TREF_ECOLI
ID TREF_ECOLI Reviewed; 549 AA.
AC P62601; P37196; Q2M7I1;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Cytoplasmic trehalase {ECO:0000255|HAMAP-Rule:MF_01059};
DE EC=3.2.1.28 {ECO:0000255|HAMAP-Rule:MF_01059};
DE AltName: Full=Alpha,alpha-trehalase {ECO:0000255|HAMAP-Rule:MF_01059};
DE AltName: Full=Alpha,alpha-trehalose glucohydrolase {ECO:0000255|HAMAP-Rule:MF_01059};
GN Name=treF {ECO:0000255|HAMAP-Rule:MF_01059};
GN OrderedLocusNames=b3519, JW3487;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP CHARACTERIZATION, AND PROTEIN SEQUENCE OF N-TERMINUS.
RC STRAIN=DHB4, and K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=8892826; DOI=10.1128/jb.178.21.6250-6257.1996;
RA Horlacher R., Uhland K., Klein W., Ehrmann M., Boos W.;
RT "Characterization of a cytoplasmic trehalase of Escherichia coli.";
RL J. Bacteriol. 178:6250-6257(1996).
RN [5]
RP SUBCELLULAR LOCATION.
RC STRAIN=DHB3, and K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=10816581; DOI=10.1074/jbc.m002793200;
RA Uhland K., Mondigler M., Spiess C., Prinz W., Ehrmann M.;
RT "Determinants of translocation and folding of TreF, a trehalase of
RT Escherichia coli.";
RL J. Biol. Chem. 275:23439-23445(2000).
CC -!- FUNCTION: Hydrolyzes trehalose to glucose. Could be involved, in cells
CC returning to low osmolarity conditions, in the utilization of the
CC accumulated cytoplasmic trehalose, which was synthesized in response to
CC high osmolarity.
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_01059};
CC -!- ACTIVITY REGULATION: Activity decreases with increasing salt
CC concentrations.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.0.;
CC -!- PATHWAY: Glycan degradation; trehalose degradation; D-glucose from
CC alpha,alpha-trehalose: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01059}.
CC -!- SUBUNIT: Monomer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01059,
CC ECO:0000269|PubMed:10816581}.
CC -!- INDUCTION: Weakly induced by high osmolarity but not by trehalose.
CC Expression is partially dependent on RpoS.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 37 family.
CC {ECO:0000255|HAMAP-Rule:MF_01059}.
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DR EMBL; U00039; AAB18495.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76544.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77775.1; -; Genomic_DNA.
DR PIR; S47739; S47739.
DR RefSeq; NP_417976.1; NC_000913.3.
DR RefSeq; WP_000934216.1; NZ_SSZK01000039.1.
DR AlphaFoldDB; P62601; -.
DR SMR; P62601; -.
DR BioGRID; 4260775; 13.
DR IntAct; P62601; 2.
DR STRING; 511145.b3519; -.
DR jPOST; P62601; -.
DR PaxDb; P62601; -.
DR PRIDE; P62601; -.
DR EnsemblBacteria; AAC76544; AAC76544; b3519.
DR EnsemblBacteria; BAE77775; BAE77775; BAE77775.
DR GeneID; 58462844; -.
DR GeneID; 948037; -.
DR KEGG; ecj:JW3487; -.
DR KEGG; eco:b3519; -.
DR PATRIC; fig|1411691.4.peg.3199; -.
DR EchoBASE; EB2156; -.
DR eggNOG; COG1626; Bacteria.
DR HOGENOM; CLU_006451_3_1_6; -.
DR InParanoid; P62601; -.
DR OMA; DAPFGWA; -.
DR PhylomeDB; P62601; -.
DR BioCyc; EcoCyc:TREHALACYTO-MON; -.
DR BioCyc; MetaCyc:TREHALACYTO-MON; -.
DR UniPathway; UPA00300; UER00535.
DR PRO; PR:P62601; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004555; F:alpha,alpha-trehalase activity; IDA:EcoCyc.
DR GO; GO:0071474; P:cellular hyperosmotic response; IEP:EcoCyc.
DR GO; GO:0005993; P:trehalose catabolic process; IMP:EcoCyc.
DR Gene3D; 1.50.10.10; -; 1.
DR HAMAP; MF_01059; Cyt_trehalase; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR023715; Cyt_trehalase.
DR InterPro; IPR001661; Glyco_hydro_37.
DR InterPro; IPR018232; Glyco_hydro_37_CS.
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 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Glycosidase; Hydrolase;
KW Reference proteome.
FT CHAIN 1..549
FT /note="Cytoplasmic trehalase"
FT /id="PRO_0000173786"
FT ACT_SITE 326
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01059"
FT ACT_SITE 509
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01059"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01059"
FT BINDING 175..176
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01059"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01059"
FT BINDING 221..223
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01059"
FT BINDING 292..294
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01059"
FT BINDING 324
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01059"
FT BINDING 525
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01059"
SQ SEQUENCE 549 AA; 63697 MW; 543B82A7FAD4CB9D CRC64;
MLNQKIQNPN PDELMIEVDL CYELDPYELK LDEMIEAEPE PEMIEGLPAS DALTPADRYL
ELFEHVQSAK IFPDSKTFPD CAPKMDPLDI LIRYRKVRRH RDFDLRKFVE NHFWLPEVYS
SEYVSDPQNS LKEHIDQLWP VLTREPQDHI PWSSLLALPQ SYIVPGGRFS ETYYWDSYFT
MLGLAESGRE DLLKCMADNF AWMIENYGHI PNGNRTYYLS RSQPPVFALM VELFEEDGVR
GARRYLDHLK MEYAFWMDGA ESLIPNQAYR HVVRMPDGSL LNRYWDDRDT PRDESWLEDV
ETAKHSGRPP NEVYRDLRAG AASGWDYSSR WLRDTGRLAS IRTTQFIPID LNAFLFKLES
AIANISALKG EKETEALFRQ KASARRDAVN RYLWDDENGI YRDYDWRREQ LALFSAAAIV
PLYVGMANHE QADRLANAVR SRLLTPGGIL ASEYETGEQW DKPNGWAPLQ WMAIQGFKMY
GDDLLGDEIA RSWLKTVNQF YLEQHKLIEK YHIADGVPRE GGGGEYPLQD GFGWTNGVVR
RLIGLYGEP
