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Protein

Periplasmic trehalase

Gene

treA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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

Keywordsi

Molecular functionGlycosidase, Hydrolase

Enzyme and pathway databases

BioCyciEcoCyc:TREHALAPERI-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

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

BioGridi4260095135 interactors.
DIPiDIP-11022N
IntActiP13482 5 interactors.
STRINGi316385.ECDH10B_1250

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
OMAiKYDISNG
PhylomeDBiP13482

Family and domain databases

Gene3Di1.50.10.101 hit
HAMAPiMF_01060 Peripl_trehalase, 1 hit
InterProiView protein in InterPro
IPR008928 6-hairpin_glycosidase_sf
IPR012341 6hp_glycosidase-like_sf
IPR001661 Glyco_hydro_37
IPR018232 Glyco_hydro_37_CS
IPR023720 Trehalase_periplasmic
PANTHERiPTHR23403 PTHR23403, 1 hit
PfamiView protein in Pfam
PF01204 Trehalase, 1 hit
PRINTSiPR00744 GLHYDRLASE37
SUPFAMiSSF48208 SSF48208, 1 hit
PROSITEiView protein in PROSITE
PS00927 TREHALASE_1, 1 hit
PS00928 TREHALASE_2, 1 hit

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
PATRICifig|1411691.4.peg.1089

Similar proteinsi

Entry informationi

Entry nameiTREA_ECOLI
AccessioniPrimary (citable) accession number: P13482
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: March 28, 2018
This is version 150 of the entry and version 1 of the sequence. See 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