Protein Information

General Information
MoonProt ID127
First appeared in release1.0
Name(s)ATP-dependent zinc metalloprotease FtsH ftsH hflB
UniProt IDP0AAI4 (FTSH_SHIFL) Reviewed
GO termsGO: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 GO:0008233 peptidase activity GO:0008237 metallopeptidase activity
Organisms for which functions have been demonstratedShigella flexneri
Sequence length644
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
Quaternary structure
Function 1
Function descriptionchaperone
References for functionSuzuki 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. numberN/A
Location of functional site(s)Active site:415 Metal binding site:492,418,414 Nucleotide binding site:192-199
Cellular location of functioncytoplasmic membrane protein
Comments
Function 2
Function descriptionMetalloprotease, enzyme ATP-dependent zinc metallopeptidase, hydrolyzes cytoplasmic and transmembrane proteins
References for functionSuzuki 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. number3.4.24.-
Location of functional site(s)
Cellular location of functioncytoplasmic membrane, transmembrane protein
Comments