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Chlamydia trachomatis Search Results

Record: 1 of 1  
MiniMap IGR553 IGR548 IGR555 IGR556 IGR551 IGR552 IGR554 IGR550 IGR549 IGR557 CT665 CT666 CT663 CT667 CT670 CT668 CT671 CT672 sctN,yscN, - CT669 pkn5, - CT673 CT664 yscC,sctC, - CT674 CT665 CT666 CT663 CT667 CT670 CT668 CT671 CT672 sctN,yscN, - CT669 pkn5, - CT673 CT664 yscC,sctC, - CT674 CT665 CT663 CT667 CT670 CT668 CT671 CT672 sctN,yscN, - CT669 pkn5, - CT673 CT664 yscC,sctC, - CT674 CT666
* Calculated from Protein Sequence

Gene ID: CT669

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
sctN  yscN  

Definition:
flagellar type ATPase (probable beta subunit)

Gene Start:
765053

Gene Stop:
766378

Gene Length:
1326

Molecular Weight*:
48191

pI*:
5.63

Net Charge*:
-6.36

EC:
3.6.1.34  

Functional Class:
cellular processes; secretion  

Pathway: pathway table
Energy metabolism; oxidative phosphorylation
Membrane transport; Type III secretion system

Comment:
This protein may have a translocase function related to flagellar-specific export. Other functions are possible.
See CT559, CT560, CT561, CT562, CT563 and CT564.

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.
Archaebacterial membrane-associated ATPases are composed of three subunits. The alpha chain is related to F-ATPases beta chain and the beta chain is related to F-ATPases alpha chain.

A protein highly similar to F-ATPase beta subunits is found in some bacterial apparatus involved in a specialized protein export pathway that proceeds without signal peptide cleavage. This protein is known as fliI in Bacillus and Salmonella, Spa47 (mxiB) in Shigella flexneri, HrpB6 in Xanthomonas campestris and yscN in Yersinia virulence plasmids.

Blast Summary:  PSI-Blast Search
Numerous hits in gapped BLAST to ATP synthase proteins, e.g., 53% similarity to PscN in P. aeruginosa (AF010151) , 52% similarity to YSCN_YEREN.
CT669 is similar to TP0402, a predicted flagellum-specific ATP synthase in T.pallidum. It is also similar
to MG399, a predicted ATP synthase beta chain sequence in M.genitalium.

CT669 is orthologously related to CPn0707: residues 1-442 of CT699 are
92% similar to residues 1-442 of CPn0707, a predicted flagellar type ATPase
(probable beta subunit) from C. pneumoniae.

COGS Summary:  COGS Search
BeTs to 8 clades of COG1157
COG name: Flagellar ATPase-like component
Functional Class:  C
The phylogenetic pattern of COG1157 is -----qv-eb--uj--olIN-
Number of proteins in this genome belonging to this COG is 2


Blocks Summary:  Blocks Search
Residues 90-115, 241-252, 260-304, 326-362 are significantly matched to BL00152A,B,C,D, concerned with ATP synthase alpha and beta subunit proteins, e.g. ATPA_HALVO and ATPA_SULAC.

ProDom Summary:  Protein Domain Search
Residues 222 to 392 are 64% similar to an ATP synthase chain subunit domain as seen in ATP2_ACTCH and ATPA_BOVIN. Residues 152 to 200 are 73% similar to an ATP synthase chain domain as seen in FLII_BACSU. Residues 201 to 218 are 94% similar to an ATP synthase chain subunit domain as seen in YSCN_YEREN.

Paralogs:  Local Blast Search
This protein is paralogously related to four other CT proteins:
CT717, probable flagellar-type ATP synthase, CT307, ATP
synthase beta chain, CT308, ATP synthase alpha chain, and
CT491, transcription termination factor rho. Residues 25-437 are
36% similar to CT717, residues 20-415 are 26% similar to CT307,
residues 147-382 are 30% similar to CT308, and residues 138-362
are 30% similar to CT308.

