLIYR HRWHMLAGVM LGYAAILDSL TLLAWMSPAL IGLWIAVPIS AWTGSVKIGE
     VFKRAGILAT PEERNPAQIC LQAHEARAAY QKHIAEPWTL AQVLKDPALM ELHLAMVDKQ
     PLRAAGTPIE AMEAIVHVKV HEARCQQSAL AVLNRQEMAM VLANPLMLRS LQKLPEQFVE
     EDLVSFC
//
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