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Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR0635 IGR0639 IGR0643 IGR0640 IGR0637 IGR0642 IGR0638 IGR0641 IGR0636 NG0768 NG0761 cca, - NG0763 yjjK,yahG,ybiT, - NG0764 NG0762 NG0765 recR, - NG0767 lolC, - NG0769 ppiD, - NG0766 recD, - NG0771 NG0768 NG0761 cca, - NG0763 yjjK,yahG,ybiT, - NG0764 NG0762 NG0765 recR, - NG0767 lolC, - NG0769 ppiD, - NG0766 recD, - NG0771 NG0768 NG0761 cca, - NG0763 yjjK,yahG,ybiT, - NG0764 NG0762 NG0765 recR, - NG0767 lolC, - NG0769 ppiD, - NG0766 recD, - NG0771 lolD, - NG0770 lolD, - NG0770
* Calculated from Protein Sequence

Gene ID: NG0766

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
ppiD  

Definition:
peptidyl-prolyl cis-trans isomerase

Gene Start:
760501

Gene Stop:
762036

Gene Length:
1536

Molecular Weight*:
56704

pI*:
6.10

Net Charge*:
-5.54

EC:
5.2.1.8  

Functional Class:
Translation; Protein modification and translation factors  

Pathway: pathway table

Secondary Evidence:
Dartigalongue,C. and Raina,S. A new heat-shock gene, ppiD, encodes a peptidyl-prolyl isomerase required for folding of outer membrane proteins in Escherichia coli. EMBO J. 17 (14): 3968-3980 (1998) [Medline: 98336187].

Comment:
From GenBANK (gi:2499780): PPIases accelerate the folding of proteins. PPID seems to be involved in the folding of outer membrane proteins. Its preference at the p1 position of the peptide substrate is glu > leu > ala > his > val > phe > ile > gly > lys > thr. PPID performs cis-trans isomerization of proline imidic peptide bonds in oligopeptides. This type II membrane protein is induced by heat shock and belongs to the PPIC/parvulin family of rotamases.

See also ppiA (NG0544) and ppiB (NG0376).

Oklahoma ID: NGO.766

Blast Summary:  PSI-Blast Search
Several significant hits in gapped BLAST to peptidyl-prolyl cis-trans isomerases; e.g. residues 13-307 are 24% similar to 2499780 of Escherichia coli.

NG0766 is orthologous to AE002472, N. meningitidis MC58 peptidyl-prolyl cis-trans isomerase-related protein: residues 1-512 have 96% similarity to residues 1-512 in NG0766.


COGS Summary:  COGS Search
BeTs to 6 clades of COG0760
COG name: Parvulin-like peptidyl-prolyl isomerase
Functional Class:  O
The phylogenetic pattern of COG0760 is ----yQVcEB-HUJ--ol--X
Number of proteins in this genome belonging to this COG is 3

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

ProDom Summary:  Protein Domain Search
Residues 12-245 are 25% similar to a (PROTEIN ISOMERASE PEPTIDYL-PROLYL) protein domain (PD013665) which is seen in CYPD_HAEIN.

Residues 254-465 are 22% similar to a (ISOMERASE PEPTIDYL-PROLYL CIS-TRANS D) protein domain (PD023956) which is seen in CYPD_ECOLI.



Paralogs:  Local Blast Search


NG0766 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
cleavable N-terminal sequence  
1  
32
coil-coil  
255  
285
coil-coil  
356  
404
non-globular  
416  
512

PDB Hit:
No hits to the PDB database.

Gene Protein Sequence:
MFHSIEKYRTPAQVLLGLIALTFVGFGVSTVSHPGADYIVQVGDEKISEH
SINNAMQNEQADGGSPWRDAVFQSLLQRAYLKQGAKLMGISVSSEQIKQM
IVDDPNFHDANGKFSHALLSQYLSQRHMSEDQFVEEIRDQFALQNLVSLV
QNGVLVGDAQAEQLIRLTQVNRTIRSHTFNPDEFIAQVKASEADLQKFYN
ANKKDYLLPQAVKLEYVALNLKDFADKQTVSETEVKNAFEERVARLPAHE
AKPSFEQEKAAVENELKMKKAVADFNKAKEKLGDDAFNHPSSLAEAAKNS
GLKVETQETWLSRQDAQMSGMPENLINAVFSDDVLKKKHNSEVLTINSET
AWVVRAKEVREEKNLLFEEAKDAVRQAYIRTEAAKLAENKAKEVLTQLNG
GKAVDVKWSEVSVLGAQQARQSMPPEAYAELLKAKPANGKPAYVRLTGLP
APVIVEAQAVTPPEDIAAQLPPAKQALAQQQSANTFDLLIRYFNGKIKQT
KGAQSVDNGDGQ

