TREA_ECOLI
ID TREA_ECOLI Reviewed; 565 AA.
AC P13482;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 171.
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 Short=Tre37A;
DE Flags: Precursor;
GN Name=treA {ECO:0000255|HAMAP-Rule:MF_01060}; Synonyms=osmA;
GN OrderedLocusNames=b1197, JW1186;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 31-33 AND 35-43.
RC STRAIN=K12;
RX PubMed=2671658; DOI=10.1007/bf02464903;
RA Gutierrez C., Ardourel M., Bremer E., Middendorf A., Boos W., Ehmann U.;
RT "Analysis and DNA sequence of the osmoregulated treA gene encoding the
RT periplasmic trehalase of Escherichia coli K12.";
RL Mol. Gen. Genet. 217:347-354(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-66.
RC STRAIN=K12;
RX PubMed=1710760; DOI=10.1111/j.1365-2958.1991.tb00745.x;
RA Repoila F., Gutierrez C.;
RT "Osmotic induction of the periplasmic trehalase in Escherichia coli K12:
RT characterization of the treA gene promoter.";
RL Mol. Microbiol. 5:747-755(1991).
RN [6]
RP CHARACTERIZATION.
RC STRAIN=K12;
RX PubMed=2820965; DOI=10.1016/s0021-9258(18)45189-7;
RA Boos W., Ehmann U., Bremer E., Middendorf A., Postma P.;
RT "Trehalase of Escherichia coli. Mapping and cloning of its structural gene
RT and identification of the enzyme as a periplasmic protein induced under
RT high osmolarity growth conditions.";
RL J. Biol. Chem. 262:13212-13218(1987).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 31-565 IN COMPLEXES WITH
RP INHIBITORS, CATALYTIC ACTIVITY, AND PREDICTED ACTIVE SITE.
RC STRAIN=K12;
RX PubMed=17455176; DOI=10.1002/anie.200604825;
RA Gibson R.P., Gloster T.M., Roberts S., Warren R.A., Storch de Gracia I.,
RA Garcia A., Chiara J.L., Davies G.J.;
RT "Molecular basis for trehalase inhibition revealed by the structure of
RT trehalase in complex with potent inhibitors.";
RL Angew. Chem. Int. Ed. Engl. 46:4115-4119(2007).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 31-565 IN COMPLEX WITH INHIBITOR,
RP CATALYTIC ACTIVITY, AND PREDICTED ACTIVE SITE.
RC STRAIN=K12;
RX PubMed=19123216; DOI=10.1002/chem.200801578;
RA Cardona F., Parmeggiani C., Faggi E., Bonaccini C., Gratteri P., Sim L.,
RA Gloster T.M., Roberts S., Davies G.J., Rose D.R., Goti A.;
RT "Total syntheses of casuarine and its 6-O-alpha-glucoside: complementary
RT inhibition towards glycoside hydrolases of the GH31 and GH37 families.";
RL Chemistry 15:1627-1636(2009).
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.
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 ECO:0000269|PubMed:17455176, ECO:0000269|PubMed:19123216};
CC -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:19123216}.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- INDUCTION: By growth at high osmolarity, is regulated by cAMP.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 37 family.
CC {ECO:0000255|HAMAP-Rule:MF_01060}.
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DR EMBL; X15868; CAA33878.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74281.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA36054.1; -; Genomic_DNA.
DR PIR; S04782; S04782.
DR RefSeq; NP_415715.1; NC_000913.3.
DR RefSeq; WP_000841714.1; NZ_SSZK01000010.1.
DR PDB; 2JF4; X-ray; 2.20 A; A=31-565.
DR PDB; 2JG0; X-ray; 1.50 A; A=31-565.
DR PDB; 2JJB; X-ray; 1.90 A; A/B/C/D=31-565.
DR PDB; 2WYN; X-ray; 2.10 A; A/B/C/D=31-565.
DR PDBsum; 2JF4; -.
DR PDBsum; 2JG0; -.
DR PDBsum; 2JJB; -.
DR PDBsum; 2WYN; -.
DR AlphaFoldDB; P13482; -.
DR SMR; P13482; -.
DR BioGRID; 4260095; 135.
DR DIP; DIP-11022N; -.
DR IntAct; P13482; 5.
DR STRING; 511145.b1197; -.
DR CAZy; GH37; Glycoside Hydrolase Family 37.
DR jPOST; P13482; -.
DR PaxDb; P13482; -.
DR PRIDE; P13482; -.
DR EnsemblBacteria; AAC74281; AAC74281; b1197.
DR EnsemblBacteria; BAA36054; BAA36054; BAA36054.
DR GeneID; 945757; -.
DR KEGG; ecj:JW1186; -.
DR KEGG; eco:b1197; -.
DR PATRIC; fig|1411691.4.peg.1089; -.
DR EchoBASE; EB1010; -.
DR eggNOG; COG1626; Bacteria.
DR HOGENOM; CLU_006451_3_1_6; -.
DR InParanoid; P13482; -.
DR OMA; TNGVLIW; -.
DR PhylomeDB; P13482; -.
DR BioCyc; EcoCyc:TREHALAPERI-MON; -.
