TREA_SALTI
ID TREA_SALTI Reviewed; 570 AA.
AC P59765;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 95.
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=STY1924, t1080;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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. The sequence has been
CC verified by the authors and is believed to be correct. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AE014613; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=AL513382; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL513382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AE014613; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; WP_000612840.1; NZ_LT904887.1.
DR AlphaFoldDB; P59765; -.
DR SMR; P59765; -.
DR OMA; TNGVLIW; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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; Signal.
FT SIGNAL 1..34
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT CHAIN 35..570
FT /note="Putative periplasmic trehalase"
FT /id="PRO_0000012046"
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; 63590 MW; E9485741887C3A1B CRC64;
MIPPEIRRSV LLQKAIKLAL AGTLLTFASF SATAADPSSD TETPQPPDIL LGPLFNDVQN
AKLFPDQKTF ADAIPNSDPL MILADYRMQR NQSGFDLRHF VDVNFTLPKA GEKYVPPAGQ
SLREHIDGLW PVLTRSTKNV EKWDSLLPLP ESYVVPGGRF REIYYWDSYF TMLGLAESGH
WDKVADMVAN FGYEIDAWGY IPNGNRTYYL SRSQPPFFAF MVELLVQHEG DDALKEYLPQ
LQKEYAYWME GVETLQPGQQ NQRVVKLEDG SVLNRYWDDR DTPRPESWVE DIATAKSNPS
RPATEIYRDL RSAAASGWDF SSRWMDNPQQ LSTIRTTTIV PVDLNALLYQ LEKTLARASA
AAGDRAKASQ YDALANARQK AIEMHLWNNK EGWYADYDLQ NNKIRDQLTA AALFPLYVNA
AAKDRAAKVA AAAQAHLLQP GGLATTSVKS GQQWDAPNGW APLQWVAAEG LQNYGQDDVA
MEVTWRFLTN VQHTYDREKK LVEKYDVSST GTGGGGGEYP LQDGFGWSNG VTLKMLDLIC
PQEKPCDSVP STRPASLSAT PTKTPSAATQ
