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Protein

Periplasmic trehalase

Gene

treA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Provides the cells with the ability to utilize trehalose at high osmolarity by splitting it into glucose molecules that can subsequently be taken up by the phosphotransferase-mediated uptake system.

Catalytic activityi

Alpha,alpha-trehalose + H2O = beta-D-glucose + alpha-D-glucose.UniRule annotation2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei152SubstrateCurated1
Binding sitei196SubstrateCurated1
Binding sitei310Substrate; via carbonyl oxygenCurated1
Active sitei312Proton donor/acceptorUniRule annotation1
Active sitei496Proton donor/acceptorUniRule annotation1
Binding sitei511SubstrateCurated1

GO - Molecular functioni

  • alpha,alpha-trehalase activity Source: UniProtKB

GO - Biological processi

  • cellular hyperosmotic response Source: EcoCyc
  • cellular response to DNA damage stimulus Source: EcoliWiki
  • trehalose catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BioCyciEcoCyc:TREHALAPERI-MONOMER.
ECOL316407:JW1186-MONOMER.
MetaCyc:TREHALAPERI-MONOMER.
BRENDAi3.2.1.28. 2026.

Protein family/group databases

CAZyiGH37. Glycoside Hydrolase Family 37.

Names & Taxonomyi

Protein namesi
Recommended name:
Periplasmic trehalaseUniRule annotation (EC:3.2.1.28UniRule annotation)
Alternative name(s):
Alpha,alpha-trehalaseUniRule annotation
Alpha,alpha-trehalose glucohydrolaseUniRule annotation
Short name:
Tre37A
Gene namesi
Name:treAUniRule annotation
Synonyms:osmA
Ordered Locus Names:b1197, JW1186
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11017. treA.

Subcellular locationi

GO - Cellular componenti

  • outer membrane-bounded periplasmic space Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 30UniRule annotation1 PublicationAdd BLAST30
ChainiPRO_000001204131 – 565Periplasmic trehalaseAdd BLAST535

Proteomic databases

EPDiP13482.
PaxDbiP13482.
PRIDEiP13482.

Expressioni

Inductioni

By growth at high osmolarity, is regulated by cAMP.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi4260095. 121 interactors.
DIPiDIP-11022N.
IntActiP13482. 5 interactors.
STRINGi511145.b1197.

Structurei

Secondary structure

1565
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi40 – 43Combined sources4
Helixi45 – 53Combined sources9
Beta strandi57 – 59Combined sources3
Helixi61 – 64Combined sources4
Beta strandi67 – 70Combined sources4
Helixi72 – 82Combined sources11
Helixi90 – 97Combined sources8
Helixi115 – 122Combined sources8
Turni123 – 126Combined sources4
Helixi158 – 170Combined sources13
Helixi174 – 191Combined sources18
Beta strandi196 – 199Combined sources4
Helixi200 – 202Combined sources3
Helixi211 – 222Combined sources12
Helixi224 – 241Combined sources18
Turni242 – 244Combined sources3
Helixi245 – 247Combined sources3
Beta strandi252 – 254Combined sources3
Beta strandi257 – 259Combined sources3
Beta strandi265 – 267Combined sources3
Helixi278 – 280Combined sources3
Helixi281 – 289Combined sources9
Helixi296 – 308Combined sources13
Helixi315 – 317Combined sources3
Beta strandi318 – 320Combined sources3
Helixi324 – 326Combined sources3
Helixi329 – 331Combined sources3
Helixi335 – 355Combined sources21
Helixi358 – 378Combined sources21
Beta strandi379 – 381Combined sources3
Turni382 – 385Combined sources4
Turni392 – 395Combined sources4
Helixi403 – 406Combined sources4
Helixi407 – 410Combined sources4
Helixi416 – 429Combined sources14
Beta strandi438 – 440Combined sources3
Beta strandi444 – 448Combined sources5
Helixi454 – 465Combined sources12
Turni466 – 468Combined sources3
Helixi470 – 491Combined sources22
Beta strandi492 – 496Combined sources5
Beta strandi502 – 504Combined sources3
Beta strandi510 – 512Combined sources3
Helixi519 – 532Combined sources14
Beta strandi535 – 537Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JF4X-ray2.20A31-565[»]
2JG0X-ray1.50A31-565[»]
2JJBX-ray1.90A/B/C/D31-565[»]
2WYNX-ray2.10A/B/C/D31-565[»]
ProteinModelPortaliP13482.
SMRiP13482.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13482.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni159 – 160Substrate bindingCurated2
Regioni205 – 207Substrate bindingCurated3
Regioni277 – 279Substrate bindingCurated3

Sequence similaritiesi

Belongs to the glycosyl hydrolase 37 family.UniRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105E53. Bacteria.
COG1626. LUCA.
HOGENOMiHOG000215464.
InParanoidiP13482.
KOiK01194.
OMAiWAGQLHQ.
PhylomeDBiP13482.

