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Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR0473 IGR0472 IGR0475 IGR0477 IGR0474 IGR0476 IGR0478 NG0569 creA,rob, - NG0570 cyn,cah, - NG0574 NG0567 ctpA, - NG0572 NG0571 uvrB, - NG0573 NG0569 creA,rob, - NG0570 cyn,cah, - NG0574 NG0567 ctpA, - NG0572 NG0571 uvrB, - NG0573 Type: tandem, Name:  - 30 creA,rob, - NG0570 cyn,cah, - NG0574 NG0568 NG0569 NG0568 NG0567 ctpA, - NG0572 NG0571 uvrB, - NG0573
* Calculated from Protein Sequence

Gene ID: NG0572

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
ctpA  

Definition:
carboxy-terminal processing protease

Gene Start:
555789

Gene Stop:
557261

Gene Length:
1473

Molecular Weight*:
52725

pI*:
9.60

Net Charge*:
6.49

EC:
3.4.-.-  

Functional Class:
Translation; Degradation of proteins, peptides, and glycopeptides  

Pathway: pathway table
Biotin metabolism
Lysine degradation

Primary Evidence:
Black,C.G., Fyfe,J.A. and Davies,J.K., A promoter associated with the neisserial repeat can be used to transcribe the uvrB gene from Neisseria gonorrhoeae, J. Bacteriol. 177 (8), 1952-1958 (1995). Medline: 95238263


Secondary Evidence:
Mitchell,S.J. and Minnick,M.F. A carboxy-terminal processing protease gene is located immediately upstream of the invasion-associated locus from Bartonellabacilliformis. Microbiology 143 (Pt 4): 1221-1233 (1997) Medline: 97286538.
Shestakov,S.V., Anbudurai,P.R., Stanbekova,G.E., Gadzhiev,A.,Lind,L.K. and Pakrasi,H.B. Molecular cloning and characterization of the ctpA gene encoding a carboxyl-terminal processing protease. Analysis of a spontaneousphotosystem II-deficient mutant strain of the cyanobacteriumSynechocystis sp. PCC 6803. J. Biol. Chem. 269 (30): 19354-19359 (1994) Medline: 94308215.
Anbudurai,P.R., Mor,T.S., Ohad,I., Shestakov,S.V. and Pakrasi,H.B. The ctpA gene encodes the C-terminal processing protease for the D1 protein of the photosystem II reaction center complex. Proc. Natl. Acad. Sci. U.S.A. 91 (17): 8082-8086 (1994) Medline: 94336690.

Comment:
Fron GenBANK (gi:6226805): This protein may degrade proteins with nonpolar C-termini and may be involved in protection of the bacterium from thermal and osmotic stresses. It may be secreted may undergo autocatalytic processing at the c-terminus (398-434 or 425-434 missing).

Fron GenBANK (gi:6226806): The function of CtpA is the cleavage of the 16 C-terminal residues from the D1 precursor of photosystem II.

From Medline (94308215): Hydrophobicity analysis of the amino acid sequence suggested that this protein is largely hydrophilic. A stretch of the first 31 amino-terminal residues of the polypeptide resembled a bacterial signal peptide and may be responsible for the translocation of this protein to the lumen space of the thylakoid membranes. The spontaneous photosynthesis-disabling mutation in the SK18 strain was identified to be a single nucleotide change introducing a premature termination codon in this ORF. The predicted sequence of the encoded protein showed significant similarity to that of the Prc protein, a carboxyl-terminal processing protease in Escherichia coli. The cyanobacterial protein encoded by ORF427 is a similar processing protease, the gene ctpA (carboxyl-terminal processing protease).

