TREA_PSEAE
ID TREA_PSEAE Reviewed; 545 AA.
AC Q9I165;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=PA2416;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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 -!- 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE004091; AAG05804.1; -; Genomic_DNA.
DR PIR; H83342; H83342.
DR RefSeq; NP_251106.1; NC_002516.2.
DR RefSeq; WP_010895614.1; NZ_QZGE01000027.1.
DR AlphaFoldDB; Q9I165; -.
DR SMR; Q9I165; -.
DR STRING; 287.DR97_6017; -.
DR CAZy; GH37; Glycoside Hydrolase Family 37.
DR PaxDb; Q9I165; -.
DR PRIDE; Q9I165; -.
DR EnsemblBacteria; AAG05804; AAG05804; PA2416.
DR GeneID; 882861; -.
DR KEGG; pae:PA2416; -.
DR PATRIC; fig|208964.12.peg.2526; -.
DR PseudoCAP; PA2416; -.
DR HOGENOM; CLU_006451_3_1_6; -.
DR InParanoid; Q9I165; -.
DR OMA; TNGVLIW; -.
DR PhylomeDB; Q9I165; -.
DR BioCyc; PAER208964:G1FZ6-2453-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004555; F:alpha,alpha-trehalase activity; IBA:GO_Central.
DR GO; GO:0015927; F:trehalase activity; IMP:PseudoCAP.
DR GO; GO:0044248; P:cellular catabolic process; IMP:PseudoCAP.
DR GO; GO:0071474; P:cellular hyperosmotic response; IEA:InterPro.
DR GO; GO:0005993; P:trehalose catabolic process; IBA:GO_Central.
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;
KW Glycosidase; Hydrolase; Periplasm; Reference proteome; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT CHAIN 31..545
FT /note="Periplasmic trehalase"
FT /id="PRO_0000012044"
FT ACT_SITE 320
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 160
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT BINDING 167..168
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT BINDING 213..215
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT BINDING 285..287
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT BINDING 318
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
FT BINDING 518
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01060"
SQ SEQUENCE 545 AA; 61166 MW; 57790CC7AD797C4F CRC64;
MPDRTALPRA MLAAWVLLLL AACSQGPAPT PPASWGWQDA SGERAIAPDE AYPELFQAVQ
ENRLFSDQKH FVDALPLREP ARIRADYLRE RERPGFDLRA FVGRNFEESG SVETAPPEAG
ADLASHISDL WPALTRHYEQ VPAHSSLLPL PKPYVVPGGR FREVYYWDSY FTMLGLAESG
QHQRVRDMLD NFAYLIDTYG HIPNGNRSYY LSRSQPPFFA YMVDLQARRE GDAAYRRYLP
QLQKEYAYWM EGSAGLRPNE ARLHVVKLAD GSLLNRYWDN RDTPRQESFL EDRATAARAP
QRPAGEVYRD LRAGAESGWD FSSRWLDDGR ELASIRTTAI VPVDLNALLY HLERIIAKAC
ASSALKACEQ GYGARAEKRR QAIEDHLWHP AGYYADYDWQ RRRPIERINA ASLFPLFTGL
ASAERAGRTA DSVAAQLLRP GGLATTTRAS GQQWDEPNGW APLQWVAVQG LRAYGRDALA
EDIGRRFLAQ VQQVYDREGK LVEKYDISGN QGGGGGGEYP LQDGFGWSNG VTLQLLRLYG
PGAGR
