ATP-dependent zinc metalloprotease FtsH - Alicycliphilus denitrificans (strain DSM 14773 / CIP 107495 / K601)

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:	Alide2_2675 EMBL AEB85032.1

Organism

Alicycliphilus denitrificans (strain DSM 14773 / CIP 107495 / K601) [Complete proteome] [HAMAP] EMBL AEB85032.1

Taxonomic identifier

596154 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Alicycliphilus ›

Protein attributes

Sequence length	653 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 inner 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 inner membrane HAMAP-Rule MF_01458 Cell membrane 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 AEB85032.1 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 – 14

14

Cytoplasmic By similarity HAMAP-Rule MF_01458

Transmembrane

15 – 35

21

Helical; By similarity HAMAP-Rule MF_01458

Topological domain

36 – 120

85

Periplasmic By similarity HAMAP-Rule MF_01458

Transmembrane

121 – 141

21

Helical; By similarity HAMAP-Rule MF_01458

Topological domain

142 – 653

512

Cytoplasmic By similarity HAMAP-Rule MF_01458

Nucleotide binding

214 – 221

8

ATP By similarity HAMAP-Rule MF_01458

Sites

Active site

437

1

By similarity HAMAP-Rule MF_01458

Metal binding

436

1

Zinc; catalytic By similarity HAMAP-Rule MF_01458

Metal binding

440

1

Zinc; catalytic By similarity HAMAP-Rule MF_01458

Metal binding

512

1

Zinc; catalytic By similarity HAMAP-Rule MF_01458

Sequences

Sequence

Length

Mass (Da)

Tools

F4GFL7 [UniParc].

Last modified June 28, 2011. Version 1.
Checksum: 7396C094C53E88F6
Show »

FASTA

653

71,790

        10         20         30         40         50         60 
MAVHLFLNLE PRLNNQWFSK VAVWLVIAMV LFTVFKQFDT RVGAGAGAIG YSDFLEDVRS 

        70         80         90        100        110        120 
HRIKSVTIQE GPGGATEILA TTNDDRRIRT TATYLDRGLV GDLINNNVKF DVKPREEGSL 

       130        140        150        160        170        180 
LMTLLVSWGP MLLLIGVWVY FMRQMQGGGK GGAFSFGKSK ARMLDENNNT VTFADVAGCD 

       190        200        210        220        230        240 
EAKEEVKEVV DFLKDPQKFQ KLGGRIPRGL LLVGPPGTGK TLLAKSIAGE AKVPFFSISG 

       250        260        270        280        290        300 
SDFVEMFVGV GAARVRDMFE NAKKNAPCII FIDEIDAVGR QRGAGLGGGN DEREQTLNQM 

       310        320        330        340        350        360 
LVEMDGFETN LGVIVVAATN RPDILDAALL RPGRFDRQVY VTLPDIRGRE QILNVHMRKI 

       370        380        390        400        410        420 
PVGQDVNPAI IARGTPGMSG ADLANLCNEA ALMAARRNAR TVEMQDFEKA KDKIIMGPER 

       430        440        450        460        470        480 
KSMVMPEEER RNTAYHEAGH ALIGKLLPKC DPVHKVTIIP RGRALGVTMS LPEKDRYSYD 

       490        500        510        520        530        540 
KEYMLNQIAM LFGGRIAEEV FMHQMTTGAS NDFERATNLA RDMVMKYGMS EALGPMVYAE 

       550        560        570        580        590        600 
NEGEVFLGRS VTKTTNISEE TMQKVDAEVR RIIDEQYALA RKLIEDNQDK MHAMAKAMLE 

       610        620        630        640        650 
WETIDAEQLD DIMAGRAPRP PKDWTPRTPS SGGDGSAGGG TPAVKPDPAP SAA

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References

[1]

"Complete sequence of chromosome of Alicycliphilus denitrificans K601."
US DOE Joint Genome Institute
Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Peters L., Zeytun A., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Oosterkamp M.

Woyke T.
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 14773 / CIP 107495 / K601.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP002657 Genomic DNA. Translation: AEB85032.1.
RefSeq	YP_004388548.1. NC_015422.1.
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	M41.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AEB85032; AEB85032; Alide2_2675.
GeneID	10483723.
KEGG	adk:Alide2_2675.
PATRIC	54528050. VBIAliDen79014_2708.
Organism-specific databases
CMR	Search...
Phylogenomic databases
KO	K03798.
Enzyme and pathway databases
BioCyc	ADEN596154:GHU6-2796-MONOMER.
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

F4GFL7_ALIDK

Accession

Primary (citable) accession number: F4GFL7

Entry history

Integrated into UniProtKB/TrEMBL:	June 28, 2011
Last sequence update:	June 28, 2011
Last modified:	April 3, 2013
This is version 14 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

Enzyme and pathway databases

Family and domain databases

Entry information