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Q92JJ9 (FTSH_RICCN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
ATP-dependent zinc metalloprotease FtsH

EC=3.4.24.-
Gene names
Name:ftsH
Ordered Locus Names:RC0068
OrganismRickettsia conorii (strain ATCC VR-613 / Malish 7) [Complete proteome] [HAMAP]
Taxonomic identifier272944 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group

Protein attributes

Sequence length637 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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. HAMAP MF_01458

Subunit structure

Homohexamer Potential.

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 – 637637ATP-dependent zinc metalloprotease FtsH HAMAP MF_01458
PRO_0000084645

Regions

Topological domain1 – 66Cytoplasmic Potential
Transmembrane7 – 2721Helical; Potential
Topological domain28 – 10376Periplasmic Potential
Transmembrane104 – 12421Helical; Potential
Topological domain125 – 637513Cytoplasmic Potential
Nucleotide binding195 – 2028ATP Potential

Sites

Active site4181 By similarity
Metal binding4171Zinc; catalytic By similarity
Metal binding4211Zinc; catalytic By similarity
Metal binding4951Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
Q92JJ9 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: BAFB799AB272EAAE

FASTA63769,915
        10         20         30         40         50         60 
MNNQGRSILA WATLFIFVIL LFNVFQSDSL LGGRNNITFS DFLTRVDEKT VNSVKIQGRV 

        70         80         90        100        110        120 
IEGTSNDGST FNTYAPDYPD LVNRLTSNDV NIEVVPLETR MNTFLGFLIS WFPMLLLIGV 

       130        140        150        160        170        180 
WVFFMRQMHG GGKAMGFGKS KARLLSDKGP KITFKDVAGI DEAKEELTEI VDFLRDPSKF 

       190        200        210        220        230        240 
QKLGGKIPKG CLLIGPPGTG KTLLAKAIAG EANVPFFSIS GSDFVEMFVG VGASRVRDMF 

       250        260        270        280        290        300 
EQGKRNAPCI IFIDEIDAVG RHRGIGMGGG NDEREQTLNQ MLVEMDGFEA NEGVVIIAAT 

       310        320        330        340        350        360 
NRPDVLDRAL LRPGRFDRQI AVANPDINGR EQILKVHLKK IKYNSTVLAR IIARGTPGFS 

       370        380        390        400        410        420 
GAELANLVNE AALIAARLGK KEVDMHDMEE AKDKVLMGVA RRSIAMSEKE KRLTAYHEGG 

       430        440        450        460        470        480 
HALVGLYCPA ASPIHKATII PRGNALGMVQ RLPETDEYSQ NREQMESSIA VYMAGRVAEE 

       490        500        510        520        530        540 
IIFGRNKVTS GASSDIKGAT NIARAMVTKA GLSDLIGPIF HGSSGDDMYG RQPNNETSEA 

       550        560        570        580        590        600 
TAELIDAEVK RIITQGYEFA KDILTKHIDQ LHTLANALIE YETLSGQQIK NLLSGRALDS 

       610        620        630 
EEENKFPFND SSTIKIDKEK SPEKTKTTKA KKENYAS 

« Hide

References

[1]"Mechanisms of evolution in Rickettsia conorii and R. prowazekii."
Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.
Science 293:2093-2098(2001) [PubMed: 11557893] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-613 / Malish 7.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006914 Genomic DNA. Translation: AAL02606.1.
PIRD97708.
RefSeqNP_359705.1. NC_003103.1.

3D structure databases

ProteinModelPortalQ92JJ9.
SMRQ92JJ9. Positions 144-399.
ModBaseSearch...

Protein family/group databases

MEROPSM41.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID928595.
GenomeReviewsGene locus RC0068 in contig AE006914_GR.
KEGGrco:RC0068.
NMPDRfig|272944.1.peg.68.
PATRIC17887230. VBIRicCon45613_0079.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAYISDETK.
ProtClustDBCLSK870717.

Enzyme and pathway databases

BioCycRCON272944:RC0068-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.
IPR011546. Pept_M41_FtsH_extracell.
IPR000642. Peptidase_M41.
[Graphical view]
KOK03798.
PfamPF00004. AAA. 1 hit.
PF06480. FtsH_ext. 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_RICCN
AccessionPrimary (citable) accession number: Q92JJ9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 26, 2002
Last sequence update: December 1, 2001
Last modified: January 25, 2012
This is version 74 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

Rickettsia conorii

(strain Malish 7): entries and gene names

SIMILARITY comments

Index of protein domains and families