From Medline (94336690): The D1 protein of the photosystem II (PSII) complex in the thylakoid membrane of oxygenic photosynthetic organisms is synthesized as a precursor polypeptide (pD1) with a C-terminal extension. Posttranslational processing of the pD1 protein is essential to establish water oxidation activity of the PSII complex. A mutation in a gene, ctpA, resulted in a loss of PSII activity in the cyanobacterium Synechocystis sp. PCC 6803. The resultant mutant strain, T564, had no PSII-mediated water oxidation activity, but it had normal cytochrome b6f and photosystem I activities. Measurements of thermoluminescence profiles and rates of reduction of 2,6-dichlorophenolindophenol indicated that PSII complexes in the mutant cells had functional reaction centers that were unable to accept electrons from water. Immunoblot analysis showed that D1, D2, CP47, CP43, and the alpha subunit of cytochrome b559, five integral membrane proteins of PSII, were present in T564 cells. Interestingly, the D1 protein in the mutant cells was 2 kDa larger than that in wild-type cells, due to the presence of a C-terminal extension. We conclude that the CtpA protein is a processing enzyme that cleaves off the C-terminal extension of the D1 protein. Interestingly, the CtpA protein shows significant sequence similarity to the interphotoreceptor retinoid-binding proteins in the bovine, human, and insect eye systems.

Oklahoma ID: NGO.572

Blast Summary:  PSI-Blast Search
NG0572 is 99% identical to a previously sequenced N.gonorrhoeae protein in GenBank, 555748.

Numerous significant hits in gapped BLAST to carboxyl-terminal proteases; e.g. residues 3-427 are 49% similar to gb|AAG08519.1|AE004926_9 (AE004926) probable carboxyl-terminal protease of Pseudomonas aeruginosa.

Residues 1-484 are 98% similar to NMA1546 and NMB1332, carboxy-terminal processing proteases of N.meningitidis (11279532, 11279533).



COGS Summary:  COGS Search
BeTs to 10 clades of COG0793
COG name: Periplasmic protease
Functional Class:  M
The phylogenetic pattern of COG0793 is -----qvCeB-huj--olinx
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
***** IPB003581 (Tail specific protease) with a combined E-value of 5.7e-21.
    IPB003581B    240-249
    IPB003581C    315-344


ProDom Summary:  Protein Domain Search
Residues 96-172 are 39% similar to a (CARBOXYL-TERMINAL PROTEASE CTP PROTEASE) protein domain (PD211153) which is seen in O83301_TREPA.

Residues 174-387 are 50% similar to a (PROTEASE CARBOXYL-TERMINAL PRECURSOR) protein domain (PD004132) which is seen in Q9ZF67_BARQU.

Residues 102-172 are 61% similar to a (PROTEIN DOMAIN PROTEASE PDZ) protein domain (PD000073) which is seen in Q9ZF67_BARQU.



Paralogs:  Local Blast Search


NG0572 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.


Pfam Summary:  Pfam Search
Residues 95 to 173 (E-value = 9.9e-12) place NG0572 in the PDZ family which is described as PDZ domain (Also known as DHR or GLGF) (PF00595)
Residues 201 to 388 (E-value = 2.6e-73) place NG0572 in the Peptidase_S41 family which is described as Peptidase family S41B (PF03572)

Structural Feature(s):
Feature Type  Start  Stop
gram negative signal  
1  
30
uncleavable N-terminal sequence N-terminal sequence  
1  
23
transmembrane  
9  
25
non-globular  
215  
329
transmembrane  
253  
269
non-globular  
383  
491

PDB Hit:
pdb|1FC6|1FC6-A PHOTOSYSTEM II D1 C-TERMINAL PROCESSING PROTEASE153.0 6e-38
pdb|1FC7|1FC7-A PHOTOSYSTEM II D1 C-TERMINAL PROCESSING PROTEASE151.0 3e-37
pdb|1FC6|1FC6-A PHOTOSYSTEM II D1 C-TERMINAL PROCESSING PROTEASE120.0 7e-28

