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B0RNH1 (TREA_XANCB) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 25. 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:xcc-b100_0667
OrganismXanthomonas campestris pv. campestris (strain B100) [Complete proteome] [HAMAP]
Taxonomic identifier509169 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length568 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

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 – 3838 Potential
Chain39 – 568530Periplasmic trehalase HAMAP MF_01060
PRO_1000136428

Sequences

Sequence LengthMass (Da)Tools
B0RNH1 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 29E4FA266074FF0A

FASTA56862,663
        10         20         30         40         50         60 
MPHAPARSGD AMSAAAPPCC TSLLGLSLSM FVAPCALAAT PLEGAVVSAP APTPPTPDLA 

        70         80         90        100        110        120 
YPELFQAVQR GELFDDQKHF VDFLPLRDPA LINADYLAQH EHAGFDLRKF VDANFEESPP 

       130        140        150        160        170        180 
VQTDAIRQDT ALREHIDALW PKLVRSQTNV PAHSSLLALP HPYVVPGGRF REVYYWDSYF 

       190        200        210        220        230        240 
TMLGLVKSGE TTLSRQMLDN FAYLIDTYGH IPNGNRTYYL SRSQPPFFSY MVELQAGVEG 

       250        260        270        280        290        300 
EAVYQRYLPQ LQKEYAYWMQ GGDDLQPGQA ARHVVRLADG SVLNRYWDER DTPRPEAWLH 

       310        320        330        340        350        360 
DTRTAAEAHD RPAADVYRDL RAGAESGWDY TSRWLADGKT LSTIRTTAIV PIDLNSLLYH 

       370        380        390        400        410        420 
LERTLAQACA HTGTACSQDY AALAQQRKQA IDAHLWNAAG YYADYDWQTR TLSNQVTAAA 

       430        440        450        460        470        480 
LYPLFAGLAS ADHAKRTATS VRARLLRPGG LATTALKTGQ QWDEPNGWAP LQWVAVDGLR 

       490        500        510        520        530        540 
RYGEDGLART IGERFLTQVQ ALFAREHKLV EKYGLDADAA GGGGGEYALQ DGFGWTNGVT 

       550        560 
LMLLNLYPSP GAIQAPAKTK RKPEPAAP 

« Hide

References

[1]"The genome of Xanthomonas campestris pv. campestris B100 and its use for the reconstruction of metabolic pathways involved in xanthan biosynthesis."
Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T., Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., Sidhu V.K., Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K., Puehler A.
J. Biotechnol. 134:33-45(2008) [PubMed: 18304669] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: B100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM920689 Genomic DNA. Translation: CAP50006.1.
RefSeqYP_001902072.1. NC_010688.1.

3D structure databases

ProteinModelPortalB0RNH1.
SMRB0RNH1. Positions 54-549.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0RNH1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6321140.
GenomeReviewsGene locus xcc-b100_0667 in contig AM920689_GR.
PATRIC24081147. VBIXanCam108527_0685.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG485982.
OMANRYWDAS.
ProtClustDBPRK13272.

Enzyme and pathway databases

BioCycXCAM487884:XCC-B100_0667-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]
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_XANCB
AccessionPrimary (citable) accession number: B0RNH1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 8, 2008
Last modified: January 25, 2012
This is version 25 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