ID   TREF_ECOUT              Reviewed;         549 AA.
AC   Q1R584;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Cytoplasmic trehalase {ECO:0000255|HAMAP-Rule:MF_01059};
DE            EC=3.2.1.28 {ECO:0000255|HAMAP-Rule:MF_01059};
DE   AltName: Full=Alpha,alpha-trehalase {ECO:0000255|HAMAP-Rule:MF_01059};
DE   AltName: Full=Alpha,alpha-trehalose glucohydrolase {ECO:0000255|HAMAP-Rule:MF_01059};
GN   Name=treF {ECO:0000255|HAMAP-Rule:MF_01059}; OrderedLocusNames=UTI89_C4051;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC;
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA   Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA   Gordon J.I.;
RT   "Identification of genes subject to positive selection in uropathogenic
RT   strains of Escherichia coli: a comparative genomics approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
CC   -!- FUNCTION: Hydrolyzes trehalose to glucose. Could be involved, in cells
CC       returning to low osmolarity conditions, in the utilization of the
CC       accumulated cytoplasmic trehalose, which was synthesized in response to
CC       high osmolarity. {ECO:0000255|HAMAP-Rule:MF_01059}.
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:0000255|HAMAP-Rule:MF_01059};
CC   -!- PATHWAY: Glycan degradation; trehalose degradation; D-glucose from
CC       alpha,alpha-trehalose: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01059}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01059}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01059}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 37 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01059}.
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DR   EMBL; CP000243; ABE09480.1; -; Genomic_DNA.
DR   RefSeq; WP_000934214.1; NC_007946.1.
DR   AlphaFoldDB; Q1R584; -.
DR   SMR; Q1R584; -.
DR   CAZy; GH37; Glycoside Hydrolase Family 37.
DR   EnsemblBacteria; ABE09480; ABE09480; UTI89_C4051.
DR   KEGG; eci:UTI89_C4051; -.
DR   HOGENOM; CLU_006451_3_1_6; -.
DR   OMA; DAPFGWA; -.
DR   UniPathway; UPA00300; UER00535.
DR   Proteomes; UP000001952; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; 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:UniProtKB-UniPathway.
DR   Gene3D; 1.50.10.10; -; 1.
DR   HAMAP; MF_01059; Cyt_trehalase; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR023715; Cyt_trehalase.
DR   InterPro; IPR001661; Glyco_hydro_37.
DR   InterPro; IPR018232; Glyco_hydro_37_CS.
DR   PANTHER; PTHR23403; PTHR23403; 1.
DR   Pfam; PF01204; Trehalase; 1.
DR   PRINTS; PR00744; GLHYDRLASE37.
DR   SUPFAM; SSF48208; SSF48208; 1.
DR   PROSITE; PS00927; TREHALASE_1; 1.
DR   PROSITE; PS00928; TREHALASE_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Glycosidase; Hydrolase.
FT   CHAIN           1..549
FT                   /note="Cytoplasmic trehalase"
FT                   /id="PRO_1000064444"
FT   ACT_SITE        326
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01059"
FT   ACT_SITE        509
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01059"
FT   BINDING         168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01059"
FT   BINDING         175..176
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01059"
FT   BINDING         212
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01059"
FT   BINDING         221..223
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01059"
FT   BINDING         292..294
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01059"
FT   BINDING         324
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01059"
FT   BINDING         525
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01059"
SQ   SEQUENCE   549 AA;  63724 MW;  54269FA7E7C9CB9D CRC64;
     MLNQKIQNPN PDELMIEVDL CYELDPYELK LDEMIEAEPE PEMIEGLPAS DALTPADRYL
     ELFEHVQSAK IFPDSKTFPD CAPKMDPLDI LIRYRKVRRH RDFDLRKFVE NHFWLPEVYS
     SEYVSDPQNS LKEHIDQLWP VLTREPQDHI PWSSLLALPQ SYIVPGGRFS ETYYWDSYFT
     MLGLAESGRE DLLKCMADNF AWMIENYGHI PNGNRTYYLS RSQPPVFALM VELFEEDGVR
     GARRYLDHLK MEYAFWMDGA ESLIPNQAYR HVVRMPDGSL LNRYWDDRDT PRDESWLEDV
     ETAKHSGRPP NEVYRDLRAG AASGWDYSSR WLRDTGRLAS IRTTQFIPID LNAFLFKLES
     AIANISALKG EKETEALFRQ KASARRDAVN RYLWDDENGI YRDYDWRREQ LALFSAAAIV
     PLYVGMANHE QADRLANAVR SRLLTPGGIL ASEYETGEQW DKPNGWAPLQ WMAIQGFKMY
     GDDLLGDEIA RNWLKTVNQF YLEQHKLIEK YHIADGVPRE GGGGEYPLQD GFGWTNGVVR
     RLIGLYGEP