Family and domain databases

HAMAPiMF_01060. Peripl_trehalase. 1 hit.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR001661. Glyco_hydro_37.
IPR018232. Glyco_hydro_37_CS.
IPR023720. Trehalase_periplasmic.
[Graphical view]
PANTHERiPTHR23403. PTHR23403. 1 hit.
PfamiPF01204. Trehalase. 1 hit.
[Graphical view]
PRINTSiPR00744. GLHYDRLASE37.
SUPFAMiSSF48208. SSF48208. 1 hit.
PROSITEiPS00927. TREHALASE_1. 1 hit.
PS00928. TREHALASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P13482-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSPAPSRPQ KMALIPACIF LCFAALSVQA EETPVTPQPP DILLGPLFND
60 70 80 90 100
VQNAKLFPDQ KTFADAVPNS DPLMILADYR MQQNQSGFDL RHFVNVNFTL
110 120 130 140 150
PKEGEKYVPP EGQSLREHID GLWPVLTRST ENTEKWDSLL PLPEPYVVPG
160 170 180 190 200
GRFREVYYWD SYFTMLGLAE SGHWDKVADM VANFAHEIDT YGHIPNGNRS
210 220 230 240 250
YYLSRSQPPF FALMVELLAQ HEGDAALKQY LPQMQKEYAY WMDGVENLQA
260 270 280 290 300
GQQEKRVVKL QDGTLLNRYW DDRDTPRPES WVEDIATAKS NPNRPATEIY
310 320 330 340 350
RDLRSAAASG WDFSSRWMDN PQQLNTLRTT SIVPVDLNSL MFKMEKILAR
360 370 380 390 400
ASKAAGDNAM ANQYETLANA RQKGIEKYLW NDQQGWYADY DLKSHKVRNQ
410 420 430 440 450
LTAAALFPLY VNAAAKDRAN KMATATKTHL LQPGGLNTTS VKSGQQWDAP
460 470 480 490 500
NGWAPLQWVA TEGLQNYGQK EVAMDISWHF LTNVQHTYDR EKKLVEKYDV
510 520 530 540 550
STTGTGGGGG EYPLQDGFGW TNGVTLKMLD LICPKEQPCD NVPATRPTVK
560
SATTQPSTKE AQPTP
Length:565
Mass (Da):63,637
Last modified:January 1, 1990 - v1
Checksum:i4885D7556A3C0781
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15868 Genomic DNA. Translation: CAA33878.1.
U00096 Genomic DNA. Translation: AAC74281.1.
AP009048 Genomic DNA. Translation: BAA36054.1.
PIRiS04782.
RefSeqiNP_415715.1. NC_000913.3.
WP_000841714.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74281; AAC74281; b1197.
BAA36054; BAA36054; BAA36054.
GeneIDi945757.
KEGGiecj:JW1186.
eco:b1197.
PATRICi32117642. VBIEscCol129921_1243.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15868 Genomic DNA. Translation: CAA33878.1.
U00096 Genomic DNA. Translation: AAC74281.1.
AP009048 Genomic DNA. Translation: BAA36054.1.
PIRiS04782.
RefSeqiNP_415715.1. NC_000913.3.
WP_000841714.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JF4X-ray2.20A31-565[»]
2JG0X-ray1.50A31-565[»]
2JJBX-ray1.90A/B/C/D31-565[»]
2WYNX-ray2.10A/B/C/D31-565[»]
ProteinModelPortaliP13482.
SMRiP13482.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260095. 121 interactors.
DIPiDIP-11022N.
IntActiP13482. 5 interactors.
STRINGi511145.b1197.

Protein family/group databases

CAZyiGH37. Glycoside Hydrolase Family 37.

Proteomic databases

EPDiP13482.
PaxDbiP13482.
PRIDEiP13482.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74281; AAC74281; b1197.
BAA36054; BAA36054; BAA36054.
GeneIDi945757.
KEGGiecj:JW1186.
eco:b1197.
PATRICi32117642. VBIEscCol129921_1243.

Organism-specific databases

EchoBASEiEB1010.
EcoGeneiEG11017. treA.

Phylogenomic databases

eggNOGiENOG4105E53. Bacteria.
COG1626. LUCA.
HOGENOMiHOG000215464.
InParanoidiP13482.
KOiK01194.
OMAiWAGQLHQ.
PhylomeDBiP13482.

Enzyme and pathway databases

BioCyciEcoCyc:TREHALAPERI-MONOMER.
ECOL316407:JW1186-MONOMER.
MetaCyc:TREHALAPERI-MONOMER.
BRENDAi3.2.1.28. 2026.

Miscellaneous databases

EvolutionaryTraceiP13482.
PROiP13482.

Family and domain databases

HAMAPiMF_01060. Peripl_trehalase. 1 hit.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR001661. Glyco_hydro_37.
IPR018232. Glyco_hydro_37_CS.
IPR023720. Trehalase_periplasmic.
[Graphical view]
PANTHERiPTHR23403. PTHR23403. 1 hit.
PfamiPF01204. Trehalase. 1 hit.
[Graphical view]
PRINTSiPR00744. GLHYDRLASE37.
SUPFAMiSSF48208. SSF48208. 1 hit.
PROSITEiPS00927. TREHALASE_1. 1 hit.
PS00928. TREHALASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTREA_ECOLI
AccessioniPrimary (citable) accession number: P13482
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: November 2, 2016
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.