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Ureaplasma urealyticum Search Results

Record: 1 of 1  
MiniMap IGR358 IGR365 IGR361 IGR362 IGR360 IGR359 IGR364 IGR357 IGR356 IGR363 ure3,ureA, - UU434 ure2,ureB, - UU433 UU427 ureG, - UU429 ureF, - UU430 ureD, - UU428 ure1,ureC, - UU432 UU426 tly,hlyA, - UU436 Rev1, - UU437 fhuC, - UU435 ure3,ureA, - UU434 ure2,ureB, - UU433 UU427 ureG, - UU429 ureF, - UU430 ureD, - UU428 ure1,ureC, - UU432 UU426 tly,hlyA, - UU436 Rev1, - UU437 fhuC, - UU435 Type: tandem, Name:  - 268 Type: tandem, Name:  - 265 Type: tandem, Name:  - 270 Type: tandem, Name:  - 266 Type: tandem, Name:  - 267 Type: tandem, Name:  - 269 ure2,ureB, - UU433 UU427 ureG, - UU429 ureF, - UU430 ureD, - UU428 ure1,ureC, - UU432 ureE, - UU431 ureE, - UU431 ure3,ureA, - UU434 UU426 tly,hlyA, - UU436 Rev1, - UU437 fhuC, - UU435
* Calculated from Protein Sequence

Gene ID: UU432

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
ure1  ureC  

Definition:
urease alpha subunit (urea amidohydrolase)

Gene Start:
495390

Gene Stop:
493594

Gene Length:
1797

Molecular Weight*:
64536

pI*:
5.70

Net Charge*:
-12.34

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:
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
Numerous significant hits in gapped BLAST to urease alpha subunit sequences; e.g. residues 1-598 are 82% similar to URE1_UREUR; residues 2-598 are 52% similar to URE1_STAXY; and residues 2-595 are 53% similar to URE1_CLOPE.
BLAST also reveals no significant similarity to C.trachomatis, M.genitalium, or T.pallidum sequences.

COGS Summary:  COGS Search
The phylogenetic pattern of COG0804 is -h--c--u.
Cog name: Urea amidohydrolase (urease) - central for pathogenesis!!!.
Functional class: R.
BeTs to -h--c--u.
Number of proteins in this genome belonging to this COG is 1



Blocks Summary:  Blocks Search
Residues 4-598 span twelve regions of similarity to blocks BL01120A-I (Urease nickel ligands proteins.)

ProDom Summary:  Protein Domain Search
Residues 169-413 are 99% similar to a defined domain of Q60058_UREUR, a urease subunit sequence.


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

Pfam Summary:  Pfam Search
Residues 2 to 126 (E-value = 1.2e-74) place UU432 in the Urease_alpha family which is described as Urease alpha-subunit, N-terminal domain (PF00449)
Residues 132 to 442 (E-value = 2.1e-73) place UU432 in the Amidohydro_1 family which is described as Amidohydrolase family (PF01979)

PDB Hit:
gi|4557957|pdb|1UBP|C Chain C, Crystal Structure Of Urease From Bacillus Pasteurii Inhibited With Beta-Mercaptoethanol At 1.65 Angstroms Resolution

Gene Protein Sequence:
MFKISRKNYSDLYGITTGDSVRLGDTNLWVKVEKDLTTYGEESVFGGGKT
LREGMGMNSTMKLDDKLGNAEVMDLVITNALIVDYTGIYKADIGIKNGKI
AAIGKSGNPHLTDNVDMIVGISTEISAGEGKIYTAGGLDTHVHWLEPEIV
PVALDGGITTVIAGGTGMNDGTKATTVSPGKFWVKSALQAADGLSINAGF
LAKGQGMEDPIFEQIAAGACGLKIHEDWGATGNAIDLALTVADKTDVAVA
IHTDTLNEAGFVEHTIAAMKGRTIHAYHTEGAGGGHAPDILETVKYAHIL
PASTNPTIPYTVNTIAEHLDMLMVCHHLNPKVPEDVAFADSRIRSQTIAA
EDLLHDMGAISIMSSDTLAMGRIGEVATRTWQMAHKMKAQFGSLKGDSEF
SDNNRVKRYISKYTINPAIAHGVDSYIGSLEVGKLADIVAWEPKFFGAKP
YYVVKMGVIARCVAGDPNASIPTCEPVIMRDQFGTYGRLLTNTSVSFVSK
IGLENGIKEEYKLEKELLPVKNCRSVNKKSMKWNSATPNLEVDPQTFDAA
VDFNDLENWLEQSASELAKKLKKTSSGKYILDAEPLTEAPLAQRYFLF$

