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Haemophilus ducreyi Search Results

Record: 1 of 1  
MiniMap tRNA-Ala-1 tRNA-Ile-1 rRNA-16S-1 rRNA-23S-1 IGR7 IGR6 IGR9 IGR8 IGR10 IGR5 IGR4 IGR11 atpE, - HD0005 atpC, - HD0011 atpF, - HD0006 atpH, - HD0007 atpA, - HD0004 atpG, - HD0009 atpD, - HD0010 atpA, - HD0008 atpE, - HD0005 atpC, - HD0011 atpF, - HD0006 atpH, - HD0007 atpA, - HD0004 atpG, - HD0009 atpD, - HD0010 atpA, - HD0008 atpE, - HD0005 atpC, - HD0011 atpF, - HD0006 atpH, - HD0007 atpA, - HD0004 atpG, - HD0009 atpD, - HD0010 atpA, - HD0008
* Calculated from Protein Sequence

Gene ID: HD0010

DNA Molecule Name:
1  

Genbank ID:
0

Gene Name:
atpD  

Definition:
ATP synthase F1, subunit beta

Gene Start:
8323

Gene Stop:
9696

Gene Length:
1374

Molecular Weight*:
49683

pI*:
4.80

Net Charge*:
-15.60

EC:
3.6.1.34  

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

Pathway: pathway table
Oxidative phosphorylation

Secondary Evidence:
Nielsen,J., Hansen,F.G., Hoppe,J., Friedl,P. and von Meyenburg,K. The nucleotide sequence of the atp genes coding for the F0 subunits a, b, c and the F1 subunit delta of the membrane bound ATP synthase of Escherichia coli.
Mol. Gen. Genet. 184 (1), 33-39 (1981)
Medline: 82147764.

Kanazawa,H., Mabuchi,K., Kayano,T., Noumi,T., Sekiya,T. and Futai,M.
Nucleotide sequence of the genes for F0 components of the proton-translocating ATPase from Escherichia coli: prediction of the primary structure of F0 subunits.
Biochem. Biophys. Res. Commun. 103 (2), 613-620 (1981)
Medline: 82134799.

Cain,B.D. and Simoni,R.D.
Impaired proton conductivity resulting from mutations in the a subunit of F1F0 ATPase in Escherichia coli.
J. Biol. Chem. 261 (22), 10043-10050 (1986)
Medline: 86278048.

Kumamoto,C.A. and Simoni,R.D.
Genetic evidence for interaction between the a and b subunits of the F0 portion of the Escherichia coli proton translocating ATPase.
J. Biol. Chem. 261 (22), 10037-10042 (1986)
Medline: 86278047.

Cain,B.D. and Simoni,R.D.
Proton translocation by the F1F0ATPase of Escherichia coli. Mutagenic analysis of the a subunit.
J. Biol. Chem. 264 (6), 3292-3300 (1989)
Medline: 89123453.

Yamada,H., Moriyama,Y., Maeda,M. and Futai,M.
Transmembrane topology of Escherichia coli H(+)-ATPase (ATP synthase) subunit a.
FEBS Lett. 390 (1), 34-38 (1996)
Medline: 96314544.

Valiyaveetil,F.I. and Fillingame,R.H.
Transmembrane topography of subunit a in the Escherichia coli F1F0 ATP synthase.
J. Biol. Chem. 273 (26), 16241-16247 (1998)
Medline: 98298136.

Hausrath,A.C., Gruber,G., Matthews,B.W. and Capaldi,R.A.
Structural features of the gamma subunit of the Escherichia coli F(1) ATPase revealed by a 4.4-A resolution map obtained by x-ray
crystallography.
Proceedings of the National Academy of Sciences of the United States of America. 96 (24),
13697-13702 (1999)
Medline: 20040613

Comment:
From GenBank (gi:114546): AtpG produces ATP from ADP in the presence of a proton gradient across the membrane. The beta chain is the catalytic subunit. F-type ATPases have two 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.

See also other chains of the F1 subunit: atpD (delta chain), HD0007; atpD (delta chain), HD0008; atpG (gamma chain), HD0009; atpE (epsilon chain), HD0011.

In addition, see chains of the F0 subunit of this ATPase: atpF (B chain), HD0006; and atp6 (A chain), HD0004; and atpL (C chain), HD0005.

Blast Summary:  PSI-Blast Search
Numerous significant hits in gapped BLAST to atpB proteins; e.g., residues 1-457 are 91% similar to ATPB_HAEIN; residues 1-457 are 84% similar to ATPB_ECOLI; and residues 1-457 are 84% similar to the ATP synthase subunit beta in Salmonella typhimurium. BLAST reveals many similarities to other bacterial and eukaryotic ATPB sequences.



COGS Summary:  COGS Search
BeTs to 10 clades of COG0055
COG name: FoF1-type ATP synthase beta subunit
Functional Class: C
The phylogenetic pattern of COG0055 is ----yqvcebrhujgp----x
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
***** IPB000194 (ATP synthase alpha and beta subunit, N-terminal) with a combined E-value of 1.3e-106.
    IPB000194A    63-94
    IPB000194B    126-163
    IPB000194C    199-230
    IPB000194D    240-281
    IPB000194E    286-333
***** IPB003255 (ATP synthase beta subunit, C-terminal) with a combined E-value of 5.7e-17.
    IPB003255B    67-111
    IPB003255C    112-157
    IPB003255H    297-332
    IPB003255D    167-200
***** IPB000790 (ATP synthase alpha subunit, C-terminal) with a combined E-value of 2.3e-12.
    IPB000790B    116-159
    IPB000790C    195-240
    IPB000790D    241-282
    IPB000790E    312-349


ProDom Summary:  Protein Domain Search
Residues 347-449 are 91% similar to a (BETA ION HYDROLASE TRANSPORT) protein domain (PD000108) which is seen in ATPB_HAEIN.

