ID   TREA_ECOSM              Reviewed;         565 AA.
AC   B1LHA4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=EcSMS35_1946;
OS   Escherichia coli (strain SMS-3-5 / SECEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=439855;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMS-3-5 / SECEC;
RX   PubMed=18708504; DOI=10.1128/jb.00661-08;
RA   Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA   Ravel J., Stepanauskas R.;
RT   "Insights into the environmental resistance gene pool from the genome
RT   sequence of the multidrug-resistant environmental isolate Escherichia coli
RT   SMS-3-5.";
RL   J. Bacteriol. 190:6779-6794(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   -!- SUBUNIT: Monomer. {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; CP000970; ACB17767.1; -; Genomic_DNA.
DR   RefSeq; WP_000841922.1; NC_010498.1.
DR   AlphaFoldDB; B1LHA4; -.
DR   SMR; B1LHA4; -.
DR   CAZy; GH37; Glycoside Hydrolase Family 37.
DR   EnsemblBacteria; ACB17767; ACB17767; EcSMS35_1946.
DR   KEGG; ecm:EcSMS35_1946; -.
DR   HOGENOM; CLU_006451_3_1_6; -.
DR   OMA; TNGVLIW; -.
DR   Proteomes; UP000007011; 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..30
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT   CHAIN           31..565
FT                   /note="Periplasmic trehalase"
FT                   /id="PRO_1000136422"
FT   REGION          539..565
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        544..565
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        312
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT   ACT_SITE        496
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT   BINDING         152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT   BINDING         159..160
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT   BINDING         196
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT   BINDING         205..207
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT   BINDING         277..279
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT   BINDING         310
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT   BINDING         511
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
SQ   SEQUENCE   565 AA;  63673 MW;  FA8DBBB6861F3E57 CRC64;
     MKSPTPSRPQ KMALIPACIF LCFAALSVQA EETSVTPQPP DILLGPLFND VQNAKLFPDQ
     KTFADAVPNS DPLMILADYR MQQNQSGFDL RHFVNVNFTL PKEGEKYVPP EGQSLREHID
     GLWPVLTRAT ENTEKWDSLL PLPEPYVVPG GRFREVYYWD SYFTMLGLAE SGHWDKVADM
     VANFAHEIDT YGHIPNGNRS YYLSRSQPPF FALMVELLAQ HEGDAALKQY LPQMQKEYAY
     WMDGVENLQA GQQEKRVVKL QDGTLLNRYW DDRDTPRPES WVEDIATAKS NPNRPATEIY
     RDLRSAAASG WDFSSRWMDN PQQLNTLRTT SIVPVDLNSL MFKMEKILAR ASKAAGDNAM
     ANQYETLANA RQKGIEKYLW NDQQGWYADY DLKSHKVRNQ LTAAALFPLY VNAAAKDRAS
     KMATATKTHL LQPGGLNTTS VKSGQQWDAP NGWAPLQWVA TEGLQNYGQK EVAMDISWHF
     LTNVQNTYDR EKKLVEKYDV SATGTGGGGG EYPLQDGFGW TNGVTLKMLD LICPKEQPCD
     NVPATRPLSE STTQPLKQKE AEPTP