ID   OPGD_SHIB3              Reviewed;         551 AA.
AC   B2U143;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Glucans biosynthesis protein D {ECO:0000255|HAMAP-Rule:MF_01068};
DE   Flags: Precursor;
GN   Name=mdoD {ECO:0000255|HAMAP-Rule:MF_01068};
GN   Synonyms=opgD {ECO:0000255|HAMAP-Rule:MF_01068};
GN   OrderedLocusNames=SbBS512_E1649;
OS   Shigella boydii serotype 18 (strain CDC 3083-94 / BS512).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=344609;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 3083-94 / BS512;
RA   Rasko D.A., Rosovitz M., Maurelli A.T., Myers G., Seshadri R., Cer R.,
RA   Jiang L., Ravel J., Sebastian Y.;
RT   "Complete sequence of Shigella boydii serotype 18 strain BS512.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probably involved in the control of the structural glucose
CC       backbone of osmoregulated periplasmic glucans (OPGs).
CC       {ECO:0000255|HAMAP-Rule:MF_01068}.
CC   -!- PATHWAY: Glycan metabolism; osmoregulated periplasmic glucan (OPG)
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01068}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_01068}.
CC   -!- PTM: Predicted to be exported by the Tat system. The position of the
CC       signal peptide cleavage has not been experimentally proven.
CC   -!- SIMILARITY: Belongs to the OpgD/OpgG family. {ECO:0000255|HAMAP-
CC       Rule:MF_01068}.
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DR   EMBL; CP001063; ACD06382.1; -; Genomic_DNA.
DR   RefSeq; WP_000375947.1; NC_010658.1.
DR   AlphaFoldDB; B2U143; -.
DR   SMR; B2U143; -.
DR   STRING; 344609.SbBS512_E1649; -.
DR   EnsemblBacteria; ACD06382; ACD06382; SbBS512_E1649.
DR   KEGG; sbc:SbBS512_E1649; -.
DR   HOGENOM; CLU_023403_2_0_6; -.
DR   OMA; DVQFFHV; -.
DR   UniPathway; UPA00637; -.
DR   Proteomes; UP000001030; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0009250; P:glucan biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 2.70.98.10; -; 1.
DR   HAMAP; MF_01068; MdoD_OpgD; 1.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR014718; GH-type_carb-bd.
DR   InterPro; IPR023724; Glucan_biosyn_MdoD.
DR   InterPro; IPR014438; Glucan_biosyn_MdoG/MdoD.
DR   InterPro; IPR007444; Glucan_biosyn_MdoG_C.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR006311; TAT_signal.
DR   InterPro; IPR019546; TAT_signal_bac_arc.
DR   PANTHER; PTHR30504; PTHR30504; 1.
DR   Pfam; PF04349; MdoG; 1.
DR   PIRSF; PIRSF006281; MdoG; 1.
DR   SUPFAM; SSF74650; SSF74650; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Periplasm; Signal.
FT   SIGNAL          1..32
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01068"
FT   CHAIN           33..551
FT                   /note="Glucans biosynthesis protein D"
FT                   /id="PRO_1000136603"
SQ   SEQUENCE   551 AA;  62772 MW;  E822E2E8D5A00F70 CRC64;
     MDRRRFIKGS MAMAAVCGTS GIASLFSQAA FAADSDIADG QTQRFDFSIL QSMAHDLAQT
     AWRGAPRPLP DTLATMTPQA YNSIQYDAEK SLWHNVENRQ LDAQFFHMGM GFRRRVRMFS
     VDPATHLARE IHFRPELFKY NDAGVDTKQL EGQSDLGFAG FRVFKAPELA RRDVVSFLGA
     SYFRAVDDTY QYGLSARGLA IDTYTDSKEE FPDFTAFWFD TVKPGATTFT VYALLDSASI
     TGAYKFTIHC EKSQVIMDVE NHLYARKDIK QLGIAPMTSM FSCGTNERRM CDTIHPQIHD
     SDRLSMWRGN GEWICRPLNN PQKLQFNAYT DNNPKGFGLL QLDRDFSHYQ DIMGWYNKRP
     SLWLEPRNKW GKGTIGLMEI PTTGETLDNI VCFWQPEKAV KAGDEFAFQY RLYWSAQPPV
     HCPLARVMAT RTGMGGFPEG WAPGEHYPEK WARRFAVDFV GGDLKAAAPK GIEPVITLSS
     GEAKQIEILY IEPIDGYRIQ FDWYPTSDST DPVDMRMYLR CQGDAISETW LYQYFPPASD
     KRQYVDDRVM S