ID E6WBA5_PANSA Unreviewed; 560 AA.
AC E6WBA5;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Periplasmic trehalase {ECO:0000256|HAMAP-Rule:MF_01060};
DE EC=3.2.1.28 {ECO:0000256|HAMAP-Rule:MF_01060};
DE AltName: Full=Alpha,alpha-trehalase {ECO:0000256|HAMAP-Rule:MF_01060};
DE AltName: Full=Alpha,alpha-trehalose glucohydrolase {ECO:0000256|HAMAP-Rule:MF_01060};
DE Flags: Precursor;
GN Name=treA {ECO:0000256|HAMAP-Rule:MF_01060};
GN OrderedLocusNames=Pat9b_1557 {ECO:0000313|EMBL:ADU68874.1};
OS Pantoea sp. (strain At-9b).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=592316 {ECO:0000313|EMBL:ADU68874.1, ECO:0000313|Proteomes:UP000001624};
RN [1] {ECO:0000313|EMBL:ADU68874.1, ECO:0000313|Proteomes:UP000001624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=At-9b {ECO:0000313|EMBL:ADU68874.1,
RC ECO:0000313|Proteomes:UP000001624};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pinto A., Currie C., Woyke T.;
RT "Complete sequence chromosome of Pantoea sp. At-9b.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|ARBA:ARBA00001576, ECO:0000256|HAMAP-
CC Rule:MF_01060};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01060}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|HAMAP-Rule:MF_01060}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 37 family.
CC {ECO:0000256|HAMAP-Rule:MF_01060}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01060}.
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DR EMBL; CP002433; ADU68874.1; -; Genomic_DNA.
DR RefSeq; WP_013508735.1; NC_014837.1.
DR AlphaFoldDB; E6WBA5; -.
DR STRING; 592316.Pat9b_1557; -.
DR KEGG; pao:Pat9b_1557; -.
DR eggNOG; COG1626; Bacteria.
DR HOGENOM; CLU_006451_3_1_6; -.
DR OrthoDB; 106887at2; -.
DR Proteomes; UP000001624; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004555; F:alpha,alpha-trehalase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071474; P:cellular hyperosmotic response; IEA:InterPro.
DR GO; GO:0005993; P:trehalose catabolic process; IEA:InterPro.
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; TREHALASE; 1.
DR PANTHER; PTHR23403:SF1; TREHALASE; 1.
DR Pfam; PF01204; Trehalase; 1.
DR PRINTS; PR00744; GLHYDRLASE37.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR PROSITE; PS00927; TREHALASE_1; 1.
DR PROSITE; PS00928; TREHALASE_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|HAMAP-
KW Rule:MF_01060};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01060};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|HAMAP-Rule:MF_01060};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_01060}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01060"
FT CHAIN 30..560
FT /note="Periplasmic trehalase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01060"
FT /id="PRO_5009010960"
FT ACT_SITE 315
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01060"
FT ACT_SITE 499
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01060"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01060"
FT BINDING 162..163
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01060"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01060"
FT BINDING 208..210
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01060"
FT BINDING 313
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01060"
FT BINDING 515
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01060"
SQ SEQUENCE 560 AA; 63360 MW; 48E05B4C58ACC800 CRC64;
MIKNVVFTPG HLRLLLSTAL LMGSAVAHAE DNGRMLNNPP QPPDVRLGPL FNAVQQAKFY
PDQKTFADAV PNYNPASILA DWQMQKSQRN FDLKHFVDAN FTLPKQQDKY VPPAGQSLRA
HIDGLWPVLT RSTPQTSQYD SLLPLPKPYV VPGGRFREVY YWDSYFTMLG LAESGHWDRV
QDMVDNFASE LDRYGHIPNG NRSYYLSRSQ PPFFSLMIDL LATHDGDSVY THYLPQLQKE
YDYWMADSDK VPAGQASKRV IKLSDGTLLN RYWDERDVPR TESWLDDVNT AKKATQRDKA
QVYRDLRAGA ASGWDFSSRW FSDAHNLATI RTTQLAPVDL NSLLFHLEQT LAKAEKLAHH
DQQAQQWAAK AETRQAAINR YLWNAQQGWY ADYNWQKKQV QPQLTAAALF PLYMQLASDK
QAERTAAAVE KQLLKPGGLV TTTVNNGQQW DAPNGWAPLQ WVAVTGLEHY KQPQLAQQIG
QRFLQNVQMT YDKEHKLVEK YVVEGAKLGG GGGGEYPLQD GFGWTNGVTL MLLDKYCPKE
KTCASAHDIP NMPTLTAAQP
//