Gene Protein Sequence:
MSKPVFKKIALYTLGAISGVAVSLAVQGFAAEKDGRDNEVLPVQSIRTMA
EVYGQIKANYYHDKPDADLFEGAMKGMVAGLDPHSEYMDKKGYAEIKEST
SGEFGGLGMEIGQEDGFVKVVSPIEDTPAERAEVKSGDFIVKIDNVSTRG
MTVSEAVKKMRGKPGTKITLTLSRKNADKPIVVNLTRAIIKVKSVRHHLI
EPDYGYIRVSQFQERTVESVNTAAKELVKENKGKPLKGLVLDLRDDPGGL
LTGAVGVSAAFLPSEAVVVSTKGRDGKDGMVLKAVPEDYVYGMGGDPLAG
IPAELKTIPMTVLVNSGSASASEIVAGALQDHKRAVIVGTQSFGKGSVQT
LIPLSNGSAVKLTTALYYTPNDRSIQAQGIVPDVEVKDKERTFESREADL
VGHIGNPLGGEDVNSETLAVPLEKDADKPAAKEKGKKKKDEDLSSRRIPN
PAKDDQLRKALDLVKSPEQWQKSLGLAAKKPVSNKDKKDKK

Gene Nucleotide Sequence:  Sequence Viewer
ATGTCGAAACCTGTTTTTAAGAAAATCGCACTTTATACTTTGGGTGCAAT
CAGCGGCGTGGCCGTAAGTCTGGCGGTGCAGGGTTTTGCCGCCGAGAAGG
ACGGGCGGGATAACGAAGTCCTGCCGGTGCAATCCATCCGTACGATGGCG
GAGGTTTACGGTCAGATTAAGGCAAACTACTATCATGACAAACCCGATGC
CGATTTGTTTGAAGGTGCGATGAAGGGTATGGTGGCCGGTTTGGATCCGC
ATTCCGAATATATGGATAAAAAAGGTTATGCCGAGATAAAGGAGTCCACC
AGCGGCGAATTTGGCGGCTTGGGGATGGAAATCGGGCAGGAAGACGGTTT
TGTCAAAGTGGTTTCGCCGATTGAGGACACGCCTGCCGAACGGGCGGAGG
TGAAAAGCGGCGATTTCATTGTGAAAATCGATAATGTTTCGACGCGCGGT
ATGACGGTCAGCGAAGCGGTGAAAAAAATGCGGGGCAAGCCGGGTACGAA
GATTACTTTGACGTTGTCGCGCAAAAATGCCGACAAGCCGATAGTCGTCA
ACCTGACCCGTGCCATTATTAAAGTGAAAAGCGTCCGCCATCACCTGATC
GAACCCGATTACGGCTATATCCGCGTGTCGCAGTTCCAAGAGCGGACGGT
CGAAAGCGTCAATACCGCCGCAAAAGAGCTGGTAAAGGAAAATAAAGGAA
AACCGCTCAAGGGGCTGGTGTTGGATTTGCGCGACGACCCCGGCGGGCTT
TTGACCGGCGCGGTCGGCGTGTCGGCGGCGTTTCTGCCGTCTGAAGCGGT
CGTCGTCAGCACCAAGGGACGCGACGGCAAAGACGGCATGGTACTGAAAG
CCGTTCCCGAGGATTATGTGTACGGTATGGGCGGCGACCCTTTGGCGGGT
ATTCCTGCCGAGTTGAAAACGATTCCGATGACGGTATTGGTCAATTCCGG
TTCGGCTTCCGCGTCGGAGATTGTCGCCGGCGCATTGCAGGACCACAAAC
GCGCGGTCATCGTCGGTACGCAGAGCTTCGGTAAAGGTTCGGTTCAGACT
TTGATTCCTTTGTCCAACGGCAGCGCGGTCAAGTTGACGACCGCCCTGTA
TTACACGCCGAACGACCGTTCCATTCAGGCACAGGGGATTGTTCCCGATG
TCGAAGTAAAAGATAAGGAACGTACTTTTGAAAGCCGCGAGGCGGACCTG
GTCGGACACATCGGCAATCCCTTGGGCGGCGAGGATGTGAACAGTGAAAC
CCTTGCCGTACCGCTTGAAAAAGATGCGGATAAGCCCGCTGCAAAAGAAA
AAGGTAAAAAGAAAAAGGACGAGGATTTGTCTTCAAGGCGGATTCCGAAC
CCTGCGAAAGACGATCAGTTGCGTAAGGCTTTGGATTTGGTCAAGTCGCC
CGAGCAGTGGCAGAAGTCTTTGGGGCTGGCGGCGAAAAAACCGGTTTCAA
ATAAAGATAAAAAAGATAAGAAG


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