ATP-dependent zinc metalloprotease FtsH - Filifactor alocis (strain ATCC 35896 / D40 B5)

Preferred order of sections

Names and origin

Protein names

Recommended name:
ATP-dependent zinc metalloprotease FtsH HAMAP-Rule MF_01458
EC=3.4.24.- HAMAP-Rule MF_01458

Gene names

Name:	ftsH HAMAP-Rule MF_01458
Ordered Locus Names:	HMPREF0389_00529 EMBL EFE28612.1

Organism

Filifactor alocis (strain ATCC 35896 / D40 B5) (Fusobacterium alocis) [Complete proteome] [HAMAP] EMBL EFE28612.1

Taxonomic identifier

546269 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Peptostreptococcaceae › Filifactor ›

Protein attributes

Sequence length	666 AA.
Sequence status	Complete.
Protein existence	Inferred 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-Rule MF_01458
Cofactor	Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_01458
Subunit structure	Homohexamer By similarity. HAMAP-Rule MF_01458
Subcellular location	Cell membrane; Multi-pass membrane protein; Cytoplasmic side By similarity HAMAP-Rule MF_01458.
Sequence similarities	In the C-terminal section; belongs to the peptidase M41 family. HAMAP-Rule MF_01458 In the central section; belongs to the AAA ATPase family. HAMAP-Rule MF_01458

Ontologies

Keywords
Cellular component	Cell membrane HAMAP-Rule MF_01458 Membrane
Domain	Transmembrane Transmembrane helix HAMAP-Rule MF_01458
Ligand	ATP-binding HAMAP-Rule MF_01458 Metal-binding HAMAP-Rule MF_01458 Nucleotide-binding Zinc HAMAP-Rule MF_01458
Molecular function	Hydrolase Metalloprotease HAMAP-Rule MF_01458 EMBL EFE28612.1 Protease
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	ATP catabolic process Inferred from electronic annotation. Source: GOC protein catabolic process Inferred from electronic annotation. Source: HAMAP proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP ATPase activity Inferred from electronic annotation. Source: HAMAP metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Regions

Topological domain

1 – 3

3

Cytoplasmic By similarity HAMAP-Rule MF_01458

Transmembrane

4 – 24

21

Helical; By similarity HAMAP-Rule MF_01458

Topological domain

25 – 109

85

Extracellular By similarity HAMAP-Rule MF_01458

Transmembrane

110 – 130

21

Helical; By similarity HAMAP-Rule MF_01458

Topological domain

131 – 666

536

Cytoplasmic By similarity HAMAP-Rule MF_01458

Nucleotide binding

203 – 210

8

ATP By similarity HAMAP-Rule MF_01458

Sites

Active site

426

1

By similarity HAMAP-Rule MF_01458

Metal binding

425

1

Zinc; catalytic By similarity HAMAP-Rule MF_01458

Metal binding

429

1

Zinc; catalytic By similarity HAMAP-Rule MF_01458

Metal binding

501

1

Zinc; catalytic By similarity HAMAP-Rule MF_01458

Sequences

Sequence

Length

Mass (Da)

Tools

D6GSH1 [UniParc].

Last modified July 13, 2010. Version 1.
Checksum: 83345E2DA7F3141A
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FASTA

666

73,635

        10         20         30         40         50         60 
MKKFLQGTMF YIALIFVIMS LVFIQSNSTS KVEKIPFSEF YTSILEHKVS EVEIQDNGMI 

        70         80         90        100        110        120 
QGKMAGSDKV FTTYAGYLAK TDGLTKEILE QTQQGVLKSK VKEPTQTHWI LDLLPMVMLI 

       130        140        150        160        170        180 
LIIVAFWFIF VQQAQGGGSK VMGFGKSRAK LHKEDENIKI TFNDVAGLQE EKEELKEIVD 

       190        200        210        220        230        240 
FLRSPQKYWN LGARIPKGIL MVGPPGTGKT YLSKAVAGEA GVPFYSISGS DFVEMFVGVG 

       250        260        270        280        290        300 
ASRVRDLFEQ AKKTAPCIIF IDEIDAVGRK RGAGLGGGHD EREQTLNQLL VEMDGFRVNE 

       310        320        330        340        350        360 
SIIVMAATNR PDILDPALLR PGRFDRQVMV GSPDVKGREE ILKVHSRKKP LAEDVDLKVI 

       370        380        390        400        410        420 
ARGTAGFTAA DIENLMNEAA LLTARNNGTK IKMQTIEEAI VKTIVGLAKK SRIITEDEKK 

       430        440        450        460        470        480 
LTAYHEAGHA ILATVQKFCD PVHQVTIIPR GMAGGFTMSR PQEDRYYTTK QELKEKMVEL 

       490        500        510        520        530        540 
LGGRVAEELI LEDVSTGASN DLERVAKIAR AMVTTYAMTD KLGAMAYGDS SDEVFLGKDF 

       550        560        570        580        590        600 
TTKPNYSEEV ASQIDHEIKI IVDEAYATAR KLLQENIDRL HNVAQALMVY ETLDSEQFKK 

       610        620        630        640        650        660 
AFNGELDLNE DVEESISEGA DTFFDGEKSD DAKVSDENSD ISETPINGES GVVVDVTTSV 


DASEQK

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References

[1]

"The genome sequence of Filifactor alocis strain ATCC 35896."
The Broad Institute Genome Sequencing Platform
Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q., Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.

Birren B.
Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35896 / D40 B5.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP002390 Genomic DNA. Translation: EFE28612.1.
RefSeq	YP_005053851.1. NC_016630.1.
3D structure databases
ProteinModelPortal	D6GSH1.
ModBase	Search...
Protein family/group databases
MEROPS	M41.021.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EFE28612; EFE28612; HMPREF0389_00529.
GeneID	11570315.
KEGG	faa:HMPREF0389_00529.
Organism-specific databases
CMR	Search...
Phylogenomic databases
KO	K03798.
OMA	NANADEQ.
Family and domain databases
HAMAP	MF_01458. FtsH.
InterPro	IPR003593. AAA+_ATPase. IPR003959. ATPase_AAA_core. IPR003960. ATPase_AAA_CS. IPR005936. FtsH. IPR011546. Pept_M41_FtsH_extracell. IPR000642. Peptidase_M41. [Graphical view]
Pfam	PF00004. AAA. 1 hit. PF06480. FtsH_ext. 1 hit. PF01434. Peptidase_M41. 1 hit. [Graphical view]
SMART	SM00382. AAA. 1 hit. [Graphical view]
TIGRFAMs	TIGR01241. FtsH_fam. 1 hit.
PROSITE	PS00674. AAA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

D6GSH1_FILAD

Accession

Primary (citable) accession number: D6GSH1

Entry history

Integrated into UniProtKB/TrEMBL:	July 13, 2010
Last sequence update:	July 13, 2010
Last modified:	May 1, 2013
This is version 15 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information