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Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR0313 IGR0315 IGR0317 IGR0320 IGR0318 IGR0312 IGR0319 IGR0321 IGR0316 IGR0314 NG0378 NG0381 ppiB, - NG0376 pth, - NG0379 ftsJ,rrmJ, - NG0383 metC,metB2, - NG0386 NG0377 ftsH,hflB, - NG0382 NG0384 NG0387 hemB, - NG0385 NG0378 NG0381 ppiB, - NG0376 pth, - NG0379 ftsJ,rrmJ, - NG0383 metC,metB2, - NG0386 NG0377 ftsH,hflB, - NG0382 NG0384 NG0387 hemB, - NG0385 NG0378 ppiB, - NG0376 pth, - NG0379 ftsJ,rrmJ, - NG0383 metC,metB2, - NG0386 NG0377 ftsH,hflB, - NG0382 NG0380 NG0381 NG0380 NG0384 NG0387 hemB, - NG0385
* Calculated from Protein Sequence

Gene ID: NG0382

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
ftsH  hflB  

Definition:
cell division protein (HflB/FtsH protease) (ATP-dependent zinc metallopeptidase)

Gene Start:
376680

Gene Stop:
374716

Gene Length:
1965

Molecular Weight*:
72077

pI*:
5.10

Net Charge*:
-13.37

EC:
3.4.24.-  

Functional Class:
Cellular processes; Cell division  
Translation; Degradation of proteins, peptides, and glycopeptides  

Pathway: pathway table

Secondary Evidence:
Tomoyasu,T., Yuki,T., Morimura,S., Mori,H., Yamanaka,K., Niki,H.,
Hiraga,S. and Ogura,T. 1993.
The Escherichia coli FtsH protein is a prokaryotic member of a protein family of putative ATPases involved in membrane functions, cell cycle control, and gene expression.
J. Bacteriol. 175 (5): 1344-1351.
Medline: 93186701.

Ogura,T., Tomoyasu,T., Yuki,T., Morimura,S., Begg,K.J., Donachie,W.D., Mori,H., Niki,H. and Hiraga,S. 1991.
Structure and function of the ftsH gene in Escherichia coli.
Res. Microbiol. 142 (2-3): 279-282.
Medline: 92021790.

Tomoyasu,T., Gamer,J., Bukau,B., Kanemori,M., Mori,H., Rutman,A.J., Oppenheim,A.B., Yura,T., Yamanaka,K., Niki,H., Hiraga,S. and Ogura,T. 1995.
Escherichia coli FtsH is a membrane-bound, ATP-dependent protease which degrades the heat-shock transcription factor sigma 32.
EMBO J. 14 (11): 2551-2560.
Medline: 95300788.

Krzywda S, Brzozowski A, Verma C, Karata K, Ogura T, Wilkinson A. The Crystal Structure of the AAA Domain of
the ATP-Dependent Protease FtsH of Escherichia coli at 1.5 A Resolution.
Structure (Camb). 2002 Aug;10(8):1073.
PMID: 12176385

Chiba S, Akiyama Y, Ito K.
Membrane protein degradation by FtsH can be initiated from either
end.
J Bacteriol. 2002 Sep;184(17):4775-82.
PMID: 12169602

Zellmeier S, Zuber U, Schumann W, Wiegert T.
The absence of FtsH metalloprotease activity causes overexpression of the sigmaW-controlled pbpE gene, resulting in filamentous
growth of Bacillus subtilis.
J Bacteriol. 2003 Feb;185(3):973-82.
PMID: 12533473



Comment:
Oklahoma ID: NGO.382c

For other 'fts' genes, see NG2060 (ftsY)), NG0383 (ftsJ), NG0590 (ftsK), NG0851 (ftsK), NG1528 (ftsZ), NG1529 (ftsA), NG1530 (ftsQ), NG1534 (ftsW), NG1921 (ftsX), NG1922 (ftsE). See also NG1543 (ftsL-related).

Blast Summary:  PSI-Blast Search
NG0382 is orthologously related to AE002433, Neisseria meningitidis, strain MC58, a cell division protein (FtsH): residues 1-655 are 98% similar to residues 1-655 of NG0382. NG0382 is orthologously related to AL162754, Neisseria meningitidis, strain Z2491, a putative ATP-dependent zinc metallopeptidase protein: residues 1-655 are 98% similar to residues 1-655 of NG0382.

Numerous significant hits in gapped BLAST; e.g. residues 6-650 are 58% similar to dbj|BAB37480.1| cell division protein HflB/FtsH protease of Escherichia coli O157:H7, residues 6-647 are 58% similar to gb|AAF93803.1| cell division protein FtsH of Vibrio cholerae, residues 6-610 are 61% similar to gb|AAG08137.1|AE004888_12 cell division protein FtsH of Pseudomonas aeruginosa.

