ID   TREA_ECOLC              Reviewed;         565 AA.
AC   B1IU96;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=EcolC_2429;
OS   Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 /
OS   WDCM 00012 / Crooks).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=481805;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Ingram L., Richardson P.;
RT   "Complete sequence of Escherichia coli C str. ATCC 8739.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000946; ACA78063.1; -; Genomic_DNA.
DR   RefSeq; WP_000841714.1; NZ_CP022959.1.
DR   AlphaFoldDB; B1IU96; -.
DR   SMR; B1IU96; -.
DR   CAZy; GH37; Glycoside Hydrolase Family 37.
DR   KEGG; ecl:EcolC_2429; -.
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..30
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT   CHAIN           31..565
FT                   /note="Periplasmic trehalase"
FT                   /id="PRO_5000313992"
FT   REGION          538..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;  63637 MW;  4885D7556A3C0781 CRC64;
     MKSPAPSRPQ KMALIPACIF LCFAALSVQA EETPVTPQPP DILLGPLFND VQNAKLFPDQ
     KTFADAVPNS DPLMILADYR MQQNQSGFDL RHFVNVNFTL PKEGEKYVPP EGQSLREHID
     GLWPVLTRST 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 VNAAAKDRAN
     KMATATKTHL LQPGGLNTTS VKSGQQWDAP NGWAPLQWVA TEGLQNYGQK EVAMDISWHF
     LTNVQHTYDR EKKLVEKYDV STTGTGGGGG EYPLQDGFGW TNGVTLKMLD LICPKEQPCD
     NVPATRPTVK SATTQPSTKE AQPTP