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Ureaplasma urealyticum Search Results

Record: 1 of 1  
MiniMap IGR358 IGR361 IGR362 IGR355 IGR360 IGR359 IGR364 IGR357 IGR356 IGR363 UU425.1 ure3,ureA, - UU434 ure2,ureB, - UU433 UU427 ureG, - UU429 ureF, - UU430 ureD, - UU428 ure1,ureC, - UU432 UU426 tly,hlyA, - UU436 UU425 fhuC, - UU435 UU425.1 ure3,ureA, - UU434 ure2,ureB, - UU433 UU427 ureG, - UU429 ureF, - UU430 ureD, - UU428 ure1,ureC, - UU432 UU426 tly,hlyA, - UU436 UU425 fhuC, - UU435 Type: tandem, Name:  - 267 Type: tandem, Name:  - 264 Type: tandem, Name:  - 269 Type: tandem, Name:  - 265 Type: tandem, Name:  - 266 Type: tandem, Name:  - 268 UU425.1 ure3,ureA, - UU434 ure2,ureB, - UU433 UU427 ureG, - UU429 ureF, - UU430 ureD, - UU428 ure1,ureC, - UU432 ureE, - UU431 ureE, - UU431 UU426 tly,hlyA, - UU436 UU425 fhuC, - UU435
* Calculated from Protein Sequence

Gene ID: UU431

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
ureE  

Definition:
urease accessory protein

Gene Start:
493529

Gene Stop:
493080

Gene Length:
450

Molecular Weight*:
17340

pI*:
5.40

Net Charge*:
-4.84

EC:
3.5.1.5  

Functional Class:
central intermediary metabolism; other  

Pathway: pathway table
Purine metabolism
Urea cycle and metabolism of amino groups

Primary Evidence:
Ruifu Y, Minli Z, Guo Z, Wang X. 1997. Biovar diversity is reflected by variations of genes encoding urease of Ureaplasma urealyticum. Microbiol Immunol 41(8):625-7. Medline: 9310943.

MacKenzie CR, Henrich B, Hadding U. 1996. Biovar-specific epitopes of the urease enzyme of Ureaplasma urealyticum. J Med Microbiol
45(5):366-71. Medline: 8918953.

Nagata K, Takagi E, Satoh H, Okamura H, Tamura T. 1995. Growth inhibition of Ureaplasma urealyticum by the proton pump inhibitor lansoprazole: direct attribution to inhibition by lansoprazole of
urease activity and urea-induced ATP synthesis in U. urealyticum.
Antimicrob Agents Chemother 39(10):2187-92. Medline: 8619564.

Smith DG, Russell WC, Ingledew WJ, Thirkell D. 1993. Hydrolysis of urea by Ureaplasma urealyticum generates a transmembrane potential
with resultant ATP synthesis. J Bacteriol. 175(11):3253-8. Medline: 8501029.

Scheurlen W, Frauendienst G, Schrod L, von Stockhausen HB. 1992.
Polymerase chain reaction-amplification of urease genes: rapid
screening for ureaplasma urealyticum infection in endotracheal
aspirates of ventilated newborns. Eur J Pediatr 151(10):740-2. Medline: 1425793.

Willoughby JJ, Russell WC, Thirkell D, Burdon MG. 1991. Isolation and detection of urease genes in Ureaplasma urealyticum. Infect Immun. 59(7):2463-9. Medline : 2050410.

Thirkell D, Myles AD, Precious BL, Frost JS, Woodall JC, Burdon MG, Russell WC. 1989. The urease of Ureaplasma urealyticum. J Gen Microbiol. 135 ( Pt 2):315-23. Medline: 2482331.

Blanchard A. 1990. Ureaplasma urealyticum urease genes; use of a UGA tryptophan codon. Mol Microbiol. 4(4):669-76. Medline: 2191184.

Eng H, Robertson JA, & Stemke GW. 1986. Properties of urease from Ureaplasma urealyticum: kinetics, molecular weight, and demonstration of multiple enzyme isoelectric point forms. Can J Microbiol. 32(6):487-93. Medline: 3730958.

Secondary Evidence:
Neyrolles O, Ferris S, Behbahani N, Montagnier L, Blanchard A. 1996. Organization of Ureaplasma urealyticum urease gene cluster and expression in a suppressor strain of Escherichia coli. J Bacteriol. 178(9):2725. Medline: 8626347.

Blanchard A, Barile MF. 1989. Cloning of Ureaplasma urealyticum DNA sequences showing genetic homology with urease genes from gram-negative bacteria. Res Microbiol 140(4-5):281-90. Medline: 2799066.

Comment:
From Mobley, H. et al. (1995), Medline: 7565414:
It is tempting to speculate that UreE may function to bind cellular nickel ion by its polyhistidine tail and act as the nickel donor during urease activation. [...] It remains to possible that the protein has multiple functions in some microorganisms and a single funtion in others, that it serves no function in certain species, or that it serves distinct functions in different cells. Overall, the role for UreE has not been established.

See UU427-UU434.

