(data stored in SCRATCH zone)

HOGENOM: SAENT4_1_PE1008

ID   SAENT4_1_PE1008                      STANDARD;      PRT;   570 AA.
AC   SAENT4_1_PE1008; Q5PI73;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Periplasmic trehalase; EC=3.2.1 28;AltName:
DE   Full=Alpha,alpha-trehalase;AltName: Full=Alpha,alpha-trehalose
DE   glucohydrolase;Flags: Precursor; (SAENT4_1.PE1008).
GN   Name=treA; OrderedLocusNames=SPA1077;
OS   SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR PARATYPHI A STR. ATCC 9150.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS SAENT4_1.PE1008.
CC       Salmonella enterica subsp. enterica serovar Paratyphi A str. ATCC 9150
CC       chromosome, complete genome.
CC   -!- ANNOTATIONS ORIGIN:TREA_SALPA
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 = 2 D-glucose.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Periplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 37 family.
CC   -!- GENE_FAMILY: HOG000215464 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q5PI73; -.
DR   EMBL; CP000026; AAV77047.1; -; Genomic_DNA.
DR   RefSeq; YP_150359.1; NC_006511.1.
DR   ProteinModelPortal; Q5PI73; -.
DR   SMR; Q5PI73; 44-554.
DR   GeneID; 3178027; -.
DR   GenomeReviews; CP000026_GR; SPA1077.
DR   KEGG; spt:SPA1077; -.
DR   NMPDR; fig|295319.3.peg.1760; -.
DR   OMA; NRYWDAS; -.
DR   ProtClustDB; PRK13271; -.
DR   BioCyc; SENT295319:SPA1077-MON; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004555; F:alpha,alpha-trehalase activity; IEA:EC.
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; Glyco_hydro_37; 1.
DR   Pfam; PF01204; Trehalase; 1.
DR   PRINTS; PR00744; GLHYDRLASE37.
DR   SUPFAM; SSF48208; Glyco_trans_6hp; 1.
DR   PROSITE; PS00927; TREHALASE_1; 1.
DR   PROSITE; PS00928; TREHALASE_2; 1.
DR   HOGENOMDNA; SAENT4_1.PE1008; -.
KW   Complete proteome; Glycosidase; Hydrolase; Periplasm; Signal.
SQ   SEQUENCE   570 AA;  UNKNOWN MW;  UNKNOWN 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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