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Ureaplasma urealyticum Search Results

Record: 1 of 1  
MiniMap IGR112 IGR113 IGR108 IGR111 IGR109 IGR110 atpD,atpH-2, - UU133 UU127 atpE, - UU128 UU131 atpG, - UU130 UU125 atpB, - UU129 atpA, - UU132 UU126 atpD,atpH-2, - UU133 UU127 atpE, - UU128 UU131 atpG, - UU130 UU125 atpB, - UU129 atpA, - UU132 UU126 Type: tandem, Name:  - 95 Type: tandem, Name:  - 100 Type: tandem, Name:  - 94 Type: tandem, Name:  - 98 Type: tandem, Name:  - 92 Type: tandem, Name:  - 99 Type: tandem, Name:  - 97 Type: tandem, Name:  - 93 Type: tandem, Name:  - 96 atpD,atpH-2, - UU133 UU127 atpE, - UU128 UU131 atpG, - UU130 UU125 atpB, - UU129 atpA, - UU132 UU126
* Calculated from Protein Sequence

Gene ID: UU129

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
atpB  

Definition:
ATP synthase beta chain

Gene Start:
171331

Gene Stop:
169937

Gene Length:
1395

Molecular Weight*:
50824

pI*:
5.30

Net Charge*:
-9.88

EC:
3.6.1.34  

Functional Class:
energy metabolism; ATP-proton motive force interconversion  

Pathway: pathway table
Oxidative phosphorylation

Primary Evidence:
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.

Romano N, La Licata R, Russo Alesi D. 1986. Energy Production in Ureaplasma urealyticum. Pediatr Infect Dis. 5(6 Suppl):S308-12. Medline: 3797330.

Secondary Evidence:
Das A, Ljungdahl LG. 1997. Composition and primary structure of the F1F0 ATP synthase from the obligately anaerobic bacterium Clostridium thermoaceticum. J Bacteriol 179(11):3746-55. Medline: 9171425.

Rasmussen OF, Shirvan MH, Margalit H, Christiansen C, Rottem S. 1992. Nucleotide sequence, organization and characterization of the atp genes and the encoded subunits of Mycoplasma gallisepticum ATPase. Biochem J. 285(Pt 3):881-8. Medline: 1386735.

Comment:
Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. F-type ATPases have 2 components: CF(1) - the catalytic core and CF(0) - the membrane proton channel. CF(1) has five subunits: Alpha(3), Beta(3), Gamma(1), Delta(1) and Epsilon(1). CF(0) has three main subunits: A, B and C.

This gene is part of a cluster encompassing records UU128-UU138. The products of these genes are responsible for the ATP synthase complex, generation of ATP from ADP and Pi.

The complete list of predicted ATP synthases in U.u. is: UU053, UU054, UU128, UU129, UU130, UU132, UU133, UU134, UU135, UU136, UU137, and UU138.

This gene cluster is a likely candidate for the ATP synthase activity seen in conjunction with the urease present in Ureaplasma urealyticum (see UU427-UU434).

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

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, Medline: 8501029) [...] 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.

Blast Summary:  PSI-Blast Search
A gapped BLAST revealed a signficant hits to a number of ATP Synthase Beta Chain proteins. For example: Residues 2-460 are 68% similar to the ATP synthase beta chain of M.gallisepticum (APTB_MYCGA). Residues 7-464 were 66% similar to the ATP synthase beta chain of M.pneumoniae (ATPB_MYCPN). In addition to the above mentioned hits, significant hits to a number of other APT synthase beta chain proteins from a wide assortment of organisms was seen, including a significant hit to the ATP synthase beta chain of E.coli (ATPB_ECOLI) where residues 7-462 are 63% similar.


COGS Summary:  COGS Search
The phylogenetic pattern of COG0055 is EHgpcMYU.
Cog name: ATP synthase beta subunit/transription termination factor rho.
Functional class: C/K.
BeTs to -h-pcmyu.
Number of proteins in this genome belonging to this COG is 2



Blocks Summary:  Blocks Search
Residues 75-100, 131-168, 224-235, 244-288, 292-329 and 339-348 rank in the 100.00th percentile to Block BL00152(A,B,C,D,E and F respectively), described as ATP synthase alpha and beta subunits proteins.

Residues 147-162 rank in the 99.76th percentile to Block PR00364A, described as Disease Resistance Protein Signature.

Residues 146-167 rank in the 99.51th percentile to Block PR00449A, described as Transforming Protein p21 RAS Signature.

Residues 48-63 rank in the 96.83th percentile to Block PR00357C, described as Type III Antifreeze Protein Signature.



ProDom Summary:  Protein Domain Search
Residues 292-429 are 72% similar to a defined domain of ATPB_MYCGA.
Residues 204-299 are 84% similar to a defined domain of ATPB_MARPO.
Residues 7-94 are 60% similar to a defined domain of ATP2_CHLRE.

Paralogs:  Local Blast Search
This protein is paralogously related to UU054, UU132 and UU053.
Compared to UU054, residues 4-456 are 38% 58% similar.
Compared to UU132, residues 69-347 are 26% similar.
Compared to UU053, residues 69-346 are 22% similar.

