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Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR1173 IGR1176 IGR1175 IGR1174 IGR1171 IGR1177 IGR1178 IGR1172 NG1440 aqpZ, - NG1439 priA, - NG1437 pilV, - NG1441 cysA, - NG1434 cadD, - NG1435 dsbC, - NG1438 adhA, - NG1442 NG1436 NG1440 aqpZ, - NG1439 priA, - NG1437 pilV, - NG1441 cysA, - NG1434 cadD, - NG1435 dsbC, - NG1438 adhA, - NG1442 NG1436 Type: tandem, Name:  - 63 NG1440 aqpZ, - NG1439 priA, - NG1437 pilV, - NG1441 cadD, - NG1435 dsbC, - NG1438 adhA, - NG1442 NG1436 cysA, - NG1434
* Calculated from Protein Sequence

Gene ID: NG1438

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
dsbC  

Definition:
thiol:disulfide interchange protein DsbC

Gene Start:
1402287

Gene Stop:
1403069

Gene Length:
783

Molecular Weight*:
28692

pI*:
8.30

Net Charge*:
3.25

EC:
5.3.4.1  

Functional Class:
Translation; Protein modification and translation factors  

Pathway: pathway table

Secondary Evidence:
Missiakas,D., Georgopoulos,C. and Raina,S.
The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation. EMBO J. 13 (8), 2013-2020 (1994)
M:94222049

Zapun,A., Missiakas,D., Raina,S. and Creighton,T.E.
Structural and functional characterization of DsbC, a protein
involved in disulfide bond formation in Escherichia coli. Biochemistry 34 (15), 5075-5089 (1995)
M:95226395

Shevchik,V.E., Condemine,G. and Robert-Baudouy,J.
Characterization of DsbC, a periplasmic protein of Erwinia
chrysanthemi and Escherichia coli with disulfide isomerase activity. EMBO J. 13 (8), 2007-2012 (1994)
M:94222048

Joly,J.C. and Swartz,J.R.
In vitro and in vivo redox states of the Escherichia coli
periplasmic oxidoreductases DsbA and DsbC. Biochemistry 36 (33), 10067-10072 (1997)
M:97400462

McCarthy,A.A., Haebel,P.W., Torronen,A., Rybin,V., Baker,E.N. and
Metcalf,P.
Crystal structure of the protein disulfide bond isomerase, DsbC,
from Escherichia coli. Nat. Struct. Biol. 7 (3), 196-199 (2000)
M:20165176


Comment:
From GenBANK (gi:729371): DsbC is required for disulfide bond formation in some periplasmic proteins. It acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbC is reoxidized by a yet uncharacterized protein. It also acts as a disulfide isomerase. This periplasmic homodimer belongs to the thioredoxin family; DsbC subfamily.

See also: DsbA, NG1548 & NG1717; DsbB, NG1292; and DsbD, NG0978.

Oklahoma ID: NGO.1438

Blast Summary:  PSI-Blast Search
Several matches in gapped BLAST to protein disulfide-isomerases. Residues 42-255 are 28% similar to the thiol:disulfide interchange protein DsbC in P.aeruginosa (gb|AAC16483).

Residues 1-260 are virtually identical to NMB0550 in N.meningitidis (gb|AAF40979).

COGS Summary:  COGS Search
BeTs to 3 clades of COG1651
COG name: Protein-disulfide isomerases DsbC/DsbG
Functional Class:  O
The phylogenetic pattern of COG1651 is a----Q-cEBRhuj----inX
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
Residues 123-255 are 32% similar to a (HYPOTHETICAL 19.3 KD PROTEIN) protein domain (PD098904) which is seen in O67626_AQUAE.

Residues 51-255 are 29% similar to a (PROTEIN PRECURSOR THIOL:DISULFIDE INTERCHANGE SIGNAL) protein domain (PD013570) which is seen in O68904_PSEAE.

Residues 53-239 are 29% similar to a (THIOL:DISULFIDE INTERCHANGE PROTEIN DSBG PRECURSOR) protein domain (PD038456) which is seen in O67863_AQUAE.



Paralogs:  Local Blast Search


NG1438 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
may be a lipoprotein  
  
gram negative signal  
1  
30

PDB Hit:
pdb|1EEJ|1EEJ-A CRYSTAL STRUCTURE OF THE PROTEIN DISULFIDE BOND 86.6 4e-18
pdb|1G0T|1G0T-A DSBC MUTANT C101S 82.7 6e-17
pdb|1EEJ|1EEJ-A CRYSTAL STRUCTURE OF THE PROTEIN DISULFIDE BOND 71.1 2e-13

Gene Protein Sequence:
MKTKLIKILTPFTVLPLLACGQTPVSNANAESAVKAESAGKSVAASLKAR
LEKTYSAQDLKVLSVSETPVKGIYEVVVSGRQIIYTDAEGGYMFVGELIN
IDTRKNLTEERAADLNKIDFASLPLDKAIKEVRGNGKLKVAVFSDPDCPF
CKRLEHEFEKMTDVTVYSFMMPIAGLHPDAARKAQILWCQPDRAKAWTDW
MRKGKFPVGGSICDNPVAETTSLGEQFGFNGTPTLVFPNGRTQSGYSPMP
QLEEIIRKNQQ

Gene Nucleotide Sequence:  Sequence Viewer
ATGAAAACCAAGTTAATCAAAATCTTGACCCCCTTTACCGTCCTGCCGCT
GCTGGCTTGCGGGCAAACGCCCGTTTCCAATGCCAACGCCGAATCCGCCG
TCAAAGCCGAATCCGCCGGCAAATCCGTTGCCGCTTCTTTGAAAGCGCGT
TTGGAAAAAACCTATTCCGCCCAAGATTTGAAAGTGTTGAGCGTCAGCGA
AACACCGGTCAAAGGCATTTACGAAGTCGTCGTCAGCGGCAGGCAGATTA
TCTACACCGATGCCGAAGGCGGCTATATGTTCGTCGGCGAACTCATCAAC
ATCGACACGCGCAAAAACCTGACCGAAGAACGCGCCGCCGATTTGAACAA
AATCGACTTCGCCTCCCTGCCTTTGGACAAAGCCATCAAAGAAGTACGCG
GCAACGGCAAGCTGAAAGTCGCCGTCTTCTCCGACCCCGATTGTCCGTTC
TGCAAACGCTTGGAACATGAGTTTGAAAAAATGACCGACGTGACGGTTTA
CAGCTTTATGATGCCCATTGCCGGCCTGCACCCAGATGCCGCGCGCAAGG
CGCAAATCTTATGGTGTCAGCCCGACCGTGCCAAAGCGTGGACGGATTGG
ATGCGTAAAGGCAAATTCCCGGTCGGCGGCAGCATCTGCGACAATCCCGT
CGCGGAAACCACTTCCTTGGGCGAACAGTTCGGCTTCAACGGCACGCCGA
CCCTCGTCTTCCCCAACGGGCGCACCCAAAGCGGTTACAGCCCGATGCCC
CAACTGGAGGAAATCATCCGCAAAAACCAGCAG


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