ID   OPGD_ECOBW              Reviewed;         551 AA.
AC   C4ZVG4;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 58.
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=BWG_1250;
OS   Escherichia coli (strain K12 / MC4100 / BW2952).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=595496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MC4100 / BW2952;
RX   PubMed=19376874; DOI=10.1128/jb.00118-09;
RA   Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R.,
RA   Wang L.;
RT   "Genomic sequencing reveals regulatory mutations and recombinational events
RT   in the widely used MC4100 lineage of Escherichia coli K-12.";
RL   J. Bacteriol. 191:4025-4029(2009).
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; CP001396; ACR63300.1; -; Genomic_DNA.
DR   RefSeq; WP_000375961.1; NC_012759.1.
DR   AlphaFoldDB; C4ZVG4; -.
DR   SMR; C4ZVG4; -.
DR   KEGG; ebw:BWG_1250; -.
DR   HOGENOM; CLU_023403_2_0_6; -.
DR   OMA; DVQFFHV; -.
DR   UniPathway; UPA00637; -.
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_1000213468"
SQ   SEQUENCE   551 AA;  62758 MW;  4FC3BE21F70D4C46 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
     SLWVEPRNKW GKGTIGLMEI PTTGETLDNI VCFWQPEKAV KAGDEFAFQY RLYWSAQPPV
     HCPLARVMAT RTGMGGFSEG WAPGEHYPEK WARRFAVDFV GGDLKAAAPK GIEPVITLSS
     GEAKQIEILY IEPIDGYRIQ FDWYPTSDST DPVDMRMYLR CQGDAISETW LYQYFPPAPD
     KRQYVDDRVM S