Gene Nucleotide Sequence:  Sequence Viewer
ATGTTTAAAATTTCAAGAAAAAATTATTCAGATTTATACGGTATTACAAC
TGGTGATAGCGTTAGATTAGGAGATACAAATCTTTGAGTTAAAGTTGAAA
AAGACTTAACTACTTATGGTGAAGAATCTGTTTTTGGTGGTGGAAAAACC
CTACGTGAAGGTATGGGAATGAATTCTACTATGAAGTTAGATGATAAATT
AGGTAATGCTGAAGTAATGGATTTAGTTATTACAAATGCACTAATTGTTG
ATTATACAGGTATTTATAAAGCAGATATTGGTATTAAAAATGGAAAAATT
GCTGCGATTGGTAAATCTGGAAATCCACATTTAACAGATAATGTTGATAT
GATTGTGGGTATCTCAACTGAAATTTCAGCTGGTGAGGGTAAAATTTATA
CAGCTGGTGGTTTAGATACTCACGTTCACTGACTAGAACCAGAAATAGTT
CCTGTTGCATTAGATGGTGGTATTACAACTGTTATTGCTGGTGGTACAGG
TATGAATGATGGTACAAAAGCCACAACTGTTTCACCTGGTAAATTTTGAG
TTAAATCAGCTTTACAAGCAGCTGATGGATTATCAATTAATGCCGGTTTT
TTAGCTAAAGGTCAAGGTATGGAAGATCCAATTTTTGAGCAAATTGCTGC
TGGAGCTTGTGGACTTAAAATCCATGAAGACTGAGGGGCAACAGGAAATG
CGATTGATTTAGCATTAACAGTTGCTGATAAAACTGATGTAGCTGTTGCT
ATTCATACAGATACATTAAATGAAGCTGGATTTGTAGAACATACAATTGC
AGCTATGAAAGGGCGAACAATTCATGCTTATCATACAGAAGGTGCTGGTG
GAGGGCATGCTCCAGATATTCTAGAAACTGTTAAATATGCCCATATTTTA
CCAGCTTCTACAAACCCAACAATTCCTTATACAGTAAATACAATTGCTGA
ACATTTAGATATGTTAATGGTATGTCACCACTTAAATCCTAAGGTTCCAG
AAGATGTTGCTTTTGCTGATTCACGTATTCGTAGCCAAACAATTGCAGCT
GAAGACTTATTGCACGATATGGGTGCAATTTCAATTATGTCATCAGATAC
ATTAGCTATGGGACGTATTGGCGAAGTTGCAACTCGTACATGACAAATGG
CTCACAAAATGAAAGCACAATTTGGATCATTAAAAGGTGATAGTGAATTC
AGTGATAACAATCGTGTAAAACGTTATATTTCTAAATATACAATTAACCC
AGCTATTGCACATGGTGTTGATTCTTATATTGGTTCACTAGAAGTTGGTA
AATTAGCTGATATTGTTGCTTGAGAACCTAAATTCTTTGGTGCAAAACCT
TATTATGTTGTAAAAATGGGTGTAATCGCTCGTTGTGTAGCAGGTGATCC
AAATGCTTCAATTCCAACATGCGAACCTGTAATTATGCGTGACCAATTTG
GAACTTATGGACGTTTGTTAACTAATACATCAGTAAGTTTTGTTTCAAAA
ATTGGGTTAGAAAATGGCATTAAAGAGGAATATAAATTAGAAAAAGAATT
ATTACCAGTTAAAAATTGCCGTTCAGTAAATAAAAAGAGTATGAAATGAA
ACTCTGCGACTCCAAATTTAGAAGTTGATCCGCAAACTTTTGATGCTGCT
GTTGATTTTAATGATTTAGAAAATTGACTAGAACAATCAGCTTCTGAATT
AGCTAAAAAATTAAAAAAGACTTCAAGTGGCAAATATATACTTGATGCTG
AACCTTTAACAGAAGCGCCATTAGCACAAAGATATTTCTTATTTTAA


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