COGS Summary:  COGS Search
BeTs to 13 clades of COG0465
COG name: ATP-dependent Zn proteases
Functional Class:  O
The phylogenetic pattern of COG0465 is ----YqvCeBrHUJgpoLinx
Number of proteins in this genome belonging to this COG is 2

Blocks Summary:  Blocks Search
***** IPB000642 (Peptidase family M41) with a combined E-value of 2.9e-197.
    IPB000642A    159-207
    IPB000642B    225-269
    IPB000642C    298-342
    IPB000642D    357-382
    IPB000642E    414-450
    IPB000642F    478-489
    IPB000642G    491-516
***** IPB003338 (Amino-terminal subdomain, VAT-Nn) with a combined E-value of 2e-62.
    IPB003338H    147-186
    IPB003338I    200-244
    IPB003338J    245-269
    IPB003338K    287-340
***** IPB003960 (AAA-protein subfamily) with a combined E-value of 1.3e-58.
    IPB003960A    235-268
    IPB003960B    285-331


ProDom Summary:  Protein Domain Search
Residues 194-373 are 29% similar to a (F54B3.3 PROTEIN) protein domain (PD094582) which is seen in Q20748_CAEEL.

Residues 192-392 are 25% similar to a (CELL DIVISION PROTEIN, PUTATIVE) protein domain (PD185276) which is seen in O83350_TREPA.

Residues 168-347 are 25% similar to a (HYPOTHETICAL 75.3 KD PROTEIN) protein domain (PD137110) which is seen in P96281_MYCTU.

Residues 388-573 are 54% similar to a (PROTEIN CELL DIVISION ZINC METALLOPROTEASE HOMOLOG) protein domain (PD002293) which is seen in FTSH_ECOLI.

Residues 276-312 are 83% similar to a (CELL DIVISION PROTEIN FTSH) protein domain (PD194210) which is seen in FTH2_HAEIN.

Residues 6-128 are 36% similar to a (FTSH CELL DIVISION ZINC) protein domain (PD035190) which is seen in FTSH_ECOLI.

Residues 352-382 are 83% similar to a (PROTEIN ATP-BINDING CELL DIVISION HOMOLOG SUBUNIT) protein domain (PD000272) which is seen in FTH1_HAEIN.

Residues 313-348 are 80% similar to a (PROTEIN CELL DIVISION HOMOLOG ATP-BINDING ZINC) protein domain (PD186075) which is seen in FTSH_ECOLI.

Residues 237-344 are 37% similar to a (PROTEIN CELL DIVISION ATP-BINDING) protein domain (PD094491) which is seen in FTSH_CHLVU.

Residues 148-374 are 64% similar to a (PROTEIN ATP-BINDING PROTEASE SUBUNIT REGULATORY HOMOLOG) protein domain (PD000092) which is seen in FTSH_HELFE.



Paralogs:  Local Blast Search


NG0382 is paralogously related to NG0645 (ATP-dependent Clp proteinase, ATP-binding chain ClpX) (2e-04) and NG0775 (ATP-dependent protease La (Lon protease)) (3e-04).


Pfam Summary:  Pfam Search
Residues 33 to 169 (E-value = 5.9e-41) place NG0382 in the FtsH_ext family which is described as FtsH Extracellular (PF06480)
Residues 195 to 382 (E-value = 2.7e-97) place NG0382 in the AAA family which is described as ATPase family associated with various cellular activities (AAA) (PF00004)
Residues 388 to 598 (E-value = 1.7e-108) place NG0382 in the Peptidase_M41 family which is described as Peptidase family M41 (PF01434)

Structural Feature(s):
Feature Type  Start  Stop
gram negative signal  
1  
24
cleavable N-terminal sequence  
1  
20
transmembrane  
105  
121
coil-coil  
544  
580
non-globular  
600  
655

PDB Hit:
pdb|1LV7|1LV7-A CRYSTAL STRUCTURE OF THE AAA DOMAIN OF FTSH 380.0 0e+00
pdb|1IY2|1IY2-A CRYSTAL STRUCTURE OF THE FTSH ATPASE DOMAIN FROM327.0 3e-90
pdb|1IXZ|1IXZ-A CRYSTAL STRUCTURE OF THE FTSH ATPASE DOMAIN FROM325.0 2e-89
pdb|1E32|1E32-A STRU

Gene Protein Sequence:
VGNTFKSILVWVALGIGLMAAFNALDGKKEDNGQIEYSQFIRQVNNGEVS
GVNIEGSVVSGYLIKGERTDKSTFFTNAPLDDNLIQTLLNKNVRVKVTPE
EKPSALTALFYSLLPVLLLIGAWFYFMRMQAGGGGKGGAFSFGKSRARLL
DKDANKVTFADVAGCDEAKEEVQEIVDYLKAPNRYQSLGGRVPRGILLAG
SPGTGKTLLAKAIAGEAGVPFFSISGSDFVEMFVGVGASRVRDMFEQAKK
NAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQLLVEMDGFESNQTVI
VIAATNRPDVLDPALQRPGRFDRQVVVPLPDIRGREQILNVHSKKVPLDE
SVDLLSLARGTPGFSGADLANLVNEAALFAGRRNKVKVDQSDFEDAKDKI
YMGPERRSMVMHEDEKRATAYHESGHAIVAESLPFTDPVHKVTIMPRGRA
LGLTWQLPERDRISMYKDQMLSQLSILFGGRIAEDIFVGRISTGASNDFE
RATQMAREMVTRYGMSDKMGVMVYAENEGEVFLGRSVTRSQNISEKTQQD
IDAEIRRILDEQYQVAYKILDENRDKMETMCKALMEWETIDRDQVLEIMA
GKQPSPPKDYSHNLRENADAAEDNAPHAPTREKTEAPAPADTASTESGQQ
PENKA

