ID   TREA_ECO57              Reviewed;         561 AA.
AC   Q8XDH7;
DT   03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   03-JUL-2003, sequence version 2.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Putative periplasmic trehalase;
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=Z1968, ECs1701;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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}.
CC   -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG56056.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAB35124.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AE005174; AAG56056.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; BA000007; BAB35124.1; ALT_FRAME; Genomic_DNA.
DR   PIR; D85699; D85699.
DR   PIR; E90841; E90841.
DR   AlphaFoldDB; Q8XDH7; -.
DR   SMR; Q8XDH7; -.
DR   STRING; 155864.EDL933_1900; -.
DR   EnsemblBacteria; AAG56056; AAG56056; Z1968.
DR   EnsemblBacteria; BAB35124; BAB35124; ECs_1701.
DR   KEGG; ece:Z1968; -.
DR   eggNOG; COG1626; Bacteria.
DR   HOGENOM; CLU_006451_3_1_6; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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   5: Uncertain;
KW   Glycosidase; Hydrolase; Periplasm; Reference proteome; Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT   CHAIN           31..561
FT                   /note="Putative periplasmic trehalase"
FT                   /id="PRO_0000012043"
FT   REGION          535..561
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        540..561
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        308
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT   ACT_SITE        492
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT   BINDING         148
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT   BINDING         155..156
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT   BINDING         192
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT   BINDING         201..203
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT   BINDING         273..275
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT   BINDING         306
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT   BINDING         507
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
SQ   SEQUENCE   561 AA;  63272 MW;  937A5DD473B01C4E CRC64;
     MKSPAPSRPQ KMALIPACIF LCFAALSVQA EETPVTPQPP DILLGPLFND VQNAKLFPDQ
     KTFADAVPNS DPLMIRMQQN QSGFDLRHFV NVNFTLPKEG EKYVPPEGQS LREHIDGLWP
     VLTRSTENTE KWDSLLPLPE PYVVPGGRFR EVYYWDSYFT MLGLAESGHW DKVADMVANF
     AHEIDTYGHI PNGNRSYYLS RSQPPFFALM VELLAQHEGD AALKQYLPQM QKEYAYWMDG
     VENLQAGQQE KRVVKLQDGT LLNRYWDDRD TPRPESWVED IATAKSNPNR PATEIYRDLR
     SAAASGWDFS SRWMDNPQQL NTLRTTSIVP VDLNSLMFKM EKILARASKA AGDNAMANQY
     ETLANARQKG IEKYLWNDQQ GWYADYDLKS HKVRNQLTAA ALFPLYVNAA AKDRANKMAT
     ATKTHLLQPG GLNTTSVKSG QQWDAPNGWA PLQWVATEGL QNYGQKEVAM DISWHFLTNV
     QHTYDREKKL VEKYDVSTTG TGGGGGEYPL QDGFGWTNGV TLKMLDLICP KEQPCDNVPA
     TRPLSESTTQ PVKQKEAEPT P