OPGH_SHIFL
ID OPGH_SHIFL Reviewed; 847 AA.
AC P62519; P33137; P77371;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Glucans biosynthesis glucosyltransferase H;
DE EC=2.4.1.-;
GN Name=mdoH; Synonyms=opgH; OrderedLocusNames=SF1045, S1119;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
CC -!- FUNCTION: Involved in the biosynthesis of osmoregulated periplasmic
CC glucans (OPGs). {ECO:0000250}.
CC -!- PATHWAY: Glycan metabolism; osmoregulated periplasmic glucan (OPG)
CC biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. OpgH
CC subfamily. {ECO:0000305}.
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DR EMBL; AE005674; AAN42667.2; -; Genomic_DNA.
DR EMBL; AE014073; AAP16551.1; -; Genomic_DNA.
DR RefSeq; NP_706960.2; NC_004337.2.
DR RefSeq; WP_001295445.1; NZ_WPGW01000143.1.
DR AlphaFoldDB; P62519; -.
DR STRING; 198214.SF1045; -.
DR EnsemblBacteria; AAN42667; AAN42667; SF1045.
DR EnsemblBacteria; AAP16551; AAP16551; S1119.
DR GeneID; 1023984; -.
DR GeneID; 66670683; -.
DR KEGG; sfl:SF1045; -.
DR KEGG; sfx:S1119; -.
DR PATRIC; fig|198214.7.peg.1219; -.
DR HOGENOM; CLU_015730_1_0_6; -.
DR OMA; TAGLHYW; -.
DR OrthoDB; 1049243at2; -.
DR UniPathway; UPA00637; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 Gene3D; 3.90.550.10; -; 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 Pfam; PF00535; Glycos_transf_2; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Glycosyltransferase; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..847
FT /note="Glucans biosynthesis glucosyltransferase H"
FT /id="PRO_0000210364"
FT TOPO_DOM 1..139
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..193
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..512
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 513..533
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 534..569
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 570..590
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 591..602
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 603..625
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 626..679
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 680..700
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 701..847
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
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