Gene Nucleotide Sequence:  Sequence Viewer
GTGGGGAACACCTTTAAATCAATCCTTGTCTGGGTCGCCTTGGGTATCGG
CCTGATGGCTGCGTTCAACGCTTTGGACGGCAAAAAAGAAGACAACGGGC
AAATCGAATATTCTCAGTTCATCCGACAGGTCAACAACGGCGAAGTATCC
GGCGTCAACATCGAAGGATCCGTCGTCAGCGGTTACCTGATTAAAGGCGA
GCGCACCGACAAAAGCACCTTCTTCACCAACGCGCCCTTGGATGACAACC
TGATTCAAACCCTTTTGAACAAAAACGTCCGCGTAAAAGTAACGCCGGAA
GAAAAACCGAGCGCGCTGACTGCCCTGTTTTACAGCCTGCTGCCCGTCCT
GCTGCTGATTGGCGCATGGTTCTACTTTATGCGTATGCAGGCGGGCGGCG
GCGGAAAAGGCGGCGCATTCTCCTTCGGCAAAAGCCGCGCCCGCCTGCTG
GACAAAGATGCCAACAAAGTTACCTTTGCCGATGTCGCCGGCTGCGACGA
AGCCAAAGAAGAAGTGCAGGAAATCGTCGATTACCTCAAAGCACCGAACC
GCTATCAAAGCCTCGGCGGCCGTGTTCCGCGCGGCATCCTGCTGGCGGGC
AGCCCGGGAACCGGTAAAACACTCTTGGCGAAAGCCATTGCAGGCGAGGC
CGGCGTGCCGTTCTTCAGCATTTCCGGTTCCGATTTTGTCGAAATGTTCG
TCGGTGTCGGTGCAAGCCGCGTCCGCGATATGTTCGAGCAGGCAAAGAAA
AACGCCCCATGCATTATCTTTATCGACGAGATTGACGCGGTAGGCCGCCA
ACGCGGCGCAGGTTTGGGCGGCGGCAATGATGAGCGCGAGCAAACATTAA
ACCAATTATTGGTTGAAATGGACGGTTTTGAGAGCAATCAGACTGTAATT
GTGATTGCGGCAACCAACCGCCCCGACGTACTCGATCCTGCGCTGCAACG
CCCCGGCCGCTTCGACCGCCAAGTCGTCGTCCCCCTGCCGGACATCCGGG
GGCGCGAACAGATTTTGAACGTCCATTCTAAAAAAGTGCCTTTGGACGAA
TCTGTGGATTTATTGTCCCTCGCGCGCGGCACGCCCGGTTTTTCCGGCGC
GGATTTGGCGAACCTGGTCAACGAAGCCGCCCTGTTTGCCGGCCGCCGCA
ACAAAGTCAAAGTCGATCAAAGCGATTTTGAAGACGCCAAAGACAAAATC
TATATGGGTCCGGAACGCCGCAGTATGGTGATGCACGAAGACGAAAAACG
TGCGACGGCGTATCATGAGTCCGGACACGCGATTGTTGCCGAAAGCCTGC
CCTTTACCGACCCCGTCCACAAAGTAACCATTATGCCGCGCGGACGTGCG
CTGGGTCTGACTTGGCAGCTTCCGGAGCGCGACCGCATCAGTATGTATAA
AGATCAGATGTTGAGCCAGCTCTCCATCCTGTTCGGCGGACGGATTGCCG
AAGACATCTTCGTCGGACGCATCTCCACCGGTGCATCAAACGACTTTGAA
CGCGCAACCCAAATGGCACGCGAAATGGTAACGCGCTACGGCATGAGCGA
CAAAATGGGCGTGATGGTTTATGCGGAAAACGAAGGCGAAGTCTTCTTGG
GGCGCAGCGTAACCCGTTCGCAAAACATTTCCGAGAAAACCCAGCAGGAC
ATCGACGCGGAAATCCGCCGGATTTTGGACGAGCAGTATCAGGTTGCCTA
CAAAATCCTCGATGAAAACCGCGACAAGATGGAAACGATGTGCAAAGCCC
TGATGGAATGGGAAACCATAGACCGCGATCAGGTACTGGAAATTATGGCG
GGCAAACAACCCAGCCCGCCCAAGGATTACAGCCACAACCTGCGCGAGAA
TGCGGACGCGGCGGAAGATAACGCGCCGCACGCTCCGACTCGGGAAAAAA
CCGAAGCACCTGCCCCGGCAGACACCGCCTCGACAGAGTCCGGGCAGCAG
CCTGAAAACAAGGCT


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