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Chlamydia pneumoniae Search Results

Record: 1 of 1  
MiniMap IGR47 IGR48 IGR46 IGR51 IGR45 IGR49 IGR44 IGR53 IGR52 IGR43 IGR50 CPn0063 CPn0064 dut, - CPn0059 ptsN, - CPn0060 sodM,sodA, - CPn0057 ptsN, - CPn0061 accD, - CPn0058 CPn0062 CPn0065 mrsA, - CPn0056 CPn0063 CPn0064 dut, - CPn0059 ptsN, - CPn0060 sodM,sodA, - CPn0057 ptsN, - CPn0061 accD, - CPn0058 CPn0062 CPn0065 mrsA, - CPn0056 CPn0064 dut, - CPn0059 ptsN, - CPn0060 sodM,sodA, - CPn0057 ptsN, - CPn0061 accD, - CPn0058 CPn0062 CPn0065 mrsA, - CPn0056 CPn0063
* Calculated from Protein Sequence

Gene ID: CPn0061

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
ptsN  

Definition:
nitrogen regulatory IIa protein

Gene Start:
75534

Gene Stop:
76211

Gene Length:
678

Molecular Weight*:
25845

pI*:
5.40

Net Charge*:
-7.92

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 weak hits in gapped BLAST to PTS system proteins; e.g. residues 92-191 are 38% similar to PTSN_ECOLI; residues 92-191 are 37% similar to PTSN_KLEPN; residues 92-176 are 36% similar to PTSN_HAEIN; residues 1-225 are 66% similar to CT290; residues 111-187 are 33% similar to MG062; residues 92-176 are 35% similar to CT291; and residues 37-182 are 26% similar to TP0755. No significant similarity to U.urealyticum.

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

Blocks Summary:  Blocks Search
Residues 130-139 represent block BL00372 (PTS EIIA domain proteins phosphorylation site proteins proteins 2) with an E-value of 0.00052.

ProDom Summary:  Protein Domain Search
Residues 82-213 are 33% similar to a defined domain of Q51563_PSEAE, defined as: COMPONENT PHOSPHOTRANSFERASE SYSTEM ENZYME PROTEIN PTS II IIA TRANSFERASE IIABC.

Paralogs:  Local Blast Search
Cpn0060 is a possible paralog. Residues 91-176 are 35% similar to CPn0060.

Pfam Summary:  Pfam Search
No significant hits to the Pfam 11.0 database

PDB Hit:


Gene Protein Sequence:
MDLKLDEVASLLDVSEHTVLQWLKEGAIPSYSMNNEYRFSREEIENWLLH
NQALMIQERGEDKEALKDLSLKYSLYKAIHRGGVLCDVVVHSKEEALQYA
SKYIAQKFQLDESVLFEMLSHRENLMSTGIGEGIALPHAKDFLINAYYDI
VVPMFLAEPIEYGALDGKPVGILFFLFACQDKSHLNLVNKIVHLGMSLNA
RSFFKNYPNKDQLLAYVKEWESQTH$

Gene Nucleotide Sequence:  Sequence Viewer
ATGGATTTAAAGTTAGATGAAGTCGCCTCTTTGTTAGATGTTTCCGAACA
TACAGTTCTGCAATGGCTTAAAGAAGGAGCCATTCCAAGCTATAGTATGA
ATAATGAATACCGCTTTAGTCGTGAAGAAATCGAAAACTGGCTATTGCAT
AACCAAGCACTCATGATCCAAGAACGCGGCGAAGATAAAGAAGCACTTAA
AGATCTTTCTTTGAAATATAGTCTCTACAAAGCAATTCATCGTGGCGGCG
TGCTTTGCGATGTTGTGGTTCATAGTAAAGAAGAAGCTCTCCAATACGCC
TCTAAATACATCGCCCAAAAGTTTCAATTAGACGAAAGCGTACTTTTTGA
AATGCTCTCCCACAGAGAAAATCTTATGTCCACAGGTATAGGAGAAGGAA
TTGCCCTGCCCCATGCCAAAGACTTTTTAATTAATGCCTACTATGACATT
GTGGTTCCTATGTTTCTTGCAGAGCCCATAGAATACGGGGCTCTAGATGG
AAAACCTGTAGGCATTCTTTTCTTCCTTTTTGCTTGCCAGGATAAAAGTC
ACTTAAACTTAGTAAATAAAATAGTCCACCTCGGGATGTCTTTAAATGCC
CGAAGCTTTTTTAAAAATTATCCTAACAAAGATCAACTTTTAGCGTACGT
TAAGGAATGGGAGTCCCAAACTCATTAA


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