Pfam Summary:  Pfam Search
Residues 9 to 76 (E-value = 2.4e-22) place UU129 in the ATP-synt_ab_N family which is described as ATP synthase alpha/beta family, beta-barrel domain (PF02874)
Residues 174 to 351 (E-value = 1e-85) place UU129 in the ATP-synt_ab family which is described as ATP synthase alpha/beta family, nucleotide-binding domain (PF00006)
Residues 358 to 462 (E-value = 2.7e-34) place UU129 in the ATP-synt_ab_C family which is described as ATP synthase alpha/beta chain, C terminal domain (PF00306)

PDB Hit:
gi|2981977|pdb|1SKY|E Chain E, Crystal Structure Of The Nucleotide Free Alpha3beta3 Sub-Complex Of F1-Atpase From The Thermophilic Bacillus Ps3

Gene Protein Sequence:
MTEVKKGKINQILGPVVDVRFPSEWLPEINTALELNNHGSKLVLEVSQLV
GDNIARCIAMDTTDGLVRGQEVINTQKPITMPVGKQVLGRMFNVTGDPID
EQPAPTGKRMPIHRPAPSFAEQAESIEILETGIKVVDLLVPFAKGGKIGL
FGGAGVGKTVLMQELIHNIAKNHGGLSVFAGVGERTREGNDLYYEMAESD
VLDKTALVFGQMNEPPGARMRVALSGLTMAEEFRDAFGQDVLLFIDNIFR
FTQAGSEVSALLGRMPSAVGYQPTLAFEMGQLQERITSTKKGSITSVQAV
YVPADDLTDPAPATTFSHLDAKVVLDRAIASLGLYPAISPLQSTSRLLDP
LVVGVKHYSVARRVIEILQRFMELQDIIAILGMDELSEEDRQLVMRARKV
RNYLSQPSHVAEKFSGQPGLSVKLEDTIEGFRKILDGECDDIHEQHFLYV
GKIDDVFEKAAKNK$

Gene Nucleotide Sequence:  Sequence Viewer
ATGACAGAAGTTAAAAAAGGTAAAATTAACCAAATTTTGGGCCCTGTTGT
TGACGTGCGTTTTCCCTCTGAATGATTGCCTGAAATTAACACTGCTTTAG
AATTAAACAATCATGGTTCTAAATTAGTACTTGAGGTTTCTCAATTAGTT
GGTGATAATATTGCAAGATGTATTGCAATGGATACAACTGATGGACTAGT
ACGTGGACAAGAGGTAATTAATACTCAAAAACCAATCACAATGCCTGTTG
GTAAACAAGTACTTGGACGTATGTTCAATGTAACTGGTGATCCAATTGAT
GAACAACCTGCACCAACAGGTAAACGTATGCCAATTCATCGTCCTGCACC
TTCATTCGCCGAACAAGCAGAATCAATTGAAATCCTAGAAACGGGAATTA
AAGTTGTCGACTTACTTGTACCTTTTGCAAAGGGTGGTAAGATCGGTTTA
TTTGGTGGTGCTGGAGTTGGTAAAACAGTTTTAATGCAAGAATTAATTCA
TAACATCGCTAAAAATCATGGTGGTTTATCAGTTTTTGCTGGAGTTGGAG
AAAGAACACGTGAAGGAAATGATTTATACTATGAAATGGCTGAGTCAGAT
GTTTTAGATAAAACAGCTCTTGTCTTTGGACAAATGAATGAACCACCAGG
AGCACGTATGCGCGTCGCATTAAGCGGTTTAACAATGGCTGAAGAATTCC
GTGATGCTTTTGGTCAAGATGTTTTATTATTTATCGATAACATTTTTAGA
TTCACACAAGCTGGTTCAGAAGTTTCTGCTTTACTTGGACGAATGCCATC
AGCAGTTGGTTATCAACCAACACTTGCTTTTGAAATGGGTCAATTACAAG
AACGAATTACATCAACTAAAAAAGGATCAATTACATCGGTTCAAGCTGTT
TATGTTCCAGCTGATGACTTAACTGACCCCGCACCAGCAACAACTTTTTC
ACACTTAGATGCTAAAGTTGTTTTAGATAGAGCTATTGCCTCATTGGGAT
TATATCCAGCAATTTCACCACTACAATCAACAAGTCGTTTATTAGATCCA
TTAGTTGTTGGTGTAAAACACTACAGTGTTGCGCGTCGTGTAATTGAAAT
TTTACAAAGATTTATGGAATTACAAGATATTATTGCAATTCTTGGAATGG
ATGAATTAAGCGAAGAAGATCGTCAATTAGTAATGCGCGCACGTAAAGTA
CGTAACTACTTATCACAGCCAAGCCACGTTGCTGAAAAATTCTCTGGTCA
ACCTGGATTATCAGTTAAACTTGAAGATACTATTGAAGGATTTAGAAAAA
TTCTTGATGGTGAATGTGATGATATTCATGAACAACATTTCTTATATGTT
GGTAAAATTGATGACGTTTTTGAAAAAGCAGCAAAAAATAAATAA


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