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Chlamydia pneumoniae Search Results

Record: 1 of 1  
MiniMap IGR47 IGR48 IGR46 IGR51 IGR45 IGR49 IGR44 IGR52 IGR43 IGR50 CPn0063 CPn0064 dut, - CPn0059 CPn0055 ptsN, - CPn0060 sodM,sodA, - CPn0057 ptsN, - CPn0061 accD, - CPn0058 CPn0062 CPn0065 mrsA, - CPn0056 CPn0063 CPn0064 dut, - CPn0059 CPn0055 ptsN, - CPn0060 sodM,sodA, - CPn0057 ptsN, - CPn0061 accD, - CPn0058 CPn0062 CPn0065 mrsA, - CPn0056 CPn0064 dut, - CPn0059 CPn0055 ptsN, - CPn0060 sodM,sodA, - CPn0057 ptsN, - CPn0061 accD, - CPn0058 CPn0062 CPn0065 mrsA, - CPn0056 CPn0063
* Calculated from Protein Sequence

Gene ID: CPn0060

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
ptsN  

Definition:
nitrogen regulatory IIa domain protein (PTS IIA)(phosphotransferase)

Gene Start:
75055

Gene Stop:
75531

Gene Length:
477

Molecular Weight*:
17600

pI*:
4.70

Net Charge*:
-6.38

EC:
2.7.1.69  

Functional Class:
cellular processes; signal transduction  
central intermediary metabolism; nitrogen metabolism  

Pathway: pathway table
Aminosugars metabolism
Fructose and mannose metabolism
Galactose metabolism
Glycolysis / Gluconeogenesis
Starch and sucrose metabolism

Comment:
From Prosite PDOC00528:

The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS) is a major carbohydrate transport system in bacteria. The PTS catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane. The general mechanism of the PTS is the following: a phosphoryl group from phosphoenolpyruvate (PEP) is transferred to enzyme-I (EI) of PTS which in turn transfers it to a phosphoryl carrier protein (HPr). Phospho-HPr then transfers the phosphoryl group to a sugar-specific permease which consists of at least three structurally distinct domains (IIA, IIB, and IIC) which can either be fused together in a single polypeptide chain or exist as two or three interactive chains, formerly called enzymes II (EII) and III (EIII).

The first domain (IIA , carries the first permease-specific phosphorylation site, an histidine which is phosphorylated by phospho-HPr. The second domain (IIB) is phosphorylated by phospho-IIA on a cysteinyl or histidyl residue, depending on the permease. Finally, the phosphoryl group is transferred from the IIB domain to the sugar substrate in a process catalyzed by the IIC domain; this process is coupled to the transmembrane transport of the sugar.

Blast Summary:  PSI-Blast Search
Numerous significant hits in gapped BLAST to nitrogen regulatory IIA protein sequences; e.g. residues 30-154 are 31% similar to (Z99111) phosphotransferase system (PTS) fructose-specific enzyme IIBC component [Bacillus subtilis]; residues 33-124 are 32% similar to PTVA_ECOLI; residues 1-158 are 62% similar to CT291; residues 5-154 are 33% similar to TP0755; residues 12-154 are 27% similar to TP0085; and residues 34-155 are 24% similar to MG062. No significant similarity to U.urealyticum.

COGS Summary:  COGS Search
No hit to the COGs database.

Blocks Summary:  Blocks Search
None

ProDom Summary:  Protein Domain Search
Residues 30-151 are 39% similar to a defined domain of P71012_BACSU, defined as: COMPONENT PHOSPHOTRANSFERASE SYSTEM ENZYME PROTEIN PTS II IIA TRANSFERASE IIABC.

Paralogs:  Local Blast Search
CPn0061 is a possible paralog: residues 28-112 are 35% similar to CPn0061.

Pfam Summary:  Pfam Search
Residues 15 to 158 (E-value = 3.7e-11) place CPn0060 in the PTS_EIIA_2 family which is described as Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2 (PF00359)

PDB Hit:


Gene Protein Sequence:
MPSYCQNQQDFSLFSLLSPRLVMFLGKHSRDEILQDLTDLVDAAGLLEDK
QAFFDALVRRENIMSTGIGMGVAIPHGKLESCSNFFIAIGIHTQGILWDA
IDGALVRLVFLIGGPENAQAEYLKLLSTLTLSLREESRRQQLLQVNTIEE
VMNVFVGM$

Gene Nucleotide Sequence:  Sequence Viewer
ATGCCATCCTATTGTCAAAATCAACAAGATTTTTCTTTATTCTCTCTTTT
GTCTCCTAGACTTGTAATGTTTTTAGGCAAACACTCCCGAGATGAAATCC
TCCAAGATCTTACAGATCTTGTGGATGCTGCAGGCCTACTTGAAGACAAA
CAAGCCTTTTTTGATGCTCTTGTCCGTCGTGAAAACATCATGTCCACAGG
AATCGGAATGGGCGTGGCTATTCCTCACGGAAAACTCGAAAGCTGCTCTA
ATTTTTTTATTGCTATAGGCATCCATACGCAAGGCATTTTATGGGACGCT
ATTGACGGAGCCCTCGTACGCCTCGTCTTCTTGATCGGAGGTCCAGAAAA
TGCTCAAGCCGAATATCTCAAGTTATTATCTACTTTGACTTTATCTTTGA
GAGAAGAGTCTCGTCGTCAACAGTTGTTACAGGTGAATACGATTGAAGAA
GTCATGAATGTATTTGTGGGGATGTAA


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