ID   TREA_SALPB              Reviewed;         570 AA.
AC   A9MVX4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=SPAB_01423;
OS   Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=1016998;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1250 / SPB7;
RG   The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000886; ABX66830.1; -; Genomic_DNA.
DR   RefSeq; WP_000612826.1; NC_010102.1.
DR   AlphaFoldDB; A9MVX4; -.
DR   SMR; A9MVX4; -.
DR   CAZy; GH37; Glycoside Hydrolase Family 37.
DR   KEGG; spq:SPAB_01423; -.
DR   PATRIC; fig|1016998.12.peg.1342; -.
DR   HOGENOM; CLU_006451_3_1_6; -.
DR   OMA; TNGVLIW; -.
DR   BioCyc; SENT1016998:SPAB_RS05830-MON; -.
DR   Proteomes; UP000008556; 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_1000084459"
FT   REGION          544..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;  63586 MW;  BB50C61E638929CE 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
     AAGDRAKASH YDALANARQQ AIEMHLWNNK EGWYADYDLK NNKIRDQLTA AALFPLYVNA
     AAKDRAAKVA AAAQAHLLQP GGLATTSVKS GQQWDAPNGW APLQWVAAEG LQNYGQDDVA
     MEVTWRFLTN VQHTYDREKK LVEKYDVSST GTGGGGGEYP LQDGFGWTNG VTLKMLDLIC
     PQEKPCDSVP STRPASLSAT PTKTPSAATQ