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Chlamydia trachomatis Search Results

Record: 1 of 1  
MiniMap IGR253 IGR252 IGR256 IGR251 IGR257 IGR255 IGR258 IGR254 CT312 atpK, - CT304 atpE, - CT310 tal, - CT313 atpB, - CT307 atpA, - CT308 atpI,ntpI, - CT305 rpoC, - CT314 CT311 CT312 atpK, - CT304 atpE, - CT310 tal, - CT313 atpB, - CT307 atpA, - CT308 atpI,ntpI, - CT305 rpoC, - CT314 CT311 CT312 atpK, - CT304 atpE, - CT310 tal, - CT313 atpB, - CT307 atpA, - CT308 atpI,ntpI, - CT305 rpoC, - CT314 atpD, - CT306 CT309 atpD, - CT306 CT309 CT311
* Calculated from Protein Sequence

Gene ID: CT308

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
atpA  

Definition:
ATP synthase alpha chain

Gene Start:
346562

Gene Stop:
344790

Gene Length:
1773

Molecular Weight*:
65488

pI*:
4.91

Net Charge*:
-21.70

EC:
3.6.1.34  

Functional Class:
energy metabolism; ATP-proton motive force  

Pathway: pathway table
Energy Metabolism; Oxidative phosphorylation

Comment:
The V-type ATPase complex is a multisubunit complex that
pumps H+ s, typically in intracellular acidic vacuoles.
Several 3D structures are available for this protein.
See CT669, CT717, CT304, CT305, CT306,
CT307, CT309, CT310, and CT491.

From Prosite PDOC00137:

ATP synthase (proton-translocating ATPase) (EC 3.6.1.34) is a component of the cytoplasmic membrane of eubacteria, the inner membrane of mitochondria, and the thylakoid membrane of chloroplasts. The ATPase complex is composed of an oligomeric transmembrane sector, called CF(0), and a catalytic core, called coupling factor CF(1). The former acts as a proton channel; the latter is composed of five subunits, alpha, beta, gamma, delta and epsilon. The sequences of subunits alpha and beta are related and both contain a nucleotide-binding site for ATP and ADP. The beta chain has catalytic activity, while the alpha chain is a regulatory subunit.

Vacuolar ATPases (V-ATPases) are responsible for acidifying a variety of intracellular compartments in eukaryotic cells. Like F-ATPases, they are oligomeric complexes of a transmembrane and a catalytic sector. The sequence of the largest subunit of the catalytic sector (70 Kd) is related to that of F-ATPase beta subunit, while a 60 Kd subunit, from the same sector, is related to the F-ATPases alpha subunit.


Blast Summary:  PSI-Blast Search
Numerous hits in Psi-BLAST to vacuolar ATP synthase alpha
subunit sequences, e.g., residues 6-548 are 40% similar
to the sequence from Bos taurus. As with CT307, many of the hits
with highest E values were to eukaryotic sequences. Residues
11-538 are 42% similar to ATPA_METJA. CT308 is similar to TP0426, TP0529,
TP0402, TP0528, TP0427 of T.pallidum. It is also similar to
MG399 of M.genitalium and PG1575 of P.gingivalis.

CT308 is orthologously related to CPn0088 and
they share 81% similarity.

COGS Summary:  COGS Search
BeTs to 8 clades of COG1155
COG name: Vacuolar ATPase/archaeal ATP synthase A subunit (NtpA)
Functional Class:  C
The phylogenetic pattern of COG1155 is amtKY-----------oLin-
Number of proteins in this genome belonging to this COG is 1


Blocks Summary:  Blocks Search
Residues 76-101, 102-146, 318-329, 330-374, 337-381, 408-445
have matches to blocks BL00152A,B,C,D, which include
ATP synthase alpha and beta chain sequences.

ProDom Summary:  Protein Domain Search
Residues 299-482 are 51% similar to an alpha ATP synthase domain
observed in VATA_TRYCO. Residues 224-270, 271-296, and 489-503
also correspond to ATP synthase domains, as seen in
NTPA_ENTHR and ATPA_HUMAN.

Paralogs:  Local Blast Search
CT308 is paralogously related to CT669 and CT717, two
flagellar-type ATP synthase sequences and to CT307, a
V-type ATP synthase beta sequence and (weakly) to CT491,
a termination factor rho sequence. Residues 226-472 are 30%
similar to CT669; residues 19-109 are 30% similar to CT717;
residues 220-401 are 29% similar to CT307; and residues
342-421 are 32% similar to CT491.

Pfam Summary:  Pfam Search
Residues 13 to 77 (E-value = 2.7e-12) place CT308 in the ATP-synt_ab_N family which is described as ATP synthase alpha/beta family, beta-barrel domain (PF02874)
Residues 261 to 449 (E-value = 1.1e-79) place CT308 in the ATP-synt_ab family which is described as ATP synthase alpha/beta family, nucleotide-binding domain (PF00006)
Residues 461 to 564 (E-value = 2.8e-10) place CT308 in the ATP-synt_ab_C family which is described as ATP synthase alpha/beta chain, C terminal domain (PF00306)

Structural Feature(s):
Feature Type  Start  Stop
coil-coil  
552  
591

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 Atp Synthase, F1fo Atp Synthase, F1-Atpase, Alpha3beta3 Subcomplex Of F1-Atpase, Hydrolase Mol_id: 1; Molecule:

Gene Protein Sequence:
MVATSKQTTQGYVVEAYGNLLRVHVDGHVRQGEVAYVSVDDTWLKAEIIE
VVGDEVKIQVFEETQGISRGALVTFSGHLLEAELGPGLLQGIFDGLQNRL
EILADTSLFLRRGEYVNAICRETVWAYTQKASVGSVLSRGDVLGTVKEGR
FDHKIMVPFSCFEEVTITWVISSGNYTVDTVVAKGRTSTGEELEFTMVQK
WPIKQAFLEGEKVPSHEIMDVGLRVLDTQIPVLKGGTFCTPGPFGAGKTV
LQHHLSKYAAVDIVVLCACGERAGEVVEILQEFPHLTDPHTGQSLMHRTC
IICNTSSMPVAARESSIYLGITIAEYYRQMGLHILLLADSTSRWAQALRE
ISGRLEEIPGEEAFPAYLASRIAAFYERGGAVKMKDGSEGSLTICGAVSP
AGGNFEEPVTQATLSVVGAFCGLSKARADARRYPSIDPMISWSKYLDSVA
EILEKKVPGWGESVKQASRFLEEGAEIGKRIEVVGEEGISMEDMEIFLKS
ELYDFCYLQQNAFDAEDCYCPFDRQIELFSLMNHIFNSRFCFDCPDNARS
FFLELQSKIKTLNGQKFLSEEYQKGLEVIYKLLESKMVQTV

Gene Nucleotide Sequence:  Sequence Viewer
ATGGTAGCAACTTCAAAACAAACGACGCAGGGCTATGTCGTAGAAGCTTA
CGGGAATTTATTGCGGGTGCATGTTGATGGGCATGTGCGTCAGGGAGAAG
TGGCCTATGTTAGCGTAGACGATACTTGGTTGAAAGCAGAAATTATTGAA
GTCGTAGGAGATGAAGTTAAGATCCAAGTTTTTGAGGAGACTCAAGGAAT
TTCTCGTGGCGCTTTGGTAACTTTTTCCGGACATTTATTAGAAGCTGAAT
TAGGGCCCGGTTTACTCCAAGGAATTTTTGATGGGTTACAGAATCGCTTG
GAAATATTGGCAGATACAAGCCTATTTTTGAGAAGAGGCGAATACGTTAA
TGCCATTTGTCGAGAAACAGTATGGGCTTATACGCAAAAAGCTTCGGTAG
GATCTGTACTTTCTCGAGGAGATGTACTTGGAACGGTAAAAGAAGGTCGT
TTTGATCACAAGATTATGGTGCCTTTCTCTTGTTTTGAGGAAGTAACCAT
CACATGGGTGATTTCTTCTGGGAATTATACTGTCGATACCGTTGTTGCTA
AGGGACGTACTTCAACAGGTGAAGAGCTTGAGTTCACTATGGTTCAGAAA
TGGCCTATCAAGCAAGCTTTTTTAGAAGGGGAGAAAGTTCCTTCTCACGA
GATCATGGATGTAGGGTTGCGAGTGTTAGATACACAAATTCCGGTTCTTA
AGGGAGGAACGTTCTGTACTCCTGGACCTTTTGGAGCTGGGAAAACGGTA
TTGCAGCACCATTTATCCAAATATGCTGCTGTAGACATTGTAGTTTTGTG
TGCTTGTGGAGAGCGTGCGGGGGAGGTTGTAGAAATCTTACAGGAGTTCC
CTCATCTCACAGACCCTCATACAGGGCAGTCTTTGATGCACAGAACTTGT
ATTATTTGTAATACATCTTCCATGCCTGTAGCTGCTCGAGAATCTTCTAT
TTATTTGGGGATTACAATTGCTGAGTATTACCGTCAGATGGGTCTGCACA
TTTTGTTACTGGCTGATTCGACATCTAGATGGGCACAGGCTTTAAGAGAG
ATTTCTGGGCGATTAGAAGAAATTCCTGGGGAAGAGGCTTTCCCAGCCTA
TTTAGCGTCTCGAATAGCCGCTTTCTATGAAAGAGGTGGGGCTGTAAAAA
TGAAGGATGGGTCGGAAGGATCTTTGACTATCTGTGGAGCAGTTTCGCCT
GCAGGAGGGAATTTCGAAGAGCCTGTTACACAAGCAACTTTATCTGTGGT
TGGAGCTTTCTGTGGTCTTTCGAAAGCGCGTGCAGATGCAAGAAGATATC
CTTCTATTGACCCAATGATTTCATGGTCTAAATATCTGGATTCTGTAGCA
GAAATTTTAGAGAAAAAAGTTCCGGGTTGGGGAGAATCTGTTAAACAAGC
CTCCCGCTTCTTGGAGGAAGGTGCTGAAATTGGTAAACGAATAGAAGTCG
TAGGGGAAGAAGGGATTTCTATGGAAGACATGGAAATCTTTTTGAAATCA
GAGCTATACGATTTCTGTTATTTGCAGCAAAACGCATTTGATGCTGAGGA
CTGCTACTGTCCATTTGATCGGCAGATAGAGCTCTTTTCTTTGATGAATC
ACATCTTTAACTCTAGATTCTGTTTCGATTGTCCAGATAACGCCCGCAGT
TTCTTTTTAGAGCTCCAAAGTAAAATTAAGACGCTGAATGGTCAGAAATT
CCTATCTGAAGAATATCAGAAAGGCCTGGAAGTAATCTATAAACTGTTAG
AAAGCAAAATGGTGCAGACGGTG


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