ID   TREA_XANCB              Reviewed;         568 AA.
AC   B0RNH1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
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};
GN   OrderedLocusNames=xcc-b100_0667;
OS   Xanthomonas campestris pv. campestris (strain B100).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=509169;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B100;
RX   PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013;
RA   Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T.,
RA   Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., Sidhu V.K.,
RA   Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K.,
RA   Puehler A.;
RT   "The genome of Xanthomonas campestris pv. campestris B100 and its use for
RT   the reconstruction of metabolic pathways involved in xanthan
RT   biosynthesis.";
RL   J. Biotechnol. 134:33-45(2008).
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; AM920689; CAP50006.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0RNH1; -.
DR   SMR; B0RNH1; -.
DR   KEGG; xca:xcc-b100_0667; -.
DR   HOGENOM; CLU_006451_3_1_6; -.
DR   OMA; TNGVLIW; -.
DR   Proteomes; UP000001188; Chromosome.
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..38
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT   CHAIN           39..568
FT                   /note="Periplasmic trehalase"
FT                   /id="PRO_1000136428"
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;  62663 MW;  29E4FA266074FF0A CRC64;
     MPHAPARSGD AMSAAAPPCC TSLLGLSLSM FVAPCALAAT PLEGAVVSAP APTPPTPDLA
     YPELFQAVQR GELFDDQKHF VDFLPLRDPA LINADYLAQH EHAGFDLRKF VDANFEESPP
     VQTDAIRQDT ALREHIDALW PKLVRSQTNV PAHSSLLALP HPYVVPGGRF REVYYWDSYF
     TMLGLVKSGE TTLSRQMLDN FAYLIDTYGH IPNGNRTYYL SRSQPPFFSY MVELQAGVEG
     EAVYQRYLPQ LQKEYAYWMQ GGDDLQPGQA ARHVVRLADG SVLNRYWDER DTPRPEAWLH
     DTRTAAEAHD RPAADVYRDL RAGAESGWDY TSRWLADGKT LSTIRTTAIV PIDLNSLLYH
     LERTLAQACA HTGTACSQDY AALAQQRKQA IDAHLWNAAG YYADYDWQTR TLSNQVTAAA
     LYPLFAGLAS ADHAKRTATS VRARLLRPGG LATTALKTGQ QWDEPNGWAP LQWVAVDGLR
     RYGEDGLART IGERFLTQVQ ALFAREHKLV EKYGLDADAA GGGGGEYALQ DGFGWTNGVT
     LMLLNLYPSP GAIQAPAKTK RKPEPAAP