TREA_ECO55
ID TREA_ECO55 Reviewed; 565 AA.
AC B7LGV7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, 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=EC55989_1293;
OS Escherichia coli (strain 55989 / EAEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585055;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=55989 / EAEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928145; CAU97151.1; -; Genomic_DNA.
DR RefSeq; WP_000841700.1; NC_011748.1.
DR AlphaFoldDB; B7LGV7; -.
DR SMR; B7LGV7; -.
DR CAZy; GH37; Glycoside Hydrolase Family 37.
DR EnsemblBacteria; CAU97151; CAU97151; EC55989_1293.
DR KEGG; eck:EC55989_1293; -.
DR HOGENOM; CLU_006451_3_1_6; -.
DR OMA; TNGVLIW; -.
DR Proteomes; UP000000746; 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_1000149684"
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; 63669 MW; 4885D0E37A3C0781 CRC64;
MKSPAPSRPQ KMALIPACIF LCFAALSVQA EETPVTPQPP DILLGPLFND VQNAKLFPDQ
KTFADAMPNS 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
