A7ZKW9 (TREA_ECO24) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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:	EcE24377A_1343

Organism

Escherichia coli O139:H28 (strain E24377A / ETEC) [Complete proteome] [HAMAP]

Taxonomic identifier

331111 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	565 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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 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 component	Periplasm
Domain	Signal
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	periplasmic space 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
	Signal peptide	1 – 30	30	Potential
	Chain	31 – 565	535	Periplasmic trehalase HAMAP MF_01060		PRO_1000064450

Sequences

	Sequence		Length	Mass (Da)
	A7ZKW9 [UniParc]. Last modified October 23, 2007. Version 1. Checksum: 77919C41DB1ABFD7	FASTA	565	63,655
	10 20 30 40 50 60 MKSPAPSRPQ KMALIPACIF LCFAALSVQA EETPVTPQPP DILLGPLFND VQNAKLFPDQ 70 80 90 100 110 120 KTFADAVPNS DPLMILADYR MQQNQSGFDL RHFVNVNFTL PKEGEKYVPP EGQSLREHID 130 140 150 160 170 180 GLWPVLTRST ENTEKWDSLL PLPEPYVVPG GRFREVYYWD SYFTMLGLAE SGHWDKVADM 190 200 210 220 230 240 VANFAHEIDT YGHIPNGNRS YYLSRSQPPF FAMMVELLAQ 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 ASKAAGDNAM 370 380 390 400 410 420 ANQYETLANA RQKGIEKYLW NDQQGWYADY DLKSHKVRNQ LTAAALFPLY VNAAAKDRAN 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 NVPATRPTVK SATTQPSTKE AQPTP

References

[1]

"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates." Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J. J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: E24377A / ETEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000800 Genomic DNA. Translation: ABV20897.1.
RefSeq	YP_001462448.1. NC_009801.1.
3D structure databases
ProteinModelPortal	A7ZKW9.
SMR	A7ZKW9. Positions 37-547.
ModBase	Search...
Protein-protein interaction databases
STRING	A7ZKW9.
Protein family/group databases
CAZy	GH37. Glycoside Hydrolase Family 37.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000019345; EBESCP00000018407; EBESCG00000018399.
GeneID	5586340.
GenomeReviews	Gene locus EcE24377A_1343 in contig CP000800_GR.
KEGG	ecw:EcE24377A_1343.
NMPDR	fig|331111.3.peg.3804.
PATRIC	18291942. VBIEscCol31211_1632.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1626.
GeneTree	EBGT00050000010574.
HOGENOM	HBG485982.
OMA	NRYWDAS.
ProtClustDB	PRK13271.
Enzyme and pathway databases
BioCyc	ECOL331111:ECE24377A_1343-MONOMER.
Family and domain databases
HAMAP	MF_01060. Peripl_trehalase. [Tree]
InterPro	IPR008928. 6-hairpin_glycosidase-like. IPR001661. Glyco_hydro_37. IPR018232. Glyco_hydro_37_CS. IPR023720. Trehalase_periplasmic. [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

TREA_ECO24

Accession

Primary (citable) accession number: A7ZKW9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	October 23, 2007
Last modified:	January 25, 2012
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program