Gene Nucleotide Sequence:  Sequence Viewer
ATGTTCCATTCCATCGAAAAATACAGAACACCCGCCCAAGTCTTATTAGG
CCTGATTGCATTAACTTTTGTCGGCTTCGGCGTCAGCACGGTTTCCCATC
CGGGCGCCGACTACATCGTCCAAGTGGGCGACGAAAAAATCAGCGAGCAC
TCAATCAACAACGCCATGCAGAACGAGCAGGCGGACGGCGGCAGCCCTTG
GCGCGACGCGGTGTTCCAATCCCTGCTGCAACGCGCCTACCTGAAACAGG
GCGCGAAGCTGATGGGCATTTCGGTTTCTTCCGAACAAATCAAGCAGATG
ATTGTGGACGATCCCAATTTCCACGACGCAAACGGCAAATTCAGTCACGC
GCTTTTGAGTCAATACCTGTCGCAACGCCATATGTCTGAAGACCAGTTTG
TCGAAGAAATCCGCGATCAGTTTGCCTTGCAGAATTTGGTAAGCCTCGTC
CAAAACGGCGTATTGGTCGGCGACGCGCAGGCGGAACAGCTGATCAGGCT
GACGCAGGTCAACCGCACCATCCGTTCGCACACTTTCAACCCCGACGAGT
TCATCGCCCAAGTCAAAGCGTCTGAAGCCGATTTGCAGAAATTTTATAAT
GCGAACAAAAAAGACTATCTGCTGCCGCAGGCGGTCAAATTGGAATATGT
CGCCTTGAATCTGAAGGATTTTGCAGACAAGCAGACCGTCAGTGAAACGG
AAGTGAAAAATGCGTTTGAAGAGCGCGTGGCGCGTTTGCCGGCACATGAA
GCCAAACCTTCTTTCGAGCAGGAAAAAGCCGCCGTCGAAAACGAATTGAA
AATGAAAAAGGCGGTTGCCGACTTCAACAAGGCAAAAGAAAAGCTGGGCG
ACGATGCGTTCAATCATCCCTCCTCGCTTGCCGAAGCCGCCAAAAACAGC
GGTTTGAAAGTGGAAACCCAAGAAACTTGGCTGAGCAGGCAGGACGCACA
AATGTCCGGCATGCCCGAAAACCTAATCAATGCCGTATTCAGCGACGACG
TATTGAAGAAAAAACACAATTCCGAAGTGCTGACCATCAACAGCGAAACC
GCGTGGGTCGTCCGCGCCAAAGAAGTCCGCGAAGAAAAAAACCTACTGTT
TGAAGAAGCCAAAGATGCGGTGCGTCAGGCCTATATCCGTACCGAAGCCG
CCAAACTTGCCGAAAACAAGGCAAAAGAAGTGCTTACCCAACTGAACGGC
GGCAAGGCAGTTGACGTGAAATGGTCGGAAGTGTCCGTTTTGGGCGCGCA
GCAGGCAAGGCAGTCCATGCCGCCCGAGGCTTATGCGGAACTGCTGAAAG
CAAAACCGGCAAACGGCAAACCCGCCTATGTCAGACTGACCGGTCTGCCG
GCACCCGTGATTGTCGAGGCGCAGGCAGTCACGCCTCCGGAGGATATTGC
CGCACAGCTTCCTCCTGCGAAACAGGCTTTGGCGCAACAGCAGTCTGCCA
ATACTTTCGACCTGCTGATCCGCTATTTCAACGGAAAAATCAAACAGACT
AAAGGAGCACAATCGGTTGACAACGGCGATGGTCAG


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