General Information |
MoonProt ID | 127 |
First appeared in release | 1.0 |
Name(s) | ATP-dependent zinc metalloprotease FtsH
ftsH
hflB
|
UniProt ID | P0AAI4 (FTSH_SHIFL) Reviewed |
GO terms | GO:0006200 ATP catabolic process
GO:0006508 proteolysis
GO:0030163 protein catabolic process
GO:0000166 nucleotide binding
GO:0004222 metalloendopeptidase activity
GO:0005524 ATP binding
GO:0008233 peptidase activity
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
GO:0016787 hydrolase activity
GO:0016887 ATPase activity
GO:0017111 nucleoside-triphosphatase activity
GO:0046872 metal ion binding
GO:0005886 plasma membrane
GO:0016020 membrane
GO:0016021 integral component of membrane |
Organisms for which functions have been demonstrated | Shigella flexneri |
Sequence length | 644 |
FASTA sequence | >sp|P0AAI4|FTSH_SHIFL ATP-dependent zinc metalloprotease FtsH OS=Shigella flexneri GN=ftsH PE=3 SV=1
MAKNLILWLVIAVVLMSVFQSFGPSESNGRKVDYSTFLQEVNNDQVREARINGREINVTKKDSNRYTTYIPVQDPKLLDNLLTKNVKVVGEPPEEPSLLASIFISWFPMLLLIGVWIFFMRQMQGGGGKGAMSFGKSKARMLTEDQIKTTFADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAERRSMVMTEAQKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLESQISTLYGGRLAEEIIYGPEHVSTGASNDIKVATNLARNMVTQWGFSEKLGPLLYAEEEGEVFLGRSVAKAKHMSDETARIIDQEVKALIERNYNRARQLLTDNMDILHAMKDALMKYETIDAPQIDDLMARRDVRPPAGWEEPGASNNSGDNGSPKAPRPVDEPRTPNPGNTMSEQLGDK
|
Structure Information |
PDB ID | closest is Thermotoga with 57% amino acid sequence identity |
Quaternary structure | |
SCOP | NA |
CATH | NA |
TM Helix Prediction | no TM helices |
DisProt Annotation | Not in DisProt |
Predicted Disorder Regions | 1-3, 25-27, 125-136, 261-271, 529-537, 597-644 |
Connections to Disease |
OMIM ID | |
Function 1 |
Function description | chaperone |
References for function | Suzuki CK, Rep M, van Dijl JM, Suda K, Grivell LA, Schatz G. ATP-dependent proteases that also chaperone protein biogenesis. Trends Biochem Sci. 1997 Apr;22(4):118-23.
Herman, C. et al. Cell growth and lambda phage development controlled by the same essential Escherichia coli gene, ftsH/hflB. Proc. Natl. Acad. Sci. U.S.A. 90. 10861-10865
Tomoyasu, T. et al. 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. 1993. J. Bacteriol. 175, 1344-1351. |
E.C. number | N/A |
Location of functional site(s) | |
Cellular location of function | cytoplasmic membrane protein |
Comments | |
Function 2 |
Function description | Metalloprotease, enzyme
ATP-dependent zinc metallopeptidase, hydrolyzes cytoplasmic and transmembrane proteins |
References for function | Suzuki CK, Rep M, van Dijl JM, Suda K, Grivell LA, Schatz G. ATP-dependent proteases that also chaperone protein biogenesis. Trends Biochem Sci. 1997 Apr;22(4):118-23.
Tomoyasu, T. et al. Escherichia coli FtsH is a membrane-bound protein, ATP-dependent protease which degrades the heat-shock transcription factor sigma32. EMBO J. 1995. 2551-2880. |
E.C. number | 3.4.24.- |
Location of functional site(s) | |
Cellular location of function | cytoplasmic membrane, transmembrane protein |
Comments | |