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Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR1052 IGR1050 IGR1057 IGR1049 IGR1055 IGR1053 IGR1056 IGR1054 IGR1051 NG1296 NG1298 NG1293 lrp, - NG1294 dsbB, - NG1292 NG1288 NG1297 NG1290 NG1289 NG1291 dadX, - NG1295 NG1296 NG1298 NG1293 lrp, - NG1294 dsbB, - NG1292 NG1288 NG1297 NG1290 NG1289 NG1291 dadX, - NG1295 NG1296 NG1293 lrp, - NG1294 dsbB, - NG1292 NG1288 NG1297 NG1290 NG1298 NG1289 NG1291 dadX, - NG1295
* Calculated from Protein Sequence

Gene ID: NG1292

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
dsbB  

Definition:
disulfide bond formation protein B

Gene Start:
1248297

Gene Stop:
1247608

Gene Length:
690

Molecular Weight*:
25368

pI*:
8.90

Net Charge*:
12.75

EC:
1.8.4.-  

Functional Class:
Cell envelope; Surface structures  
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].

Kadokura H, Katzen F, Beckwith J.
Protein Disulfide Bond Formation in Prokaryotes.
Annu Rev Biochem. 2003 Jan.
PMID: 12524212

Regeimbal J, Bardwell JC.
DsbB catalyzes disulfide bond formation de novo.
J Biol Chem. 2002 Sep;277(36):32706-13.
PMID: 12072444

Inaba K, Ito K.
Paradoxical redox properties of DsbB and DsbA in the protein disulfide-introducing reaction cascade.
EMBO J. 2002 Jun;21(11):2646-54.
PMID: 12032077

Comment:
Oklahoma ID: NGO.1292c

From GenBANK (gi:12230038): This is an integral membrane protein that acts through oxidizing the dsbA protein, NG1548 or NG1717. It is required for disulfide bond formation.

See also: DsbA, NG1548 & NG1717; DsbC, NG1438; and DsbD, NG0978.

Blast Summary:  PSI-Blast Search
Limited hits in gapped BLAST to disulfide bond formation proteins. Residues 6-149 are 27% similar to the enzyme in P.aeruginosa (gb|AAG08641).

Residues 1-162 are greater than 90% similar to NMA1903 in N.meningitidis (AL162757).

COGS Summary:  COGS Search
BeTs to 3 clades of COG1495
COG name: Disulfide bond formation protein DsbB
Functional Class:  O
The phylogenetic pattern of COG1495 is --------eB-huj----inx
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
***** IPB003752 (Disulfide bond formation protein DsbB) with a combined E-value of 2.3e-09.
    IPB003752    91-123


ProDom Summary:  Protein Domain Search
Residues 6-149 are 27% similar to a (PROTEIN DISULFIDE BOND FORMATION) protein domain (PD034694) which is seen in YA21_PSEAE.



Paralogs:  Local Blast Search


NG1292 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.


Pfam Summary:  Pfam Search
Residues 67 to 228 (E-value = 4e-05) place NG1292 in the DsbB family which is described as Disulfide bond formation protein DsbB (PF02600)

Structural Feature(s):
Feature Type  Start  Stop
gram negative signal  
1  
21
cleavable N-terminal sequence  
1  
21
transmembrane  
43  
59
transmembrane  
69  
85
transmembrane  
136  
152

PDB Hit:
No hits to the PDB database.

Gene Protein Sequence:
CRNSNSNPPDVFFRALCGQIAVLSFVRFCAYRENRNRPHLCRCRFVPCHL
GIYPAKSAYRYFDWCVEKMTPLFRKAVWLLFAVSVCAFAGSLAAQYVLGM
EPCVLCISQRLCVLATALCAAVVLACKPKGRVGGLSGAVFISIPAVTGIS
VAAYQLWLQSLPPGAAPSCGAPWTFRLKGWPLFDWFEPVVRGFGNCAEPD
YLLGVALPVWSAAYFLAVVLTVWWAWARAK

Gene Nucleotide Sequence:  Sequence Viewer
TGCCGAAATTCAAATTCAAATCCTCCGGATGTATTTTTTCGGGCATTGTG
CGGACAAATCGCCGTTTTGTCCTTTGTCAGGTTTTGTGCATATCGGGAAA
ACCGAAATCGTCCGCACCTGTGCCGGTGTCGATTCGTCCCTTGCCATCTC
GGGATATATCCAGCAAAATCGGCATATCGGTATTTTGATTGGTGTGTTGA
GAAAATGACCCCGTTATTTAGAAAAGCCGTTTGGCTGCTGTTTGCCGTTT
CGGTCTGTGCATTTGCCGGTTCTTTGGCGGCACAGTATGTTTTGGGTATG
GAGCCTTGCGTTTTGTGCATCAGTCAGCGGTTATGTGTTTTGGCAACCGC
ATTGTGTGCGGCAGTTGTGCTGGCGTGTAAGCCCAAGGGCAGGGTGGGCG
GACTGTCAGGCGCAGTGTTTATCAGTATTCCCGCCGTTACGGGTATTTCT
GTTGCGGCATATCAGTTGTGGTTGCAGTCGCTGCCGCCGGGTGCGGCTCC
TTCGTGCGGCGCGCCGTGGACGTTTCGATTGAAGGGCTGGCCTTTGTTTG
ATTGGTTCGAGCCTGTTGTGCGCGGGTTCGGAAATTGTGCCGAACCGGAT
TATCTGTTAGGGGTTGCTTTGCCTGTTTGGAGCGCGGCGTATTTTTTGGC
GGTTGTCCTGACGGTTTGGTGGGCGTGGGCAAGGGCTAAA


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