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Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR0810 IGR0807 IGR0809 IGR0806 IGR0805 IGR0808 IGR0811 IGR0804 IGR0811.1 slyD, - NG0981 crtB, - NG0980 virG,icsA, - NG0985 dsbD, - NG0978 NG0982 NG0983 NG0979 ackA, - NG0977 NG0984 slyD, - NG0981 crtB, - NG0980 virG,icsA, - NG0985 dsbD, - NG0978 NG0982 NG0983 NG0979 ackA, - NG0977 NG0984 Type: tandem, Name:  - 40 Type: tandem, Name:  - 41 slyD, - NG0981 crtB, - NG0980 virG,icsA, - NG0985 dsbD, - NG0978 NG0983 NG0979 ackA, - NG0977 NG0984 NG0982
* Calculated from Protein Sequence

Gene ID: NG0981

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
slyD  

Definition:
FKBP-type peptidyl-prolyl cis-trans isomerase SlyD

Gene Start:
952384

Gene Stop:
951905

Gene Length:
480

Molecular Weight*:
17329

pI*:
4.30

Net Charge*:
-20.34

EC:
5.2.1.8  

Functional Class:
Translation; Protein modification and translation factors  

Pathway: pathway table

Secondary Evidence:
Roof,W.D., Horne,S.M., Young,K.D. and Young,R. slyD, a host gene required for phi X174 lysis, is related to the FK506-binding protein family of peptidyl-prolylcis-trans-isomerases. J. Biol. Chem. 269 (4): 2902-2910 (1994) [Medline: 94132064].

Hottenrott,S., Schumann,T., Pluckthun,A., Fischer,G. andRahfeld,J.U. The Escherichia coli SlyD is a metal ion-regulated peptidyl-prolyl cis/trans-isomerase. J. Biol. Chem. 272 (25): 15697-15701 (1997) [Medline: 97332650].

Comment:
From GenBANK (gi:548939): SlyD is required for lysis of phix174 infected cells. It binds nickel and zinc with high affinity and 1:1 stoichiometry, copper and cobalt with lower affinity. There is no binding detectable for ferrous, ferric, magnesium and calcium ions. The activity of SlyD is considerably smaller than the one found in other PPIases with the same substrate. The substrate specificity carried out with suc-ala-xaa-pro-phe-4na, where xaa is the aa tested, was found to be phe > ala > leu. PPIases accelerate the folding of proteins. SlyD performs in the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Its activity is reversibly regulated by binding of three nickel ions to the histidine-rich region. This cytoplasmic protein belongs to the FKBP-type PPIase family.

See also SlyX, NG2017.

Oklahoma ID: NGO.981c

Blast Summary:  PSI-Blast Search
NG0981 is orthologous to AE002501, N. meningitidis MC58 FKBP-type peptidyl-prolyl cis-trans isomerase SlyD : residues 1-147 have 97% similarity to residues 1-147 in NG0981.

NG0981 also has significant (P-value < 1e-10) hits to SlyD protiens in several other organisms; e.g. residues 1-147 are 41% similar to 11350740 of Pseudomonas aeruginosa.

COGS Summary:  COGS Search
BeTs to 7 clades of COG1047
COG name: FKBP-type peptidyl-prolyl cis-trans isomerases 2
Functional Class:  O
The phylogenetic pattern of COG1047 is aMtk----E--huj---l---
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
No significant hits to the Blocks database.

ProDom Summary:  Protein Domain Search
No significant hit to the ProDom database.

Paralogs:  Local Blast Search


NG0981 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.


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

Structural Feature(s):
Feature Type  Start  Stop
non-globular  
1  
160

PDB Hit:
No hits to the PDB database.

Gene Protein Sequence:
MAIAKNSVVSLHYEMYDANNQLLDKTEEPIAYLHGGYDGIFPLVEEALHG
KDAGDTVDVALSSDDAFGEQDSELVRIEDAGAFPVEVEVGMMFEADDPET
GDVVVYRVTDVADGKAVVDGNHPLAGMKIRFKATVESVRDASDEEIAHGH
VHGSHGHYHH

Gene Nucleotide Sequence:  Sequence Viewer
ATGGCTATTGCAAAAAATTCCGTGGTTTCGCTGCATTATGAGATGTATGA
TGCCAACAATCAGCTTTTGGATAAAACCGAAGAACCGATTGCGTATCTGC
ACGGCGGTTACGACGGCATTTTCCCTTTGGTGGAAGAGGCGTTGCACGGT
AAGGATGCCGGCGATACGGTCGATGTGGCGCTTTCGTCCGACGATGCGTT
CGGCGAGCAGGATTCGGAGTTGGTCCGTATTGAAGATGCGGGCGCGTTCC
CTGTTGAAGTCGAAGTCGGCATGATGTTTGAAGCCGACGATCCTGAAACC
GGCGATGTTGTCGTCTATCGTGTAACCGATGTTGCCGACGGCAAGGCGGT
GGTGGACGGCAACCATCCTTTGGCAGGCATGAAAATCCGCTTTAAAGCTA
CGGTTGAAAGCGTGCGCGATGCATCCGATGAGGAAATCGCACACGGTCAT
GTCCACGGTTCGCACGGTCATTACCACCAC


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