Basic Search | Intermediate Search | Advanced SQL Search | Gene Image Map |  Home

Chlamydia trachomatis Search Results

Record: 1 of 1  
MiniMap IGR593 IGR591 IGR589 IGR592 IGR590 IGR594 CT718 nifU, - CT720 fliF, - CT719 gpsA,gpdA, - CT714 ompB, - CT713 nifS,yfhO, - CT721 fliI, - CT717 CT715 CT712 CT718 nifU, - CT720 fliF, - CT719 gpsA,gpdA, - CT714 ompB, - CT713 nifS,yfhO, - CT721 fliI, - CT717 CT715 CT712 CT718 nifU, - CT720 fliF, - CT719 gpsA,gpdA, - CT714 ompB, - CT713 nifS,yfhO, - CT721 fliI, - CT717 CT715 CT716 pgmA,gpmA, - CT722 CT716 pgmA,gpmA, - CT722 CT712
* Calculated from Protein Sequence

Gene ID: CT717

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
fliI  

Definition:
probable flagellar-type ATP synthase (beta subunit)

Gene Start:
830091

Gene Stop:
828790

Gene Length:
1302

Molecular Weight*:
47592

pI*:
7.05

Net Charge*:
0.40

EC:
3.6.1.34  

Functional Class:
cellular processes; secretion  

Pathway: pathway table
Energy Metabolism; Oxidative phosphorylation
Membrane Transport; Type III secretion system

Comment:
Possibly a catalytic subunit for a protein translocase or a proton translocase.

See CT718, CT719 and the comment to CT714.

From Prosite PDOC00137:

TP 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.

In order to detect these ATPase subunits, we took a segment of ten amino-acid residues, containing two conserved serines, as a signature pattern. The first serine seems to be important for catalysis - in the ATPase alpha chain at least - as its mutagenesis causes catalytic impairment.


Blast Summary:  PSI-Blast Search
Numerous hits in gapped BLAST to probable flagellum-specific ATP synthase proteins, e.g., 36% similarity to HRB6_XANCV, 35% similarity to FLII_ECOLI, 34% similarity to FLII_BACSU.
CT717 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.
CT717 is orthologously related to CPn0858: residues 1-427 are 68% similar to CPn0858.

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 86-111, 233-244, 252-296 are significantly matched to BL00152A,B,C, concerned with ATP synthase alpha and beta subunits proteins, e.g. ATP2_HEVBR and ATPA_HALVO.

ProDom Summary:  Protein Domain Search
Residues 215 to 378 are 37% similar to an ATP synthase chain subunit beta domain as seen in SPAL_SALTY. Residues 145 to 192 are 60% similar to an ATP synthase chain subunit beta V-ATPase domain as seen in Y4YI_RHISN.

Paralogs:  Local Blast Search
This protein is paralogously related to four other CT proteins:
CT669, flagellar type ATPase, CT307, ATP synthase beta chain,
CT308, ATP synthase alpha chain, CT491, transcription termination
factor rho. Residues 21-427 are 36% similar to CT669, residues 23-396
are 24% similar to CT307, residues 134-303 are 29% similar to CT308,
residues 146-307 are 27% similar to CT491.

Pfam Summary:  Pfam Search
Residues 183 to 357 (E-value = 6.7e-50) place CT717 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
transmembrane  
59  
81
non-globular  
84  
152
transmembrane  
218  
238

PDB Hit:
gi|2981976|pdb|1SKY|B Chain B, 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:
MTHLQEETLLIHQWRPYRECGILSRISGSLLEAQGLSACLGELCQISLSR
SDPILAEVIGIHNRTTLLLALTPIYYLAIGAEVVPLRRPASLPLSNHLLG
RVLDGFGNPLDGGPQLPKTNLSPLFSSPPSPMSRTPIQEVFPTGIRAIDA
LLTIGEGQRVGIFSEPGGGKSSLLSTIAKGSQQTINVIALIGERGREVRD
YVNQHKEGLAAQRTVIIASTAYETAASKVIAGRAAITIAEYFRDQGARVL
FTMDSLSRWIESLQEVAIARGETLSTHHYAASVFHHVAEFLERAGNNDKG
SITSFYAILHYANHPDIFTDYVKSLLDGHFFLSPQEKSFSSPPINVLTSL
SRSSRQLALPHHYAAAQELLSLLKAYHEAIDIIQLGAYVSGQDAHLDRAI
RLLPSVKQFLSQPYSHYSAIHETIEQLCQLLKHE

Gene Nucleotide Sequence:  Sequence Viewer
ATGACTCATTTACAAGAAGAAACTCTGTTGATCCATCAATGGCGCCCGTA
TCGAGAATGTGGGATTTTATCACGCATATCAGGATCTCTTCTGGAAGCTC
AAGGGCTCTCCGCATGCTTAGGAGAACTCTGTCAAATTTCTCTATCTCGG
TCAGACCCTATTCTAGCTGAAGTAATTGGCATTCACAATCGCACGACATT
ATTACTCGCTCTGACTCCCATATACTATCTTGCCATAGGAGCCGAAGTAG
TTCCCTTACGCAGGCCTGCCTCTCTTCCTCTATCCAACCATCTTTTAGGA
AGAGTCCTTGATGGATTCGGGAACCCTTTAGATGGAGGACCTCAGCTCCC
TAAAACGAACCTTTCCCCTCTATTTTCTTCTCCCCCTTCTCCTATGTCGC
GTACTCCGATCCAAGAGGTATTCCCTACAGGTATCCGCGCAATCGACGCC
CTACTTACCATAGGAGAAGGACAACGCGTAGGCATCTTTTCAGAGCCTGG
AGGAGGGAAATCTTCTCTTCTGTCTACGATAGCAAAGGGTTCCCAACAGA
CAATCAATGTCATTGCCCTAATAGGAGAACGTGGTCGTGAGGTGCGCGAC
TATGTCAACCAACACAAAGAAGGCCTAGCCGCTCAACGTACCGTTATCAT
CGCCTCTACCGCTTATGAAACTGCAGCTAGCAAAGTCATTGCAGGCCGCG
CAGCAATCACAATCGCAGAATATTTTCGAGATCAAGGAGCTCGCGTATTA
TTTACTATGGATTCCTTATCTAGATGGATAGAATCCCTTCAAGAAGTAGC
GATCGCGAGAGGAGAGACACTATCTACACACCACTATGCTGCATCCGTTT
TCCATCATGTTGCAGAGTTCCTAGAACGTGCTGGGAATAATGATAAAGGA
TCTATCACATCTTTTTATGCCATTTTGCATTACGCAAACCATCCAGATAT
TTTTACTGATTATGTAAAATCTCTTCTGGATGGGCATTTCTTTCTCTCCC
CTCAAGAAAAAAGCTTTTCTTCTCCTCCTATCAATGTATTAACGAGCCTT
TCGCGGTCTTCTCGTCAGTTAGCTCTCCCTCATCATTATGCTGCAGCTCA
AGAGCTTCTCTCCTTACTCAAAGCCTATCATGAAGCTATTGATATCATCC
AACTAGGAGCTTATGTCTCAGGACAAGATGCTCACCTCGATAGAGCCATT
CGTTTGCTCCCCTCCGTAAAACAATTCTTATCTCAACCTTATTCTCATTA
CTCAGCTATTCATGAAACTATTGAACAACTGTGCCAACTGTTGAAACATG
AA


Los Alamos National Laboratory     
Operated by the University of California for the National Nuclear Security Administration,
of the US Department of Energy.     Copyright © 2001 UC | Disclaimer/Privacy