B7V8P9 (B7V8P9_PSEA8) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Periplasmic trehalase HAMAP-Rule MF_01060
EC=3.2.1.28 HAMAP-Rule MF_01060

Alternative name(s):
Alpha,alpha-trehalase HAMAP-Rule MF_01060
Alpha,alpha-trehalose glucohydrolase HAMAP-Rule MF_01060

Gene names

Name:	treA HAMAP-Rule MF_01060 EMBL CAW27607.1
Ordered Locus Names:	PLES_28801

Organism

Pseudomonas aeruginosa (strain LESB58) [Complete proteome] [HAMAP]

Taxonomic identifier

557722 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas › Pseudomonas aeruginosa group › Pseudomonas aeruginosa

Protein attributes

Sequence length	545 AA.
Sequence status	Complete.
Protein existence	Inferred 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-Rule MF_01060
Catalytic activity	Alpha,alpha-trehalose + H2O = 2 D-glucose. HAMAP-Rule MF_01060
Subcellular location	Periplasm By similarity HAMAP-Rule MF_01060.
Sequence similarities	Belongs to the glycosyl hydrolase 37 family. HAMAP-Rule MF_01060

Ontologies

Keywords
Cellular component	Periplasm HAMAP-Rule MF_01060
Domain	Signal HAMAP-Rule MF_01060
Molecular function	Glycosidase HAMAP-Rule MF_01060 Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	cellular hyperosmotic response Inferred from electronic annotation. Source: InterPro trehalose catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	alpha,alpha-trehalase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 32	32	By similarity HAMAP-Rule MF_01060

Sequences

	Sequence		Length	Mass (Da)
	B7V8P9 [UniParc]. Last modified February 10, 2009. Version 1. Checksum: 0EB649A408138712	FASTA	545	61,156
	10 20 30 40 50 60 MPDRTALPRA MLAAWVLLLL AACSQGPAPT PPASWGWQDA SGERAIAPGE AYPELFQAVQ 70 80 90 100 110 120 ESRLFSDQKH FVDALPLREP ARIRADYLRE RERPGFDLRA FVGRNFEESG SVETAPPEAG 130 140 150 160 170 180 ADLASHISDL WPALTRHYEQ VPAHSSLLPL PKPYVVPGGR FREVYYWDSY FTMLGLAESG 190 200 210 220 230 240 QHQRVRDMLD NFAYLIDTYG HIPNGNRSYY LSRSQPPFFA YMVDLQARRE GDAAYRRYLP 250 260 270 280 290 300 QLQKEYAYWM EGSAGLRPNE ARLHVVKLAD GSLLNRYWDN RDTPRQESFL EDRATAARAP 310 320 330 340 350 360 QRPAGEVYRD LRAGAESGWD FSSRWLDDDR ELASIRTTAI VPVDLNALLY HLERTIAKAC 370 380 390 400 410 420 ASSALKACEQ GYGARAEKRR QAIEDHLWHP AGYYADYDWQ RRRPIERINA ASLFPLFTGL 430 440 450 460 470 480 ASTERAGRTA DSVAAQLLRP GGLATTTRAS GQQWDEPNGW APLQWVAVQG LRAYGRDALA 490 500 510 520 530 540 EDIGRRFLAQ VQQVYDREGK LVEKYDISGN QGGGGGGEYP LQDGFGWSNG VTLQLLRLYG PGAGR

References

[1]

"Newly introduced genomic prophage islands are critical determinants of in vivo competitiveness in the Liverpool epidemic strain of Pseudomonas aeruginosa." Winstanley C., Langille M.G.I., Fothergill J.L., Kukavica-Ibrulj I., Paradis-Bleau C., Sanschagrin F., Thomson N.R., Winsor G.L., Quail M.A., Lennard N., Bignell A., Clarke L., Seeger K., Saunders D., Harris D., Parkhill J., Hancock R.E.W., Brinkman F.S.L., Levesque R.C. Genome Res. 19:12-23(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LESB58.

Cross-references

Sequence databases
EMBL GenBank DDBJ	FM209186 Genomic DNA. Translation: CAW27607.1.
RefSeq	YP_002440471.1. NC_011770.1.
3D structure databases
ProteinModelPortal	B7V8P9.
ModBase	Search...
Protein-protein interaction databases
STRING	557722.PLES_28801.
Protein family/group databases
CAZy	GH37. Glycoside Hydrolase Family 37.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAW27607; CAW27607; PLES_28801.
GeneID	7177297.
KEGG	pag:PLES_28801.
PATRIC	19815444. VBIPseAer113719_2954.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1626.
HOGENOM	HOG000215464.
KO	K01194.
OMA	NRYWDAS.
ProtClustDB	PRK13272.
Enzyme and pathway databases
BioCyc	PAER557722:GHJW-5947-MONOMER.
Family and domain databases
HAMAP	MF_01060. Peripl_trehalase.
InterPro	IPR008928. 6-hairpin_glycosidase-like. IPR001661. Glyco_hydro_37. IPR018232. Glyco_hydro_37_CS. IPR023720. Trehalase_periplasmic. [Graphical view]
PANTHER	PTHR23403. PTHR23403. 1 hit.
Pfam	PF01204. Trehalase. 1 hit. [Graphical view]
PRINTS	PR00744. GLHYDRLASE37.
SUPFAM	SSF48208. Glyco_trans_6hp. 1 hit.
PROSITE	PS00927. TREHALASE_1. 1 hit. PS00928. TREHALASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

B7V8P9_PSEA8

Accession

Primary (citable) accession number: B7V8P9

Entry history

Integrated into UniProtKB/TrEMBL:	February 10, 2009
Last sequence update:	February 10, 2009
Last modified:	May 1, 2013
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)