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Q9WZ49 (FTSH_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP-dependent zinc metalloprotease FtsH
EC=3.4.24.-
Gene names
Name:ftsH
Ordered Locus Names:TM_0580
OrganismThermotoga maritima
Taxonomic identifier2336 [NCBI]
Taxonomic lineageBacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

Protein attributes

Sequence length610 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins By similarity. HAMAP MF_01458

Cofactor

Binds 1 zinc ion per subunit By similarity. Ref.2

Subunit structure

The isolated ADP-bound cytosolic domain forms a 6-fold symmetric protease disk and a 2-fold symmetric AAA ATPase ring. In the absence of nucleotide the AAA ATPase ring also forms symmetric hexamers. Ref.2 Ref.3

Subcellular location

Cell inner membrane; Multi-pass membrane protein; Cytoplasmic side By similarity HAMAP MF_01458.

Sequence similarities

In the central section; belongs to the AAA ATPase family.

In the C-terminal section; belongs to the peptidase M41 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 610610ATP-dependent zinc metalloprotease FtsH HAMAP MF_01458
PRO_0000400412

Regions

Topological domain1 – 55Cytoplasmic Potential
Transmembrane6 – 2621Helical; Potential
Topological domain27 – 10781Periplasmic Potential
Transmembrane108 – 12821Helical; Potential
Topological domain129 – 610482Cytoplasmic Potential
Nucleotide binding204 – 2085ATP HAMAP MF_01458

Sites

Active site4241 By similarity
Metal binding4231Zinc; catalytic
Metal binding4271Zinc; catalytic
Metal binding5001Zinc; catalytic
Binding site1641ATP; via amide nitrogen and carbonyl oxygen
Binding site2091ATP; via amide nitrogen
Binding site3431ATP
Binding site3711ATP

Experimental info

Mutagenesis4041G → L: Complete loss of protease activity and of oligomerization. Ref.3
Mutagenesis5001D → A: Complete loss of protease activity. Ref.2

Secondary structure

1 ...................................................... 610
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9WZ49 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 83F76468C8495DDF

FASTA61068,099
        10         20         30         40         50         60 
MNRSNIWNLL FTILIIVTLF WLARFFYVEN SPVSKLSYTS FVQMVEDERS VVSEVVIRDD 

        70         80         90        100        110        120 
GVLRVYTKDG RVYEVDAPWA VNDSQLIEKL VSKGIKVSGE RSGSSSFWIN VLGTLIPTIL 

       130        140        150        160        170        180 
FIVVWLFIMR SLSGRNNQAF TFTKSRATMY KPSGNKRVTF KDVGGAEEAI EELKEVVEFL 

       190        200        210        220        230        240 
KDPSKFNRIG ARMPKGILLV GPPGTGKTLL ARAVAGEANV PFFHISGSDF VELFVGVGAA 

       250        260        270        280        290        300 
RVRDLFAQAK AHAPCIVFID EIDAVGRHRG AGLGGGHDER EQTLNQLLVE MDGFDSKEGI 

       310        320        330        340        350        360 
IVMAATNRPD ILDPALLRPG RFDKKIVVDP PDMLGRKKIL EIHTRNKPLA EDVNLEIIAK 

       370        380        390        400        410        420 
RTPGFVGADL ENLVNEAALL AAREGRDKIT MKDFEEAIDR VIAGPARKSK LISPKEKRII 

       430        440        450        460        470        480 
AYHEAGHAVV STVVPNGEPV HRISIIPRGY KALGYTLHLP EEDKYLVSRN ELLDKLTALL 

       490        500        510        520        530        540 
GGRAAEEVVF GDVTSGAAND IERATEIARN MVCQLGMSEE LGPLAWGKEE QEVFLGKEIT 

       550        560        570        580        590        600 
RLRNYSEEVA SKIDEEVKKI VTNCYERAKE IIRKYRKQLD NIVEILLEKE TIEGDELRRI 

       610 
LSEEFEKVVE

« Hide

References

« Hide 'large scale' references
[1]"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima."
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. expand/collapse author list , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.
Nature 399:323-329(1999) [PubMed: 10360571] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]"The molecular architecture of the metalloprotease FtsH."
Bieniossek C., Schalch T., Bumann M., Meister M., Meier R., Baumann U.
Proc. Natl. Acad. Sci. U.S.A. 103:3066-3071(2006) [PubMed: 16484367] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) OF 147-610 WITH BOUND ADP, COFACTOR, SUBUNIT, MUTAGENESIS OF ASP-500.
[3]"The crystal structure of apo-FtsH reveals domain movements necessary for substrate unfolding and translocation."
Bieniossek C., Niederhauser B., Baumann U.M.
Proc. Natl. Acad. Sci. U.S.A. 106:21579-21584(2009) [PubMed: 19955424] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 147-610 OF MUTANT ALA-207 WITHOUT NUCLEOTIDE, SUBUNIT, MUTAGENESIS OF GLY-404.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000512 Genomic DNA. Translation: AAD35665.1.
PIRE72358.
RefSeqNP_228390.1. NC_000853.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CE7X-ray2.44A/B/C/D/E/F147-610[»]
2CEAX-ray2.75A/B/C/D/E/F147-610[»]
3KDSX-ray2.60E/F/G147-610[»]
ProteinModelPortalQ9WZ49.
SMRQ9WZ49. Positions 150-606.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-49026N.

Protein family/group databases

MEROPSM41.021.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID897649.
GenomeReviewsGene locus TM_0580 in contig AE000512_GR.
KEGGtma:TM0580.
NMPDRfig|243274.1.peg.574.
PATRIC23936071. VBITheMar51294_0589.
TIGRTM_0580.

Phylogenomic databases

HOGENOMHBG724153.
OMASILRENI.
PhylomeDBQ9WZ49.
ProtClustDBCLSK875225.

Enzyme and pathway databases

BioCycTMAR243274:TM_0580-MONOMER.

Family and domain databases

HAMAPMF_01458. FtsH.
[Tree]
InterProIPR003593. ATPase_AAA+_core.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR005936. Pept_M41_FtsH.
IPR000642. Peptidase_M41.
[Graphical view]
KOK03798.
PfamPF00004. AAA. 1 hit.
PF01434. Peptidase_M41. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
[Graphical view]
TIGRFAMsTIGR01241. FtsH_fam. 1 hit.
PROSITEPS00674. AAA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFTSH_THEMA
AccessionPrimary (citable) accession number: Q9WZ49
Entry history
Integrated into UniProtKB/Swiss-Prot: November 2, 2010
Last sequence update: November 1, 1999
Last modified: January 25, 2012
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents