(data stored in SCRATCH zone)

SWISSPROT: TREA_SALPA

ID   TREA_SALPA              Reviewed;         570 AA.
AC   Q5PI73;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   11-DEC-2019, entry version 75.
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=SPA1077;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
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}.
DR   EMBL; CP000026; AAV77047.1; -; Genomic_DNA.
DR   RefSeq; WP_000612832.1; NC_006511.1.
DR   SMR; Q5PI73; -.
DR   CAZy; GH37; Glycoside Hydrolase Family 37.
DR   PRIDE; Q5PI73; -.
DR   EnsemblBacteria; AAV77047; AAV77047; SPA1077.
DR   KEGG; spt:SPA1077; -.
DR   HOGENOM; HOG000215464; -.
DR   KO; K01194; -.
DR   OMA; DQPNVWP; -.
DR   BioCyc; SENT295319:G1G44-1133-MONOMER; -.
DR   Proteomes; UP000008185; 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;
DR   PRODOM; Q5PI73.
DR   SWISS-2DPAGE; Q5PI73.
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_1000064456"
FT   REGION          166..167
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT   REGION          212..214
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT   REGION          284..286
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
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                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT   BINDING         203
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT   BINDING         317
FT                   /note="Substrate; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT   BINDING         518
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
SQ   SEQUENCE   570 AA;  63605 MW;  AFC29D479C732FA3 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 NNKIRDQLTA AALFPLYVNA
     AAKDRAVKVA AAAQAHLLQP GGLATTSVKS GQQWDAPNGW APLQWVAAEG LQNYGQDDVA
     MEVTWRFLTN VQHTYDREKK LVEKYDVSST GTGGGGGEYP LQDGFGWTNG VTLKMLDLIC
     PQEKPCDSVP STRPASLSAT PTKTPSAATQ
//

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