P62602 (TREF_ECO57) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cytoplasmic trehalase
EC=3.2.1.28

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

Gene names

Name:	treF
Ordered Locus Names:	Z4932, ECs4399

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	549 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Hydrolyzes trehalose to glucose. Could be involved, in cells returning to low osmolarity conditions, in the utilization of the accumulated cytoplasmic trehalose, which was synthesized in response to high osmolarity By similarity. HAMAP MF_01059
Catalytic activity	Alpha,alpha-trehalose + H2O = 2 D-glucose. HAMAP MF_01059
Pathway	Glycan degradation; trehalose degradation; D-glucose from alpha,alpha-trehalose: step 1/1. HAMAP MF_01059
Subunit structure	Monomer By similarity. HAMAP MF_01059
Subcellular location	Cytoplasm By similarity HAMAP MF_01059.
Sequence similarities	Belongs to the glycosyl hydrolase 37 family.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Glycosidase 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	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	alpha,alpha-trehalase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 549	549	Cytoplasmic trehalase HAMAP MF_01059		PRO_0000173787

Sequences

	Sequence		Length	Mass (Da)
	P62602 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 543B82A7FAD4CB9D	FASTA	549	63,697
	10 20 30 40 50 60 MLNQKIQNPN PDELMIEVDL CYELDPYELK LDEMIEAEPE PEMIEGLPAS DALTPADRYL 70 80 90 100 110 120 ELFEHVQSAK IFPDSKTFPD CAPKMDPLDI LIRYRKVRRH RDFDLRKFVE NHFWLPEVYS 130 140 150 160 170 180 SEYVSDPQNS LKEHIDQLWP VLTREPQDHI PWSSLLALPQ SYIVPGGRFS ETYYWDSYFT 190 200 210 220 230 240 MLGLAESGRE DLLKCMADNF AWMIENYGHI PNGNRTYYLS RSQPPVFALM VELFEEDGVR 250 260 270 280 290 300 GARRYLDHLK MEYAFWMDGA ESLIPNQAYR HVVRMPDGSL LNRYWDDRDT PRDESWLEDV 310 320 330 340 350 360 ETAKHSGRPP NEVYRDLRAG AASGWDYSSR WLRDTGRLAS IRTTQFIPID LNAFLFKLES 370 380 390 400 410 420 AIANISALKG EKETEALFRQ KASARRDAVN RYLWDDENGI YRDYDWRREQ LALFSAAAIV 430 440 450 460 470 480 PLYVGMANHE QADRLANAVR SRLLTPGGIL ASEYETGEQW DKPNGWAPLQ WMAIQGFKMY 490 500 510 520 530 540 GDDLLGDEIA RSWLKTVNQF YLEQHKLIEK YHIADGVPRE GGGGEYPLQD GFGWTNGVVR RLIGLYGEP

References

[1]

"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R. Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.

[2]

"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005174 Genomic DNA. Translation: AAG58660.1. BA000007 Genomic DNA. Translation: BAB37822.1.
PIR	G91178. H86024.
RefSeq	NP_290099.1. NC_002655.2. NP_312426.1. NC_002695.1.
3D structure databases
ProteinModelPortal	P62602.
SMR	P62602. Positions 53-549.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000027189; EBESCP00000026082; EBESCG00000026241. EBESCT00000056225; EBESCP00000054053; EBESCG00000055273.
GeneID	915743. 961133.
GenomeReviews	Gene locus Z4932 in contig AE005174_GR. Gene locus ECs4399 in contig BA000007_GR.
KEGG	ece:Z4932. ecs:ECs4399.
PATRIC	18358377. VBIEscCol44059_4355.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000010574.
HOGENOM	HBG485982.
OMA	FWMDGAD.
ProtClustDB	PRK13270.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS4399-MONOMER.
Family and domain databases
HAMAP	MF_01059. Cyt_trehalase. [Tree]
InterPro	IPR008928. 6-hairpin_glycosidase-like. IPR023715. Cyt_trehalase. IPR001661. Glyco_hydro_37. IPR018232. Glyco_hydro_37_CS. [Graphical view]
KO	K01194.
PANTHER	PTHR23403. Glyco_hydro_37. 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

TREF_ECO57

Accession

Primary (citable) accession number: P62602
Secondary accession number(s): P37196

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	July 19, 2004
Last modified:	January 25, 2012
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program