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Database: UniProt/TrEMBL
Entry: B2JMW7_BURP8
LinkDB: B2JMW7_BURP8
Original site: B2JMW7_BURP8 
ID   B2JMW7_BURP8            Unreviewed;       574 AA.
AC   B2JMW7;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   19-FEB-2014, entry version 32.
DE   RecName: Full=Periplasmic trehalase;
DE            EC=3.2.1.28;
DE   AltName: Full=Alpha,alpha-trehalase;
DE   AltName: Full=Alpha,alpha-trehalose glucohydrolase;
DE   Flags: Precursor;
GN   Name=treA; OrderedLocusNames=Bphy_5280;
OS   Burkholderia phymatum (strain DSM 17167 / STM815).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=391038;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17167 / STM815;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Bruce D.,
RA   Goodwin L., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA   Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Bacher J., Blanchard J., Cohan F.,
RA   James E., Lawrence J., Lizotte-Waniewski M., Moulin L., Rainey P.,
RA   Riley M., Souza V., Wertz J., Young P.;
RT   "Complete sequence of chromosome 2 of Burkholderia phymatum STM815.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Provides the cells with the ability to utilize trehalose
CC       at high osmolarity by splitting it into glucose molecules that can
CC       subsequently be taken up by the phosphotransferase-mediated uptake
CC       system (By similarity).
CC   -!- CATALYTIC ACTIVITY: Alpha,alpha-trehalose + H(2)O = beta-D-glucose
CC       + alpha-D-glucose.
CC   -!- SUBCELLULAR LOCATION: Periplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 37 family.
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DR   EMBL; CP001044; ACC74360.1; -; Genomic_DNA.
DR   RefSeq; YP_001861406.1; NC_010623.1.
DR   ProteinModelPortal; B2JMW7; -.
DR   SMR; B2JMW7; 76-573.
DR   STRING; 391038.Bphy_5280; -.
DR   CAZy; GH37; Glycoside Hydrolase Family 37.
DR   EnsemblBacteria; ACC74360; ACC74360; Bphy_5280.
DR   GeneID; 6246767; -.
DR   KEGG; bph:Bphy_5280; -.
DR   PATRIC; 19197344; VBIBurPhy25146_5553.
DR   eggNOG; COG1626; -.
DR   HOGENOM; HOG000215464; -.
DR   KO; K01194; -.
DR   OMA; PPFFSLM; -.
DR   OrthoDB; EOG6CCH1S; -.
DR   ProtClustDB; CLSK897717; -.
DR   BioCyc; BPHY391038:GI4Z-5358-MONOMER; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004555; F:alpha,alpha-trehalase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0071474; P:cellular hyperosmotic response; IEA:InterPro.
DR   GO; GO:0005993; P:trehalose catabolic process; IEA:InterPro.
DR   HAMAP; MF_01060; Peripl_trehalase; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase-like.
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   Complete proteome; Glycosidase; Hydrolase; Periplasm; Signal.
FT   SIGNAL        1     13       By similarity.
FT   REGION      197    198       Substrate binding (By similarity).
FT   REGION      243    245       Substrate binding (By similarity).
FT   ACT_SITE    350    350       Proton donor/acceptor (By similarity).
FT   ACT_SITE    533    533       Proton donor/acceptor (By similarity).
FT   BINDING     190    190       Substrate (By similarity).
FT   BINDING     234    234       Substrate (By similarity).
FT   BINDING     348    348       Substrate; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING     549    549       Substrate (By similarity).
SQ   SEQUENCE   574 AA;  64135 MW;  A80C0F4362C84218 CRC64;
     MRTLSLSCMR SWTVETNHPT AVSSQSMQRA APLYAPPMRR RHAARAAALS GIVLFAGFAG
     SALIANADTQ VGSALPPPPD QLYGDLFVAV QTQQIYPDQK TFVDALPKTD PTTILQAYDA
     QKNQANFSLK AFVDQYFTAP SEPIITPPAN QSLRDHINWL WPELTRTTTS VPSYSSLIPM
     PKAYVVPGGR FREGYYWDTY FTMLGLQESG HEDLVDNMLD NFAYMIDTYG HIPNGNRTYY
     LSRSQPPFFS YMVELAAKVE GGRVYQKYLP QMRKEYAYWM QGASSTKPGE ATRNVVVLPD
     RTVLNRYWDE LDTPRDESYL EDVQTAQKAT GRAPNEVYRD LRATAESGWD FSSRWFGDNA
     NLTTVRTTSI IPVDLNSLMF HLETTIARGC SEARDFSCVV QFIGKAGKRA EGINRYLWNS
     KGYYGDYDWK LAKPRDNQTP AMLYPLFAGA AWPDRAHKTA NVVAAVLLEP GGLTTSTYDT
     TQQWDAPNGW APLHWVAIEG LRRYGRSDLA QQIGTRFLAD VKNVYAKEQK LVEKYVVEGS
     GTGGGGGGEY PLQDGFGWTN GVTLKLLDLY APGE
//
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