Periplasmic trehalase precursor - Escherichia coli (strain K12)

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
Synonyms:	osmA
Ordered Locus Names:	b1197, JW1186

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	565 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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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. HAMAP MF_01060
Catalytic activity	Alpha,alpha-trehalose + H₂O = 2 D-glucose. HAMAP MF_01060
Subunit structure	Monomer Probable.
Subcellular location	Periplasm. HAMAP MF_01060
Induction	By growth at high osmolarity, is regulated by cAMP. HAMAP MF_01060
Sequence similarities	Belongs to the glycosyl hydrolase 37 family.

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Ontologies

Keywords
Cellular component	Periplasm
Domain	Signal
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	trehalose metabolic process Inferred from electronic annotation. Source: HAMAP
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...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 30

30

Ref.1

Chain

31 – 565

535

Periplasmic trehalase HAMAP MF_01060

PRO_0000012041

Secondary structure

1

.

565

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P13482-1 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: 4885D7556A3C0781
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FASTA

565

63,637

        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 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 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

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis and DNA sequence of the osmoregulated treA gene encoding the periplasmic trehalase of Escherichia coli K12." Gutierrez C., Ardourel M., Bremer E., Middendorf A., Boos W., Ehmann U. Mol. Gen. Genet. 217:347-354(1989) [PubMed: 2671658] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 31-33 AND 35-43. Strain: K12.
[2]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Osmotic induction of the periplasmic trehalase in Escherichia coli K12: characterization of the treA gene promoter." Repoila F., Gutierrez C. Mol. Microbiol. 5:747-755(1991) [PubMed: 1710760] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-66. Strain: K12.
[6]	"Trehalase of Escherichia coli. Mapping and cloning of its structural gene and identification of the enzyme as a periplasmic protein induced under high osmolarity growth conditions." Boos W., Ehmann U., Bremer E., Middendorf A., Postma P. J. Biol. Chem. 262:13212-13218(1987) [PubMed: 2820965] [Abstract] Cited for: CHARACTERIZATION. Strain: K12.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

X15868 Genomic DNA. Translation: CAA33878.1.
U00096 Genomic DNA. Translation: AAC74281.1.
AP009048 Genomic DNA. Translation: BAA36054.1.

PIR

S04782.

RefSeq

AP_001822.1.
NP_415715.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2JF4	X-ray	2.20	A	31-565	[»]
2JG0	X-ray	1.50	A	31-565	[»]
2JJB	X-ray	1.90	A/B/C/D	31-565	[»]

ModBase

Search...

Protein family/group databases

CAZy

GH37. Glycoside Hydrolase Family 37.

Genome annotation databases

GeneID

945757.

GenomeReviews

Gene locus JW1186 in contig AP009048_GR.
Gene locus b1197 in contig U00096_GR.

KEGG

ecj:JW1186.
eco:b1197.

Organism-specific databases

EchoBASE

EB1010.

EcoGene

EG11017. treA.

CMR

Search...

Phylogenomic databases

HOGENOM

P13482.

OMA

P13482. NRYWDAS.

Enzyme and pathway databases

BioCyc

EcoCyc:TREHALAPERI-MON.
MetaCyc:TREHALAPERI-MON.

Family and domain databases

HAMAP

MF_01060.
[Tree]

InterPro

IPR001661. Glyco_hydro_37.
IPR018232. Glyco_hydro_37_CS.
[Graphical view]

PANTHER

PTHR23403. Glyco_hydro_37. 1 hit.

Pfam

PF01204. Trehalase. 1 hit.
[Graphical view]

PRINTS

PR00744. GLHYDRLASE37.

PROSITE

PS00927. TREHALASE_1. 1 hit.
PS00928. TREHALASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

TREA_ECOLI

Accession

Primary (citable) accession number: P13482

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 1, 1990
Last modified:	June 16, 2009
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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