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A1AAC5 (TREA_ECOK1) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Periplasmic trehalase

EC=3.2.1.28
Alternative name(s):
Alpha,alpha-trehalase
Alpha,alpha-trehalose glucohydrolase
Gene names
Name:treA
Ordered Locus Names:Ecok1_11210
ORF Names:APECO1_314
OrganismEscherichia coli O1:K1 / APEC [Complete proteome] [HAMAP]
Taxonomic identifier405955 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length565 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity. HAMAP MF_01060

Catalytic activity

Alpha,alpha-trehalose + H2O = 2 D-glucose. HAMAP MF_01060

Subunit structure

Monomer By similarity. HAMAP MF_01060

Subcellular location

Periplasm By similarity HAMAP MF_01060.

Sequence similarities

Belongs to the glycosyl hydrolase 37 family.

Ontologies

Keywords
   Cellular componentPeriplasm
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcellular hyperosmotic response

Inferred from electronic annotation. Source: InterPro

trehalose catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionalpha,alpha-trehalase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Potential
Chain31 – 565535Periplasmic trehalase HAMAP MF_01060
PRO_1000064452

Sequences

Sequence LengthMass (Da)Tools
A1AAC5 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 19422733AD517B7C

FASTA56563,748
        10         20         30         40         50         60 
MKSPAPSRPQ KMALIPACIF LCFAALSVQA EETSVTPQPP DILLGPLFND VQNAKLFPDQ 

        70         80         90        100        110        120 
KTFADAVPNS DPLMILADYR IQQNQSGFDL RHFVNVNFTL PKEGEKYVPP EGQSLREHID 

       130        140        150        160        170        180 
GLWPVLTRST ENTEKWDSLL PLPKPYVVPG GRFREVYYWD SYFTMLGLAE SGHWDKVADM 

       190        200        210        220        230        240 
VANFAHEIDN YGHIPNGNRS YYLSRSQPPF FALMVELLAQ HEGDAALKQY LPQMQKEYAY 

       250        260        270        280        290        300 
WMDGVENLQA GQQEKRVVKL QDGTLLNRYW DDRDTPRPES WVEDIATAKS NPNRPATEIY 

       310        320        330        340        350        360 
RDLRSAAASG WDFSSRWMDN PQQLNTLRTT SIVPVDLNSL MFKMEKILAR ASKAIGDNAM 

       370        380        390        400        410        420 
ANQYETLANA RQKGIEKYLW NDQQGWYADY DLKSHKVRNQ LTAAALFPLY VNAAAKDRAS 

       430        440        450        460        470        480 
KMATATKTHL LQPGGLNTTS VKSGQQWDAP NGWAPLQWVA TEGLQNYGQK EVAMDISWHF 

       490        500        510        520        530        540 
LTNVQHTYDR EKKLVEKYDV STTGTGGGGG EYPLQDGFGW TNGVTLKMLD LICPKEQPCD 

       550        560 
NVPATRPLSE STTQPLKQKE AEPTP 

« Hide

References

[1]"The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7 shares strong similarities with human extraintestinal pathogenic E. coli genomes."
Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J., Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.
J. Bacteriol. 189:3228-3236(2007) [PubMed: 17293413] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000468 Genomic DNA. Translation: ABJ00615.1.
RefSeqYP_852329.1. NC_008563.1.

3D structure databases

ProteinModelPortalA1AAC5.
SMRA1AAC5. Positions 37-547.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1AAC5.

Protein family/group databases

CAZyGH37. Glycoside Hydrolase Family 37.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000037376; EBESCP00000035893; EBESCG00000036426.
GeneID4492438.
GenomeReviewsGene locus Ecok1_11210 in contig CP000468_GR.
KEGGecv:APECO1_314.
PATRIC18213916. VBIEscCol127180_1245.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1626.
GeneTreeEBGT00050000010574.
HOGENOMHBG485982.
OMANRYWDAS.
ProtClustDBPRK13271.

Enzyme and pathway databases

BioCycECOL405955:APECO1_314-MONOMER.

Family and domain databases

HAMAPMF_01060. Peripl_trehalase.
[Tree]
InterProIPR008928. 6-hairpin_glycosidase-like.
IPR001661. Glyco_hydro_37.
IPR018232. Glyco_hydro_37_CS.
IPR023720. Trehalase_periplasmic.
[Graphical view]
KOK01194.
PANTHERPTHR23403. Glyco_hydro_37. 1 hit.
PfamPF01204. Trehalase. 1 hit.
[Graphical view]
PRINTSPR00744. GLHYDRLASE37.
SUPFAMSSF48208. Glyco_trans_6hp. 1 hit.
PROSITEPS00927. TREHALASE_1. 1 hit.
PS00928. TREHALASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTREA_ECOK1
AccessionPrimary (citable) accession number: A1AAC5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: January 23, 2007
Last modified: December 14, 2011
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families