Pfam Summary:  Pfam Search
Residues 27 to 91 (E-value = 1.1e-06) place CT669 in the ATP-synt_ab_N family which is described as ATP synthase alpha/beta family, beta-barrel domain (PF02874)
Residues 191 to 367 (E-value = 6.7e-104) place CT669 in the ATP-synt_ab family which is described as ATP synthase alpha/beta family, nucleotide-binding domain (PF00006)

Structural Feature(s):
Feature Type  Start  Stop
non-globular  
1  
76

PDB Hit:
gi|1827812|pdb|1COW|D Chain D, Bovine Mitochondrial F1-Atpase Complexed With Aurovertin B Atp Phosphorylase, Hydrogen Ion Transport, Atp Synthase, F1f Atp Synthase, F1-Atpase Mol_id: 1; Molecule: Bovine Mitochondrial F1-Atpase; Chain: A, B, C, D, E, F, G;

Gene Protein Sequence:
MEEITTEFNTLMTELPDVQLTAVVGRIIEVVGMLIKAVVPDVRVGEVCLV
KRHGMEPLVTEVVGFTQNFVFLSPLGELTGVSPSSEVMATGLPLHIRAGE
GLLGRVLNGLGNPIDTETKGPLENVDAIYPIFKAPPDPLHRAKLRTILST
GVRCIDGMLTVAKGQRIGIFAGAGVGKSSLLGMIARNAEEADINVIALIG
ERGREVREFIENDLGEEGMKRSVIVVSTSDQSSQLRLNAAYVGTAIAEYF
RDQGKTVVLMMDSVTRFARALREVGLAAGEPPARAGYTPSVFSTLPKLLE
RAGASDKGTITAFYTVLVAGDDMNEPVADEVKSILDGHIVLSNALAQAYH
YPAIDVLASISRLLTAIVPEEQRRIIGRAREVLAKYKANEMLIRIGEYRR
GSDREVDFAIDHIDKLNRFLKQDIHEKTNYEEAAQQLRAIFR

Gene Nucleotide Sequence:  Sequence Viewer
ATGGAAGAGATAACGACCGAGTTTAATACGCTCATGACGGAATTGCCGGA
CGTGCAATTAACCGCAGTTGTGGGACGTATTATCGAAGTTGTCGGGATGT
TAATCAAGGCTGTTGTTCCGGATGTTCGTGTCGGTGAAGTGTGCTTGGTG
AAACGTCACGGGATGGAGCCTCTAGTTACAGAGGTAGTCGGTTTTACGCA
GAATTTTGTCTTCCTTTCTCCTTTAGGGGAGTTGACAGGAGTGAGTCCTT
CTTCGGAAGTGATGGCTACTGGATTGCCATTGCATATCCGAGCAGGAGAA
GGGTTATTGGGTCGTGTATTAAATGGTTTAGGAAATCCTATTGATACAGA
GACAAAGGGACCTTTAGAGAATGTCGATGCCATTTATCCAATTTTTAAAG
CTCCACCGGATCCGTTGCATCGAGCTAAATTGCGTACGATCTTGTCTACA
GGCGTGCGCTGTATTGATGGGATGCTCACTGTAGCTAAAGGGCAGAGAAT
CGGAATTTTTGCAGGAGCCGGGGTTGGTAAGTCCTCTTTATTGGGCATGA
TTGCTCGTAATGCTGAAGAAGCAGACATTAACGTAATTGCTTTGATTGGA
GAGCGGGGACGAGAGGTTCGCGAGTTCATAGAAAATGACCTTGGTGAAGA
GGGAATGAAACGTTCCGTTATTGTGGTCTCTACTTCTGATCAGTCGTCTC
AGCTGCGACTCAATGCTGCCTACGTAGGAACTGCGATAGCAGAATATTTC
CGAGATCAAGGTAAAACGGTTGTATTGATGATGGACTCAGTTACACGTTT
TGCGCGAGCTTTACGTGAAGTGGGGTTAGCGGCTGGAGAGCCTCCTGCTC
GTGCTGGGTACACGCCTTCTGTATTTTCCACTTTGCCTAAACTGTTAGAA
AGAGCAGGAGCCTCTGATAAAGGAACGATTACAGCATTTTATACTGTGTT
AGTGGCCGGGGATGATATGAACGAGCCGGTAGCGGACGAGGTGAAATCCA
TTTTAGATGGGCATATTGTTCTTTCTAATGCATTAGCGCAAGCATATCAT
TATCCAGCGATTGATGTGTTGGCTTCTATTAGCCGATTGCTGACAGCTAT
TGTTCCTGAGGAACAACGTCGAATTATTGGGCGTGCTAGAGAGGTTTTAG
CTAAATATAAAGCTAATGAGATGTTGATTCGTATTGGGGAATATCGTCGA
GGATCGGATCGTGAAGTCGATTTCGCAATCGATCATATCGATAAATTAAA
TCGATTCCTTAAACAAGACATTCATGAAAAAACAAATTATGAGGAAGCTG
CTCAACAGTTGCGAGCAATATTCCGG


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