ID   Q2T4F3_BURTA            Unreviewed;       562 AA.
AC   Q2T4F3;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   10-JUN-2026, entry version 102.
DE   RecName: Full=Periplasmic trehalase {ECO:0000256|HAMAP-Rule:MF_01060};
DE            EC=3.2.1.28 {ECO:0000256|HAMAP-Rule:MF_01060};
DE   AltName: Full=Alpha,alpha-trehalase {ECO:0000256|HAMAP-Rule:MF_01060};
DE   AltName: Full=Alpha,alpha-trehalose glucohydrolase {ECO:0000256|HAMAP-Rule:MF_01060};
GN   Name=treA {ECO:0000256|HAMAP-Rule:MF_01060};
GN   OrderedLocusNames=BTH_II1752 {ECO:0000313|EMBL:ABC34000.1};
OS   Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CCUG 48851 /
OS   CIP 106301 / E264).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848 {ECO:0000313|EMBL:ABC34000.1, ECO:0000313|Proteomes:UP000001930};
RN   [1] {ECO:0000313|EMBL:ABC34000.1, ECO:0000313|Proteomes:UP000001930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700388 / DSM 13276 / CCUG 48851 / CIP 106301 / E264
RC   {ECO:0000313|Proteomes:UP000001930};
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).
CC   -!- FUNCTION: Provides the cells with the ability to utilize trehalose at
CC       high osmolarity by splitting it into glucose molecules that can
CC       subsequently be taken up by the phosphotransferase-mediated uptake
CC       system. {ECO:0000256|HAMAP-Rule:MF_01060}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha,alpha-trehalose + H2O = alpha-D-glucose + beta-D-
CC         glucose; Xref=Rhea:RHEA:32675, ChEBI:CHEBI:15377, ChEBI:CHEBI:15903,
CC         ChEBI:CHEBI:16551, ChEBI:CHEBI:17925; EC=3.2.1.28;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01060};
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|HAMAP-Rule:MF_01060}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 37 family.
CC       {ECO:0000256|HAMAP-Rule:MF_01060}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01060}.
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DR   EMBL; CP000085; ABC34000.1; -; Genomic_DNA.
DR   RefSeq; WP_009897811.1; NC_007650.1.
DR   AlphaFoldDB; Q2T4F3; -.
DR   GeneID; 45119184; -.
DR   KEGG; bte:BTH_II1752; -.
DR   HOGENOM; CLU_006451_3_2_4; -.
DR   Proteomes; UP000001930; Chromosome II.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004555; F:alpha,alpha-trehalase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0071474; P:cellular hyperosmotic response; IEA:InterPro.
DR   GO; GO:0005993; P:trehalose catabolic process; IEA:InterPro.
DR   FunFam; 1.50.10.10:FF:000003; Cytoplasmic trehalase; 1.
DR   Gene3D; 1.50.10.10; -; 1.
DR   HAMAP; MF_01060; Peripl_trehalase; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR001661; Glyco_hydro_37.
DR   InterPro; IPR018232; Glyco_hydro_37_CS.
DR   InterPro; IPR023720; Trehalase_periplasmic.
DR   NCBIfam; NF009773; PRK13270.1; 1.
DR   NCBIfam; NF009774; PRK13271.1; 1.
DR   PANTHER; PTHR23403; TREHALASE; 1.
DR   PANTHER; PTHR23403:SF1; TREHALASE; 1.
DR   Pfam; PF01204; Trehalase; 1.
DR   PRINTS; PR00744; GLHYDRLASE37.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   PROSITE; PS00927; TREHALASE_1; 1.
DR   PROSITE; PS00928; TREHALASE_2; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|HAMAP-
KW   Rule:MF_01060};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01060};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|HAMAP-Rule:MF_01060};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001930};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_01060}.
FT   ACT_SITE        340
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01060"
FT   ACT_SITE        523
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01060"
FT   BINDING         180
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01060"
FT   BINDING         187..188
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01060"
FT   BINDING         224
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01060"
FT   BINDING         233..235
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01060"
FT   BINDING         338
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01060"
FT   BINDING         539
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01060"
SQ   SEQUENCE   562 AA;  61874 MW;  CB4544294D1376ED CRC64;
     MVTPRHRPLH VENPFYRRLL SAPAWLALVA AAGIGCTNAT LARADSSHAS AAVSSAASAP
     SAASIPPPPS QLYGDLFVAV QTAQIFEDQK TFVDSTPNTD PATIVRLYEQ QKGQPGFSLK
     AFVAQYFTPP SDQSVTPPPN QTLREHIDWL WPKLTRTTTA AQPYSSLIAL PKPYVVPGGR
     FREGYYWDTY FTMLGLQESG REDLVDDMLE NFAYLIDTVG HVPNGNRSYY VSRSQPPFFA
     YMVTLAAKVE GNGVYQKYLP ALRKEYAYWM QGERTTPRGQ AARNVVAMPD GSVLNRYWDA
     SDTPRDESYL EDVKTAQQAS GRPAPQVWRD LRAAAESGWD FSSRWFGDGR TLATIRTTAI
     VPVDLNSLMF NLETTIVKGC AVTRDFACVA EFAGRAGKRA VAINRYLWNR NGYYGDYDWK
     LGKPRDNLSA AALYPLFAGV AWPERAKQTA KNVRKTLLKP GGLATTTYDT AQQWDAPNGW
     APLHWIALIG LRHYGEKSLA DEIGTRFLAD VKGVYAAQGK LVEKYIVEGA GTGGGGGGEY
     PLQDGFGWTN GVTLKLLDLY GG
//