TREA_SALA4
ID TREA_SALA4 Reviewed; 570 AA.
AC B5F4F0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 66.
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=SeAg_B1337;
OS Salmonella agona (strain SL483).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=454166;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SL483;
RX PubMed=21602358; DOI=10.1128/jb.00297-11;
RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA Leclerc J.E., Ravel J., Cebula T.A.;
RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT CRISPR-mediated adaptive sublineage evolution.";
RL J. Bacteriol. 193:3556-3568(2011).
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; CP001138; ACH51939.1; -; Genomic_DNA.
DR RefSeq; WP_000612835.1; NC_011149.1.
DR AlphaFoldDB; B5F4F0; -.
DR SMR; B5F4F0; -.
DR CAZy; GH37; Glycoside Hydrolase Family 37.
DR EnsemblBacteria; ACH51939; ACH51939; SeAg_B1337.
DR KEGG; sea:SeAg_B1337; -.
DR HOGENOM; CLU_006451_3_1_6; -.
DR OMA; TNGVLIW; -.
DR Proteomes; UP000008819; 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..34
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT CHAIN 35..570
FT /note="Periplasmic trehalase"
FT /id="PRO_1000136423"
FT REGION 545..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 319
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT ACT_SITE 503
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT BINDING 166..167
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT BINDING 212..214
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT BINDING 284..286
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT BINDING 317
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT BINDING 518
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
SQ SEQUENCE 570 AA; 63576 MW; 0B6F223F38CFD495 CRC64;
MIPPEIRRSV LLQKAIKLAL AGTLLTFASF SATAADPSSD TETPQPPDIL LGPLFNDVQN
AKLFPDQKTF ADAIPNSDPL MILADYRMQR NQSGFDLRHF VDVNFTLPKA GEKYVPPAGQ
SLREHIDGLW PVLTRSTKNV EKWDSLLPLP ESYVVPGGRF REIYYWDSYF TMLGLAESGH
WDKVADMVAN FGYEIDAWGH IPNGNRTYYL SRSQPPFFAF MVELLAQHEG DDALKEYLPQ
LQKEYAYWME GVETLQPGQQ NQRVVKLEDG SVLNRYWDDR DTPRPESWVE DIATAKSNPN
RPATEIYRDL RSAAASGWDF SSRWMDNPQQ LSTIRTTTIV PVDLNALLYQ LEKTLARASA
AAGDRAKASQ YDALANARQK AIEMHLWNNK EGWYADYDLQ NNKIRNQLTA AALFPLYVNA
AAKDRAAKVA AAAQAHLLQP GGLATTSVKS GQQWDAPNGW APLQWVAAEG LQNYGQDDVA
MEVTWRFLTN VQHTYDREKK LVEKYDVSST GTGGGGGEYP LQDGFGWTNG VTLKMLDLIC
PQEKPCDSVP STRPASLSAT PTKTPSAATQ