Residues 9-340 are 92% similar to a (TRANSPORT ION HYDROLASE HYDROGEN SUBUNIT SYNTHASE) protein domain (PD000090) which is seen in ATPB_HAEIN.



Paralogs:  Local Blast Search
HD0010 is paralogously related to HD0008 (2e-30) and HD0895 (2e-05).


Pfam Summary:  Pfam Search
Residues 6 to 70 (E-value = 1.1e-26) place HD0010 in the ATP-synt_ab_N family which is described as ATP synthase alpha/beta family, beta-barrel domain (PF02874)
Residues 169 to 345 (E-value = 1.2e-81) place HD0010 in the ATP-synt_ab family which is described as ATP synthase alpha/beta family, nucleotide-binding domain (PF00006)
Residues 352 to 457 (E-value = 2.1e-47) place HD0010 in the ATP-synt_ab_C family which is described as ATP synthase alpha/beta chain, C terminal domain (PF00306)

PDB Hit:
pdb|1MAB|B Chain B, Rat Liver F1-Atpase 587 9e-169
pdb|1NBM|D Chain D, The Structure Of Bovine F1-Atpase Covalentl... 585 3e-168
pdb|1E1Q|D Chain D, Bovine Mitochondrial F1-Atpase At 100k >gi|... 585 3e-168

Gene Protein Sequence:
MATGKIVQIIGAVIDVEFPQDAVPKVYDALKVESGLTLEVQQQLGGGLVR
CIALGTSDGLKRGLKVENTGNPIQVPVGTKTLGRIMNVLGEPIDEKGPIG
EEARWDIHRAAPSYEEQSNSTELLETGIKVIDLICPFAKGGKVGLFGGAG
VGKTVNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMTDSNVLDKV
SLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLFFVDNIYRYTLAGT
EVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADD
LTDPSPATTFAHLDSTVVLSRNIASLGIYPAVDPLDSTSRQLDPLVVGEE
HYNVARGVQGTLQRYKELKDIIAILGMDELSEDDKLVVSRARKIERFLSQ
PFFVAEVFTGSPGKYVSLKDTIRGFKGILEGEFDHIPEQAFYMAGSIDEV
VERASKM$

Gene Nucleotide Sequence:  Sequence Viewer
ATGGCAACAGGAAAAATTGTACAGATTATCGGTGCGGTAATCGACGTTGA
ATTCCCGCAAGATGCAGTACCAAAAGTATATGATGCTTTAAAAGTTGAAT
CAGGTTTAACCTTAGAAGTTCAACAACAATTAGGTGGTGGTTTAGTACGT
TGTATCGCATTAGGTACCTCAGATGGTTTAAAGCGTGGCTTAAAGGTTGA
AAATACAGGTAACCCTATTCAAGTTCCTGTAGGCACTAAAACATTAGGTC
GTATTATGAATGTATTAGGCGAACCAATTGATGAAAAAGGACCTATTGGC
GAAGAAGCGCGCTGGGATATTCATCGTGCGGCTCCAAGTTATGAAGAACA
GTCAAATAGTACTGAATTACTTGAAACCGGTATCAAAGTTATTGACTTAA
TTTGTCCATTTGCAAAAGGTGGTAAAGTTGGCTTATTTGGTGGAGCTGGT
GTAGGTAAAACCGTTAATATGATGGAGTTGATCCGTAATATTGCTATTGA
GCACTCAGGTTATTCGGTTTTTGCTGGTGTAGGTGAGCGTACTCGTGAAG
GTAATGATTTTTATCATGAAATGACGGATTCTAATGTATTAGATAAAGTA
TCACTAGTATATGGCCAAATGAATGAACCACCAGGTAACCGTTTACGTGT
TGCGTTAACAGGTTTAACTATGGCTGAAAAATTCCGTGATGAAGGTCGTG
ATGTATTATTTTTCGTAGATAATATTTATCGTTATACTTTAGCCGGTACA
GAAGTTTCTGCTTTATTAGGCCGTATGCCATCAGCGGTAGGTTATCAACC
AACCCTAGCAGAAGAAATGGGTGTATTACAAGAACGTATTACCTCAACTA
AAACAGGTTCAATCACGTCAGTACAAGCGGTTTATGTGCCTGCGGATGAC
TTAACAGATCCATCACCAGCGACAACCTTTGCTCATTTAGATTCAACAGT
GGTATTAAGCCGTAACATAGCCTCATTAGGTATTTACCCAGCGGTAGATC
CTCTTGACTCTACTTCCCGTCAATTAGACCCGCTTGTAGTTGGGGAAGAA
CATTATAATGTAGCGCGTGGTGTACAAGGTACATTACAACGTTATAAAGA
GTTAAAAGACATTATTGCAATTTTAGGTATGGACGAACTGTCTGAAGATG
ATAAGTTAGTTGTTTCCCGTGCACGTAAGATCGAACGTTTCTTATCACAA
CCATTCTTTGTTGCTGAAGTGTTTACAGGTTCACCAGGTAAATATGTATC
TCTAAAAGATACTATCCGCGGTTTTAAAGGAATCTTAGAAGGTGAATTTG
ATCATATCCCAGAACAGGCGTTCTATATGGCAGGTTCAATCGACGAAGTT
GTGGAAAGAGCGAGCAAGATGTAA


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