Y986_BURTA
ID Y986_BURTA Reviewed; 363 AA.
AC Q2SZV9;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Probable transglycosylase BTH_I0986 {ECO:0000303|PubMed:25786241};
DE EC=2.4.-.-;
GN OrderedLocusNames=BTH_I0986;
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS E264).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(2005).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX PubMed=25786241; DOI=10.1371/journal.pone.0120265;
RA Koskiniemi S., Garza-Sanchez F., Edman N., Chaudhuri S., Poole S.J.,
RA Manoil C., Hayes C.S., Low D.A.;
RT "Genetic analysis of the CDI pathway from Burkholderia pseudomallei
RT 1026b.";
RL PLoS ONE 10:E0120265-E0120265(2015).
CC -!- FUNCTION: Probably a transglycosylase. Probably involved in synthesis
CC of the outer membrane receptor for a cellular contact-dependent growth
CC inhibition (CDI) system. {ECO:0000305|PubMed:25786241}.
CC -!- DISRUPTION PHENOTYPE: Disruption confers resistance to cellular
CC contact-dependent growth inhibition (CDI) CdiA-2 of B.pseudomallei
CC strain 1026b, but not to endogenous CdiA. Alters lipopolysaccharide
CC structure, decreased binding to B.pseudomallei strain 1026b inhibitor
CC cells. {ECO:0000269|PubMed:25786241}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC Glycosyltransferase 4 subfamily. {ECO:0000305}.
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DR EMBL; CP000086; ABC36447.1; -; Genomic_DNA.
DR RefSeq; WP_009892326.1; NZ_CP008785.1.
DR AlphaFoldDB; Q2SZV9; -.
DR SMR; Q2SZV9; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR PRIDE; Q2SZV9; -.
DR DNASU; 3847095; -.
DR EnsemblBacteria; ABC36447; ABC36447; BTH_I0986.
DR KEGG; bte:BTH_I0986; -.
DR HOGENOM; CLU_068046_0_0_4; -.
DR OMA; EPHRINV; -.
DR OrthoDB; 635734at2; -.
DR Proteomes; UP000001930; Chromosome I.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR028098; Glyco_trans_4-like_N.
DR Pfam; PF13439; Glyco_transf_4; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase; Transferase.
FT CHAIN 1..363
FT /note="Probable transglycosylase BTH_I0986"
FT /id="PRO_0000446877"
SQ SEQUENCE 363 AA; 39696 MW; CB2FE0DA66024B45 CRC64;
MTIGLSCNAL KYGGGLERYA IDLARGLADA GVRPLVFARS FDSSVPEYQC VEPRRINVSF
LPGKCRDAWF SWRLRAARRA APVDVLIGCN RVDSSDIAIC GGTHLGFLDA IGRMPTFSDR
RQIALERRQY ARARFVVAHS MLMRDELRRF YGLSDDKIRV LFPPVDAARF TPVDAVRRAE
LRTRFGFADD EVVLLFPSSS HERKGLPLIE AILRDAGPRV VVAVAGRPPE RTSERLRYVG
YVKDIEDGYR AADFTILASK YEPFGLVGVE SVMCGTPVIL PSNIGCCDAI APSAKLVFAP
GDAAGLRGML DEAVRRVRAG AVRVESGAAA RAAIQYDPSV ARHVAQLLDL AAEAASDRRN
GGR