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Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR1404 IGR1401 IGR1405 IGR1400 IGR1399 IGR1403 IGR1402 IGR1398 NG1720 dsbA, - NG1717 surA, - NG1714 ostA, - NG1715 trpC, - NG1721 NG1719 NG1716 mviN, - NG1718 recQ, - NG1722 NG1720 dsbA, - NG1717 surA, - NG1714 ostA, - NG1715 trpC, - NG1721 NG1719 NG1716 mviN, - NG1718 recQ, - NG1722 NG1720 dsbA, - NG1717 surA, - NG1714 ostA, - NG1715 trpC, - NG1721 NG1719 NG1716 mviN, - NG1718 recQ, - NG1722
* Calculated from Protein Sequence

Gene ID: NG1717

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
dsbA  

Definition:
thiol:disulfide interchange protein (DsbA)

Gene Start:
1678097

Gene Stop:
1677396

Gene Length:
702

Molecular Weight*:
25406

pI*:
5.70

Net Charge*:
-3.93

EC:
5.3.4.1  

Functional Class:
Translation; Protein modification and translation factors  

Pathway: pathway table

Secondary Evidence:
Hayashi,S., Abe,M., Kimoto,M., Furukawa,S. and Nakazawa,T.
The dsbA-dsbB disulfide bond formation system of Burkholderia cepacia is involved in the production of protease and alkaline phosphatase, motility, metal resistance, and multi-drug resistance.
Microbiol. Immunol. 44 (1): 41-50 (2000)
Medline: 20174740.

Thony-Meyer,L., Fischer,F., Kunzler,P., Ritz,D. and Hennecke,H. Escherichia coli genes required for
cytochrome c maturation
Journal of bacteriology. 177 (15), 4321-4326 (1995)
MEDLINE: 95362656

Comment:
From GenBANK (gi:11132451): DsbA is involved in disulfide-bond formation. It acts by transferring its disulfide bond to other proteins. It is involved in the production of protease and alkaline phosphatase, motility, metal resistance, and multi-drug resistance. This periplasmic protein belongs to the thioredoxin family, DsbA subfamily.

See also: DsbA, NG1548; DsbB, NG1292; DsbC, NG1438; and DsbD, NG0978.

Oklahoma ID: NGO.1717c

Blast Summary:  PSI-Blast Search
Residues 1-234 in NG1717 have 97% similarity to residues 1-232 in
AE002384, N. meningitidis MC58 thiol:disulfide interchange protein DsbA.

Many significant hits in gapped BLAST to thiol-disulfide interchange protein dsbA; e.g. residues 36-230 in NG1717 have 34% similarity to residues 16-208 in AB012578, B. cepacia DsbA; residues 42-234 in NG1717 have 29% similarity to residues 26-214 in L76098, A. vinelandii disulfide oxidoreductase.

COGS Summary:  COGS Search
BeTs to 6 clades of COG0526
COG name: Thiol-disulfide isomerase and thioredoxins
Functional Class:  O,C
The phylogenetic pattern of COG0526 is AMTkYQVCEBRHUJgpoLINX
Number of proteins in this genome belonging to this COG is 7

Blocks Summary:  Blocks Search
***** IPB001853 (DSBA oxidoreductase) with a combined E-value of 1.8e-15.
    IPB001853A    43-55
    IPB001853B    69-83
    IPB001853D    167-205


ProDom Summary:  Protein Domain Search
Residues 49-221 are 27% similar to a (REDOX-ACTIVE CENTER PROTEIN PRECURSOR) protein domain (PD004627) which is seen in DSBA_PSEAE.



Paralogs:  Local Blast Search


NG1717 is paralogously related to NG1548 (thiol-disulfide isomerase (DsbA)) (5e-54).


Pfam Summary:  Pfam Search
Residues 68 to 227 (E-value = 1.4e-06) place NG1717 in the DSBA family which is described as DSBA-like thioredoxin domain (PF01323)

Structural Feature(s):
Feature Type  Start  Stop
may be a lipoprotein  
  
gram negative signal  
1  
19
non-globular  
20  
44

PDB Hit:
pdb|1A23|1A23 SOLUTION NMR STRUCTURE OF REDUCED DSBA FROM 53.5 4e-08
pdb|1BED|1BED STRUCTURE OF DISULFIDE OXIDOREDUCTASE 51.5 1e-07
pdb|1FVJ|1FVJ-A THE 2.06 ANGSTROM STRUCTURE OF THE H32Y MUTANT 51.2 2e-07
pdb|1BQ7|1BQ7-A DSBA

Gene Protein Sequence:
MKSRHLALALGVAALFALAACDSKVQTSVPADSAPAASAAAAPAGLVEGQ
NYTVLANPIPQQQAGKVEVLEFFGYFCPHCARLEPVLSKHAKSFKDDMYL
RTEHVVWQKEMLPLARLAAAVDMAAAESKDVANSHIFDAMVNQKIKLQEP
EVLKKWLGEQTAFDGKKVLAAYESPESQARAGKMQELTETFQIDGTPTVI
VGGKYKVEFADWESGMNTIDLLADKVREEQKAAQ

Gene Nucleotide Sequence:  Sequence Viewer
ATGAAATCCAGACACCTCGCCCTCGCCCTCGGCGTTGCCGCCCTGTTCGC
CCTTGCCGCGTGCGACAGCAAAGTCCAAACCAGCGTCCCCGCCGACAGCG
CGCCTGCCGCTTCGGCAGCCGCCGCCCCGGCAGGACTGGTCGAAGGGCAA
AACTACACCGTCCTTGCCAACCCGATTCCCCAACAGCAGGCAGGCAAGGT
TGAAGTGCTTGAGTTTTTCGGCTATTTTTGTCCGCACTGCGCCCGCCTCG
AACCTGTTTTGAGCAAACACGCCAAGTCTTTTAAAGACGATATGTACCTG
CGTACCGAACACGTCGTCTGGCAGAAAGAAATGCTGCCGCTGGCACGCCT
CGCCGCCGCCGTCGATATGGCTGCCGCCGAAAGCAAAGATGTGGCGAACA
GCCATATTTTCGATGCGATGGTCAACCAAAAAATCAAGCTGCAAGAGCCG
GAAGTCCTCAAAAAATGGCTGGGCGAACAAACCGCCTTTGACGGCAAAAA
AGTCCTTGCCGCCTACGAATCCCCCGAAAGTCAGGCGCGCGCCGGCAAAA
TGCAGGAGCTGACCGAAACCTTCCAAATCGACGGTACGCCCACGGTTATC
GTCGGCGGCAAATATAAAGTCGAATTTGCCGACTGGGAGTCCGGTATGAA
CACCATCGACCTTTTGGCGGACAAAGTACGTGAAGAACAAAAAGCCGCGC
AG


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