OPGD_XANC8
ID OPGD_XANC8 Reviewed; 533 AA.
AC Q4UNU8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 88.
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}; OrderedLocusNames=XC_4237;
OS Xanthomonas campestris pv. campestris (strain 8004).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=314565;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8004;
RX PubMed=15899963; DOI=10.1101/gr.3378705;
RA Qian W., Jia Y., Ren S.-X., He Y.-Q., Feng J.-X., Lu L.-F., Sun Q.,
RA Ying G., Tang D.-J., Tang H., Wu W., Hao P., Wang L., Jiang B.-L., Zeng S.,
RA Gu W.-Y., Lu G., Rong L., Tian Y., Yao Z., Fu G., Chen B., Fang R.,
RA Qiang B., Chen Z., Zhao G.-P., Tang J.-L., He C.;
RT "Comparative and functional genomic analyses of the pathogenicity of
RT phytopathogen Xanthomonas campestris pv. campestris.";
RL Genome Res. 15:757-767(2005).
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; CP000050; AAY51275.1; -; Genomic_DNA.
DR RefSeq; WP_011270101.1; NC_007086.1.
DR AlphaFoldDB; Q4UNU8; -.
DR SMR; Q4UNU8; -.
DR EnsemblBacteria; AAY51275; AAY51275; XC_4237.
DR KEGG; xcb:XC_4237; -.
DR HOGENOM; CLU_023403_2_0_6; -.
DR OMA; DVQFFHV; -.
DR OrthoDB; 1049230at2; -.
DR UniPathway; UPA00637; -.
DR Proteomes; UP000000420; 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 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 PROSITE; PS51318; TAT; 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..533
FT /note="Glucans biosynthesis protein D"
FT /id="PRO_1000084492"
SQ SEQUENCE 533 AA; 59789 MW; AAACEAE1849298C8 CRC64;
MQRRHFLKNA AAALAALGLP ALPPWALAAK AVGLRRLGQP QPFDYAWLKG QARALAKAPY
KSHKQVLPGP LESLNWDQYQ SIRYRQDHAL WADGNGKFQA KFFHLGLYFH TPVHIYDIVD
GKAQQLAYDP AAFDYGRSGL GGKQLPKDLG FAGFRLNTRK DTDRDFSAFL GASYFRAVGK
EGQYGQSARG LAIDTGTGGP EEFPDFIAYY LEQPADDSDT VVVYGLLDSP SVSGAYRFAI
TNGEVLVMDI DSALYPRKAI ERLGIGPCTS MYQTGENDRR MDWDWRPEIH DTDGLAMWTG
GGEWIWRPLC NPPHLRFNMF VDENPRGFGL LQRDRNFDHY QDDGVFYEKR PCLWVEPKSG
WGKGSVQLVE IPTVDETFDN IVAFWNPQAK PQPGQELLMG YRLYWGAHPP ASSPLAHCMA
TRTGLGGIVG QKRSHFSWRF AVDFAGGELA ALAKDPKAKV EAVLQVSRGT TEIVSARPLH
ELKGYRAMFD LVPPDEGTQQ IDIRLFLRAN GKPLTETWLY QWTPPPASER KIY