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Database: UniProt
Entry: D2ACC4_SHIF2
LinkDB: D2ACC4_SHIF2
Original site: D2ACC4_SHIF2 
ID   D2ACC4_SHIF2            Unreviewed;       847 AA.
AC   D2ACC4;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   27-MAR-2024, entry version 72.
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=mdoH {ECO:0000256|HAMAP-Rule:MF_01072,
GN   ECO:0000313|EMBL:ADA73442.1};
GN   Synonyms=opgH {ECO:0000256|HAMAP-Rule:MF_01072};
GN   OrderedLocusNames=SFxv_1188 {ECO:0000313|EMBL:ADA73442.1};
OS   Shigella flexneri serotype X (strain 2002017).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=591020 {ECO:0000313|EMBL:ADA73442.1, ECO:0000313|Proteomes:UP000001884};
RN   [1] {ECO:0000313|EMBL:ADA73442.1, ECO:0000313|Proteomes:UP000001884}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2002017 {ECO:0000313|EMBL:ADA73442.1,
RC   ECO:0000313|Proteomes:UP000001884};
RX   PubMed=19955273; DOI=10.1128/JCM.00614-09;
RA   Ye C., Lan R., Xia S., Zhang J., Sun Q., Zhang S., Jing H., Wang L., Li Z.,
RA   Zhou Z., Zhao A., Cui Z., Cao J., Jin D., Huang L., Wang Y., Luo X.,
RA   Bai X., Wang Y., Wang P., Xu Q., Xu J.;
RT   "Emergence of a new multidrug-resistant serotype X variant in an epidemic
RT   clone of Shigella flexneri.";
RL   J. Clin. Microbiol. 48:419-426(2010).
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 inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01072}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01072}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC       membrane protein {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; CP001383; ADA73442.1; -; Genomic_DNA.
DR   RefSeq; WP_001295445.1; NC_017328.1.
DR   AlphaFoldDB; D2ACC4; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   GeneID; 75203637; -.
DR   KEGG; sfe:SFxv_1188; -.
DR   PATRIC; fig|591020.3.peg.1278; -.
DR   HOGENOM; CLU_015730_1_0_6; -.
DR   UniPathway; UPA00637; -.
DR   Proteomes; UP000001884; 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, ECO:0000256|HAMAP-
KW   Rule:MF_01072}; 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        139..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01072"
FT   TRANSMEM        188..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01072"
FT   TRANSMEM        512..533
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01072"
FT   TRANSMEM        566..590
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01072"
FT   TRANSMEM        599..617
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01072"
FT   TRANSMEM        682..706
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01072"
FT   DOMAIN          246..428
FT                   /note="Glycosyltransferase 2-like"
FT                   /evidence="ECO:0000259|Pfam:PF00535"
SQ   SEQUENCE   847 AA;  96937 MW;  7DCAF93640180944 CRC64;
     MNKTTEYIDA MPIAASEKAA LPKTDIRAVH QALDAEHRTW AREDDSPQGS VKARLEQAWP
     DSLADGQLIK DDEGRDQLKA MPEAKRSSMF PDPWRTNPVG RFWDRLRGRD VTPRYLARLT
     KEEQESEQKW RTVGTIRRYI LLILTLAQTV VATWYMKTIL PYQGWALINP MDMVGQDLWV
     SFMQLLPYML QTGILILFAV LFCWVSAGFW TALMGFLQLL IGRDKYSISA STVGDEPLNP
     EHRTALIMPI CNEDVNRVFA GLRATWESVK ATGNAKHFDV YILSDSYNPD ICVAEQKAWM
     ELIAEVGGEG QIFYRRRRRR VKRKSGNIDD FCRRWGSQYS YMVVLDADSV MTGDCLCGLV
     RLMEANPNAG IIQSSPKASG MDTLYARCQQ FATRVYGPLF TAGLHFWQLG ESHYWGHNAI
     IRVKPFIEHC ALAPLPGEGS FAGSILSHDF VEAALMRRAG WGVWIAYDLP GSYEELPPNL
     LDELKRDRRW CHGNLMNFRL FLVKGMHPVH RAVFLTGVMS YLSAPLWFMF LALSTALQVV
     HALTEPQYFL QPRQLFPVWP QWRPELAIAL FASTMVLLFL PKLLSILLIW CKGTKEYGGF
     WRVTLSLLLE VLFSVLLAPV RMLFHTVFVV SAFLGWEVVW NSPQRDDDST SWGEAFKRHG
     SQLLLGLVWA VGMAWLDLRF LFWLAPIVFS LILSPFVSVI SSRATVGLRT KRWKLFLIPE
     EYSPPQVLVD TDRFLEMNRQ RSLDDGFMHA VFNPSFNALA TAMATARHRA SKVLEIARDR
     HVEQALNETP EKLNRDRRLV LLSDPVTMAR LHFRVWNSPE RYSSWVSYYE GIKLNPLALR
     KPDAASQ
//
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