ID   OPGD_XYLF2              Reviewed;         534 AA.
AC   B2IAA4;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Glucans biosynthesis protein D {ECO:0000255|HAMAP-Rule:MF_01068};
DE   Flags: Precursor;
GN   Name=opgD {ECO:0000255|HAMAP-Rule:MF_01068};
GN   OrderedLocusNames=XfasM23_2144;
OS   Xylella fastidiosa (strain M23).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=405441;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M23;
RX   PubMed=20601474; DOI=10.1128/jb.00651-10;
RA   Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.;
RT   "Whole genome sequences of two Xylella fastidiosa strains (M12 and M23)
RT   causing almond leaf scorch disease in California.";
RL   J. Bacteriol. 192:4534-4534(2010).
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; CP001011; ACB93540.1; -; Genomic_DNA.
DR   RefSeq; WP_004087424.1; NC_010577.1.
DR   AlphaFoldDB; B2IAA4; -.
DR   SMR; B2IAA4; -.
DR   EnsemblBacteria; ACB93540; ACB93540; XfasM23_2144.
DR   GeneID; 58017556; -.
DR   KEGG; xfn:XfasM23_2144; -.
DR   HOGENOM; CLU_023403_2_0_6; -.
DR   OMA; DVQFFHV; -.
DR   UniPathway; UPA00637; -.
DR   Proteomes; UP000001698; 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   PANTHER; PTHR30504; PTHR30504; 1.
DR   Pfam; PF04349; MdoG; 1.
DR   PIRSF; PIRSF006281; MdoG; 1.
DR   SUPFAM; SSF74650; SSF74650; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   3: Inferred from homology;
KW   Periplasm; Signal.
FT   SIGNAL          1..28
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01068"
FT   CHAIN           29..534
FT                   /note="Glucans biosynthesis protein D"
FT                   /id="PRO_1000213470"
SQ   SEQUENCE   534 AA;  61348 MW;  C197101FEE936A3E CRC64;
     MYRRDFLKSV TAAWVAFGLP NPLGGAFATN RVIPLRRLGQ SQRFDYEWLK ERARALAATP
     YHSRKRVLPT PLERLSWDQY QSIRYRQDHA LWADSDAHFQ VKFFHLGLYF HSPVRMYEVV
     DGMAQELAYD PAAFDYGSSG LNGKGLPKDL GFAGFRLNTR KDIDRDFAAF LGASYFRAVG
     QEGQYGQSAR GLAVNTGSSG PEEFPDFIAY YLEQPTADAD TVVMYGLLDS PSIAGAYRFS
     ITHADVLRMD IDSALYPRET IERLGIAPCT SMYQVGENDR RMGWDWRPEI HDTDGLFLWT
     GNGEWIWRPL CNPLHLRFNM FLDNNPRGFG LLQRDRDFDH YQDDGVFYEK RPCLWVEPKH
     GWGEGSVQLV EIPTFDETFD NIVAFWNPRN KPHPGQELLF GYRLYWGAFP PVSSSLAYCV
     ATRTGLGGVV GQKRKYFSWR FAVDFVGGKL AALARVHDVS VEPVLHMTRG RPEIVSARPL
     HEIRGYRVMF DVVPLEDSAQ QIDIRLYLRD TNGEPLTETW LYQWVPPILE ERKY