From Neyrolles. et al., 1996:
The urease gene cluster from a biotype 1 representative of U. urealyticum (serotype I) was cloned and sequenced. Seven genes were found, with ureA, ureB, and ureC encoding the structural subunits and ureE, ureF, ureG, and a truncated ureI) gene encoding accessory proteins. Urease expression was not obtained when the plasmid containing these genes was incorporated into an opal suppressor strain of Escherichia coli, although this enzymatic activity was found in the same E. coli strain transformed with pC6b, a plasmid with previously cloned urease genes from the U. urealyticum T960 strain of biotype 2 (serotype 8). Although there are 12 TGA triplets encoding tryptophan within urease genes, the level of expression obtained was comparable to the levels reported for other bacterial genes expressed in E. coli. Nested deletion experiments allowed us to demonstrate that ureD is necessary for urease activity whereas another open reading frame located downstream is not. The promoter for ureA and possibly other urease genes was identified for both serotypes.

From: Molecular Biology and Pathogenicity of Mycoplasmas, Microbiology and Molecular Biology Reviews, Dec. 1998, p.1118-1119. Shmuel Razin, David Yogev, and Yehudith Naot.

Ureaplasmas are unique among the mollicutes in possessing a very potent urease. Although protein and gene analysis of the ureaplasmal urease complex has shown that it resembles other procaryotic ureases in subunit structure and composition, the specific activity of the ureaplasmal urease is much higher and was estimated to exceed that of jack bean urease by about 100-fold. More importantly, ureaplasmas appear to be unique among procaryotes in requiring urea for growth. [...] The dependence of ureaplasmas on urea for growth has led to the hypothesis that intracellular urea hydrolysis and the resulting intracellular accumulation of ammonia/ammonium ions is coupled to ATP synthesis through a chemiosmotic type of mechanism. Experimental support for the generation of a transmembrane potential, with resultant ATP synthesis through the ureaplasmal F0F1-type ATPase, first provided by Romano et al. (1986, Medline: 3797330) was more recently extended and confirmed by Smith et al., 1993 [...] It is worth mentioning at this point that the pH of the urogenital tract is usually on the acidic side of neutrality, corresponding to the pH values optimal for ureaplasma growth, maximum increase in delta P, maximum ammonia chemical potential, maximum urease activity, and maximum ATP generation.

For reviews of ureases, see Collins, C. and D'Orazio, S. (1993), Medline: 7934918 and Mobley, H. et al. (1995), Medline: 7565414.

Blast Summary:  PSI-Blast Search
Several hits in gapped BLAST to urease accessory proteins; e.g. residues 1-149 are 94% similar to (L40489) ureE gene product of Ureaplasma urealyticum; residues 11-143 are 46% similar to UREE_BACSB; residues 17-144 are 32% similar to UREE_STRSL; and residues 11-144 are 29% similar to UREE_BACPA.
BLAST also reveals no significant similarity to M.genitalium, C.trachomatis, or T.pallidum.

COGS Summary:  COGS Search
None.

Blocks Summary:  Blocks Search
None.

ProDom Summary:  Protein Domain Search
Residues 3-144 are 94% similar to a defined domain of Q56559_UREUR, a urease subunit.
Residues 46-124 are 36% similar to a defined domain of O06708_BORBR, a urease accessory.

Paralogs:  Local Blast Search
No paralogs in U.u.

Pfam Summary:  Pfam Search
Residues 7 to 75 (E-value = 2.2e-22) place UU431 in the UreE_N family which is described as UreE urease accessory protein, N-terminal domain (PF02814)
Residues 77 to 145 (E-value = 1e-25) place UU431 in the UreE_C family which is described as UreE urease accessory protein, C-terminal domain (PF05194)

Structural Feature(s):
Feature Type  Start  Stop
coil-coil  
120  
149

PDB Hit:


Gene Protein Sequence:
LTVFKEILDNIANIKNVESYQIENIHLTSDDVLKRVIIISSDQNVEYGIR
LEEDKKLMDGDILYKDDYKLVVIRLELSDVLIITAHTIGEMAKIAHNLGN
RHMPAQFTETQMIVPYDYLVEEYLQDNKALYERKKIKLKEAFKHCSDAK$


Gene Nucleotide Sequence:  Sequence Viewer
TTGACTGTATTTAAAGAAATTTTAGATAATATTGCTAACATTAAAAATGT
TGAAAGTTATCAAATTGAGAACATTCATTTAACAAGCGACGACGTTTTAA
AACGTGTAATTATCATTTCATCAGATCAAAATGTTGAATATGGAATTCGT
TTAGAAGAGGACAAAAAATTAATGGATGGTGACATCTTATACAAGGATGA
TTATAAACTAGTTGTTATTAGATTAGAGTTATCAGATGTATTAATTATTA
CAGCACACACAATTGGTGAAATGGCAAAAATTGCCCATAATTTAGGTAAT
CGTCATATGCCGGCTCAATTTACTGAAACACAAATGATCGTTCCCTACGA
CTATTTAGTAGAAGAATACCTTCAAGATAATAAAGCCCTATATGAAAGAA
AAAAAATTAAACTTAAAGAAGCATTTAAACACTGTAGTGACGCTAAATAG



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