ID   TREA_XANOM              Reviewed;         568 AA.
AC   Q2NYS3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Periplasmic trehalase {ECO:0000255|HAMAP-Rule:MF_01060};
DE            EC=3.2.1.28 {ECO:0000255|HAMAP-Rule:MF_01060};
DE   AltName: Full=Alpha,alpha-trehalase {ECO:0000255|HAMAP-Rule:MF_01060};
DE   AltName: Full=Alpha,alpha-trehalose glucohydrolase {ECO:0000255|HAMAP-Rule:MF_01060};
DE   Flags: Precursor;
GN   Name=treA {ECO:0000255|HAMAP-Rule:MF_01060}; OrderedLocusNames=XOO3799;
OS   Xanthomonas oryzae pv. oryzae (strain MAFF 311018).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=342109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF 311018;
RA   Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.;
RT   "Genome sequence of Xanthomonas oryzae pv. oryzae suggests contribution of
RT   large numbers of effector genes and insertion sequences to its race
RT   diversity.";
RL   Jpn. Agric. Res. Q. 39:275-287(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:0000255|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:0000255|HAMAP-Rule:MF_01060};
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_01060}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 37 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01060}.
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DR   EMBL; AP008229; BAE70554.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2NYS3; -.
DR   SMR; Q2NYS3; -.
DR   CAZy; GH37; Glycoside Hydrolase Family 37.
DR   KEGG; xom:XOO3799; -.
DR   HOGENOM; CLU_006451_3_1_6; -.
DR   OMA; TNGVLIW; -.
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   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   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   Glycosidase; Hydrolase; Periplasm; Signal.
FT   SIGNAL          1..39
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT   CHAIN           40..568
FT                   /note="Periplasmic trehalase"
FT                   /id="PRO_1000064460"
FT   ACT_SITE        329
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT   ACT_SITE        511
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT   BINDING         169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT   BINDING         176..177
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT   BINDING         213
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT   BINDING         222..224
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT   BINDING         294..296
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT   BINDING         327
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT   BINDING         526
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
SQ   SEQUENCE   568 AA;  63233 MW;  22A8E541F758954E CRC64;
     MPHVVARSGD VMSSAAPPSC TSLLGLSLSM FVAPCTLTAA PLDTPVVNAP APTPPTPDQA
     YPELFQAVQS GELFDDQKHF VDFLPLRDPA LINADYLAQH DHPGFDLRKF VDANFEESPP
     VQTDAIRQDT ALREHIDLLW PKLVRSQNHV PPYSSLLSLP HPYVVPGGRF REVYYWDSYF
     TMLGLVKSGQ TTLSRQMLDN FAYLIDTYGH IPNGNRSYYL SRSQPPFFSY MVELQAGVEG
     QAVYQRYLPQ LQKEYAYWMQ GSDDVQPGQA ARHVVRLADG SVLNRYWDER DTPRPEAWLH
     DTRTAAEVKD RPAAEVYRDL RAGAESGWDY TSRWLADGQN LRTIRTTAII PIDLNSLLYH
     LERTLAQACA QPGAACSRDY AALAQQRKQA IDAHLWNKAG YYADYDWQTR TLSDQITAAA
     LYPLFAGLAS DDHAKRTAST VRRTLVRPGG LATTAVKTGQ QWDEPNGWAP LQWVAVDGLR
     RYGEQALART IGERFLAQVQ ALFAREHKLV EKYGLETNAA GGGGGEYALQ DGFGWTNGVT
     LMLLNLYPGK GAKAAPAKRV RKTEAAAR