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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
 
 
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