ID   TREA_RALSO              Reviewed;         551 AA.
AC   Q8XT38;
DT   03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=RSp0277;
GN   ORFNames=RS03687;
OS   Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OG   Plasmid megaplasmid Rsp.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=267608;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GMI1000;
RX   PubMed=11823852; DOI=10.1038/415497a;
RA   Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA   Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA   Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA   Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA   Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT   "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL   Nature 415:497-502(2002).
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; AL646053; CAD17428.1; -; Genomic_DNA.
DR   RefSeq; WP_011003591.1; NC_003296.1.
DR   AlphaFoldDB; Q8XT38; -.
DR   SMR; Q8XT38; -.
DR   STRING; 267608.RSp0277; -.
DR   CAZy; GH37; Glycoside Hydrolase Family 37.
DR   EnsemblBacteria; CAD17428; CAD17428; RSp0277.
DR   GeneID; 60503214; -.
DR   KEGG; rso:RSp0277; -.
DR   PATRIC; fig|267608.8.peg.3746; -.
DR   eggNOG; COG1626; Bacteria.
DR   HOGENOM; CLU_006451_3_1_4; -.
DR   OMA; TNGVLIW; -.
DR   Proteomes; UP000001436; Plasmid megaplasmid Rsp.
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; Plasmid; Reference proteome; Signal.
FT   SIGNAL          1..45
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT   CHAIN           46..551
FT                   /note="Periplasmic trehalase"
FT                   /id="PRO_0000012045"
FT   ACT_SITE        328
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         168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT   BINDING         175..176
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT   BINDING         212
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT   BINDING         221..223
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT   BINDING         293..295
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT   BINDING         326
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   551 AA;  60733 MW;  AE9AD74F51853274 CRC64;
     MLDPRGLARP SRFCPRIIYA GTSHIRRATA AALLAASLCA LPACADVGVG AALPLSPDKL
     YGELFVAVQT AQVYPDQKTF VDTVPKADPA VILQAYRAQK DVPGFSLKAF VDQYFTVPFE
     TVITPPAGQS LRAHINWLWP ALTRTTATAP DNSSLIPLPK PYVVPGGRFR EVYYWDTYFT
     MLGLQASGRD DLVDSMLDNF AYQINRFGHI PNGNRTYYLS RSQPPFFALM VELAATKEGE
     AAYTRYLAPL RKEYAYWMRG AAGTAPGQAS GNVVVLPDGT VLNRYWDDEA TPRPESYLQD
     VATAQQAPDR PAAEVWRDLR AAAESGWDFS SRWFGDSATL ATIRTTSILP VDLNALMFQL
     EKTIAKGCAV ARDFACTVEF GNHARKRAVA VERYLWHPAG YYADYDWKLG KVRDNLSAAA
     TYPLFVQMAP WGRARQTLRQ TQTALLQVGG LSTTTLHTQQ QWDAPNGWAP LQWIALQASQ
     HYGQALLAQT IGERFLGSVE RLYAAEQKLV EKYIVDGSGT GGGGGEYPLQ DGFGWTNGVT
     LRLLDAYGRG Q