DR BioCyc; MetaCyc:TREHALAPERI-MON; -.
DR BRENDA; 3.2.1.28; 2026.
DR EvolutionaryTrace; P13482; -.
DR PRO; PR:P13482; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0004555; F:alpha,alpha-trehalase activity; IDA:UniProtKB.
DR GO; GO:0071474; P:cellular hyperosmotic response; IEP:EcoCyc.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0005993; P:trehalose catabolic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Glycosidase; Hydrolase; Periplasm;
KW Reference proteome; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01060,
FT ECO:0000269|PubMed:2671658"
FT CHAIN 31..565
FT /note="Periplasmic trehalase"
FT /id="PRO_0000012041"
FT REGION 538..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 312
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:17455176,
FT ECO:0000305|PubMed:19123216"
FT ACT_SITE 496
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:17455176,
FT ECO:0000305|PubMed:19123216"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 159..160
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 205..207
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 277..279
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 310
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 511
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:2JG0"
FT HELIX 45..53
FT /evidence="ECO:0007829|PDB:2JG0"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:2JG0"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:2JG0"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:2JG0"
FT HELIX 72..82
FT /evidence="ECO:0007829|PDB:2JG0"
FT HELIX 90..97
FT /evidence="ECO:0007829|PDB:2JG0"
FT HELIX 115..122
FT /evidence="ECO:0007829|PDB:2JG0"
FT TURN 123..126
FT /evidence="ECO:0007829|PDB:2JG0"
FT HELIX 158..170
FT /evidence="ECO:0007829|PDB:2JG0"
FT HELIX 174..191
FT /evidence="ECO:0007829|PDB:2JG0"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:2JG0"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:2JG0"
FT HELIX 211..222
FT /evidence="ECO:0007829|PDB:2JG0"
FT HELIX 224..241
FT /evidence="ECO:0007829|PDB:2JG0"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:2JG0"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:2JJB"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:2JG0"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:2JG0"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:2JG0"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:2JG0"
FT HELIX 281..289
FT /evidence="ECO:0007829|PDB:2JG0"
FT HELIX 296..308
FT /evidence="ECO:0007829|PDB:2JG0"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:2JG0"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:2JG0"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:2JG0"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:2JG0"
FT HELIX 335..355
FT /evidence="ECO:0007829|PDB:2JG0"
FT HELIX 358..378
FT /evidence="ECO:0007829|PDB:2JG0"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:2JG0"
FT TURN 382..385
FT /evidence="ECO:0007829|PDB:2JG0"
FT TURN 392..395
FT /evidence="ECO:0007829|PDB:2JG0"
FT HELIX 403..406
FT /evidence="ECO:0007829|PDB:2JG0"
FT HELIX 407..410
FT /evidence="ECO:0007829|PDB:2JG0"
FT HELIX 416..429
FT /evidence="ECO:0007829|PDB:2JG0"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:2JG0"
FT STRAND 444..448
FT /evidence="ECO:0007829|PDB:2JG0"
FT HELIX 454..465
FT /evidence="ECO:0007829|PDB:2JG0"
FT TURN 466..468
FT /evidence="ECO:0007829|PDB:2JG0"
FT HELIX 470..491
FT /evidence="ECO:0007829|PDB:2JG0"
FT STRAND 492..496
FT /evidence="ECO:0007829|PDB:2JF4"
FT STRAND 502..504
FT /evidence="ECO:0007829|PDB:2JG0"
FT STRAND 510..512
FT /evidence="ECO:0007829|PDB:2JG0"
FT HELIX 519..532
FT /evidence="ECO:0007829|PDB:2JG0"
FT STRAND 535..537
FT /evidence="ECO:0007829|PDB:2JG0"
SQ SEQUENCE 565 AA; 63637 MW; 4885D7556A3C0781 CRC64;
MKSPAPSRPQ KMALIPACIF LCFAALSVQA EETPVTPQPP DILLGPLFND VQNAKLFPDQ
KTFADAVPNS DPLMILADYR MQQNQSGFDL RHFVNVNFTL PKEGEKYVPP EGQSLREHID
GLWPVLTRST ENTEKWDSLL PLPEPYVVPG GRFREVYYWD SYFTMLGLAE SGHWDKVADM
VANFAHEIDT YGHIPNGNRS YYLSRSQPPF FALMVELLAQ HEGDAALKQY LPQMQKEYAY
WMDGVENLQA GQQEKRVVKL QDGTLLNRYW DDRDTPRPES WVEDIATAKS NPNRPATEIY
RDLRSAAASG WDFSSRWMDN PQQLNTLRTT SIVPVDLNSL MFKMEKILAR ASKAAGDNAM
ANQYETLANA RQKGIEKYLW NDQQGWYADY DLKSHKVRNQ LTAAALFPLY VNAAAKDRAN
KMATATKTHL LQPGGLNTTS VKSGQQWDAP NGWAPLQWVA TEGLQNYGQK EVAMDISWHF
LTNVQHTYDR EKKLVEKYDV STTGTGGGGG EYPLQDGFGW TNGVTLKMLD LICPKEQPCD
NVPATRPTVK SATTQPSTKE AQPTP
