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

Chlamydia pneumoniae Search Results

Record: 1 of 1  
MiniMap IGR26 IGR30 IGR27 IGR29 IGR31 ybaB, - CPn0039 CPn0034 dnaX, - CPn0040 CPn0035 CPn0036 CPn0041 ptsI, - CPn0038 pdhAB,odbA  odbB, - CPn0033 ybaB, - CPn0039 CPn0034 dnaX, - CPn0040 CPn0035 CPn0036 CPn0041 ptsI, - CPn0038 pdhAB,odbA  odbB, - CPn0033 ybaB, - CPn0039 CPn0034 dnaX, - CPn0040 CPn0035 CPn0036 CPn0041 ptsI, - CPn0038 pdhAB,odbA  odbB, - CPn0033 ptsH, - CPn0037 ptsH, - CPn0037
* Calculated from Protein Sequence

Gene ID: CPn0037

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
ptsH  

Definition:
phosphocarrier protein HPR

Gene Start:
51792

Gene Stop:
52118

Gene Length:
327

Molecular Weight*:
11843

pI*:
5.70

Net Charge*:
-2.38

EC:
 

Functional Class:
transport and binding proteins; carbohydrates, organic alcohols and acids  

Pathway: pathway table

Comment:
An essential component of the PTS system. PEP phosphorylates the HPR carrier which in turn transfers the phosphoryl group to the permease as part of the active transport of carbohydrates. A 3D structure is available.

From Prosite PDOC00318:

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 as follows: a phosphoryl group from phosphoenolpyruvate (PEP) is transferred to Enzyme I (EI) of the PTS which in turn transfers it to a phosphoryl carrier protein (HPr). Phospho-HPr then transfers the phosphoryl group to a sugar-specific permease complex (enzymes EII/EIII).

HPr is a small cytoplasmic protein of 70 to 90 amino acid residues. In some bacteria HPr is a domain in a larger protein that includes a EIII(Fru) (IIA) domain and in some cases also the EI domain. A conserved histidine in the N-terminal section of HPr serves as an acceptor for the phosphoryl group of EI. In the central part of HPr there is a conserved serine which, in Gram-positive bacteria only, is phosphorylated by an ATP-dependent protein kinase; a process which probably play a regulatory role in sugar transport.


Blast Summary:  PSI-Blast Search
Numerous significant hits in gapped BLAST to PTS Phosphocarrier Protein Hpr sequences; e.g. residues 23-107 are 37% similar to PTHP_BACSU; residues 23-102 are 32% similar to PTHP_BACST; residues 22-107 are 31% similar to PTFA_SALTY; and residues 22-107 are 31% similar to PTFA_ECOLI.
Residues 21-108 are 56% similar to CT337; and residues 25-107 are 30% similar to TP0589. No significant similarity to M.genitalium, U.urealyticum, or M.pneumoniae.

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

Blocks Summary:  Blocks Search
Residues 28-73 represent block BL00369 (PTS HPR component histidine phosphorylation site proteins proteins) with an E-value of 7.2e-11.

ProDom Summary:  Protein Domain Search
Residues 23-84 are 43% similar to a defined domain of PTHP_BACSU, defined as: PROTEIN PHOSPHOTRANSFERASE SYSTEM HPR PHOSPHOCARRIER PHOSPHORYLATION SUGAR TRANSPORT HISTIDINE-CONTAINING COMPONENT.
Residues 31-108 are 32% similar to a defined domain of O50515_STRCO, defined as: PHOSPHOCARRIER PROTEIN HPR.

Paralogs:  Local Blast Search
No paralogs found in C.pneumoniae.

Pfam Summary:  Pfam Search
Residues 21 to 104 (E-value = 1.4e-10) place CPn0037 in the PTS-HPr family which is described as PTS HPr component phosphorylation site (PF00381)

PDB Hit:


Gene Protein Sequence:
MNEPTRTYLESEKDTQDQIEELQATCIVKNAAGIHVRPAGVIVRLFDGEP
CDVHFTYAGKTINAKSIMSILMLGAPQGGEILVTIRSKEAHRILQKIQDA
FSSGFGEL$

Gene Nucleotide Sequence:  Sequence Viewer
ATGAATGAGCCTACTCGCACTTATCTAGAAAGTGAGAAAGATACACAAGA
TCAGATCGAAGAGCTCCAGGCAACTTGTATAGTTAAGAATGCAGCAGGAA
TCCATGTGCGTCCTGCAGGTGTTATTGTTCGACTCTTTGATGGAGAGCCT
TGTGATGTGCATTTCACCTACGCAGGTAAAACGATAAATGCAAAGAGTAT
CATGAGTATTCTTATGTTGGGAGCTCCACAAGGAGGAGAGATTCTTGTGA
CTATTAGAAGCAAAGAAGCTCATCGTATCTTACAAAAGATACAAGATGCG
TTTAGTTCCGGTTTTGGAGAACTATAA


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