ATP-dependent zinc metalloprotease FtsH precursor - Deinococcus proteolyticus (strain ATCC 35074 / DSM 20540 / JCM 6276 / NBRC 101906 / NCIMB 13154 / VKM Ac-1939 / CCM 2703)

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:	Deipr_0428 EMBL ADY25598.1

Organism

Deinococcus proteolyticus (strain ATCC 35074 / DSM 20540 / JCM 6276 / NBRC 101906 / NCIMB 13154 / VKM Ac-1939 / CCM 2703) [Complete proteome] [HAMAP] EMBL ADY25598.1

Taxonomic identifier

693977 [NCBI]

Taxonomic lineage

Bacteria › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus ›

Protein attributes

Sequence length	655 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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	Signal EMBL ADY25598.1 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 ADY25598.1 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

Molecule processing

Signal peptide

1 – 36

36

Potential EMBL ADY25598.1

Chain

37 – 655

619

Potential EMBL ADY25598.1

PRO_5000718162

Regions

Topological domain

1 – 16

16

Cytoplasmic By similarity HAMAP-Rule MF_01458

Transmembrane

17 – 37

21

Helical; By similarity HAMAP-Rule MF_01458

Topological domain

38 – 139

102

Extracellular By similarity HAMAP-Rule MF_01458

Transmembrane

140 – 160

21

Helical; By similarity HAMAP-Rule MF_01458

Topological domain

161 – 655

495

Cytoplasmic By similarity HAMAP-Rule MF_01458

Nucleotide binding

233 – 240

8

ATP By similarity HAMAP-Rule MF_01458

Sites

Active site

460

1

By similarity HAMAP-Rule MF_01458

Metal binding

459

1

Zinc; catalytic By similarity HAMAP-Rule MF_01458

Metal binding

463

1

Zinc; catalytic By similarity HAMAP-Rule MF_01458

Metal binding

534

1

Zinc; catalytic By similarity HAMAP-Rule MF_01458

Sequences

Sequence

Length

Mass (Da)

Tools

F0RJX2 [UniParc].

Last modified May 3, 2011. Version 1.
Checksum: 1906EFAC65D4A1E5
Show »

FASTA

655

69,499

        10         20         30         40         50         60 
MHLRPARPVS ARRPARWSAA LGTLVLTGLL AACGPAATST QQLQEVTGDG ATPSLRTTSD 

        70         80         90        100        110        120 
AAASGGATTA LPHYTSEQFL RDLRAGKITS AMLSSSGNAT VFVRDRPGPE AVALPPDGET 

       130        140        150        160        170        180 
LTLLREANVP FTVSSSRSRF AWLGQILPVA VTLLILLVMW RTIRAQQSGA AASAFGKSRA 

       190        200        210        220        230        240 
SVIVPAKVGV TFADVAGCEE AKADLQEVVD FLRQPEKYRA LGARIPHGLL LVGPPGSGKT 

       250        260        270        280        290        300 
LLAKAVAGEA GVPYFAVSGS DFVEMFVGVG AARVRDLFEQ ARKAAPCIIF MDEIDAVGRK 

       310        320        330        340        350        360 
RGTGMQGGND EREQTLNGLL VEMDGFRGEA DEGQDIIILA ATNRPDVLDA ALLRPGRFDR 

       370        380        390        400        410        420 
QVVVDAPDAA VRERILRVHS RTKPLDPGVD LSVIARRTAG MVGADLENLL NEAALLAARS 

       430        440        450        460        470        480 
GRPRILMADI DEARDRVLMG PERRSLVIQE ADRRITAYHE VGHALAAQLL PHAHRVAKLT 

       490        500        510        520        530        540 
VVPRGRAAGY MLPDAKDTLH VTRAALQDML TVALAGRAAE EVVMGEVTAG AQNDFQQATG 

       550        560        570        580        590        600 
LARRMVTEWG MGERTGKVAW ASEDSGYLGG GPQPLPMSQA TARTIDQEVE DLVTQAHGQA 

       610        620        630        640        650 
VRLVREYLPQ VHRVAEALLQ RESLSGEEFS ALLAGGQLDG EAGTSAPPAP RPAPT

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References

[1]

"The complete sequence of chromosome of Deinococcus proteolyticus DSM 20540."
US DOE Joint Genome Institute (JGI-PGF)
Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., Zeytun A., Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.

Eisen J.A.
Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35074 / DSM 20540 / JCM 6276 / NBRC 101906 / NCIMB 13154 / VKM Ac-1939 / CCM 2703.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP002536 Genomic DNA. Translation: ADY25598.1.
RefSeq	YP_004255215.1. NC_015161.1.
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	M41.013.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ADY25598; ADY25598; Deipr_0428.
GeneID	10255895.
KEGG	dpt:Deipr_0428.
PATRIC	46928612. VBIDeiPro159979_0421.
Organism-specific databases
CMR	Search...
Phylogenomic databases
KO	K03798.
Enzyme and pathway databases
BioCyc	DPRO693977:GCFA-445-MONOMER.
Family and domain databases
HAMAP	MF_01458. FtsH.
InterPro	IPR003593. AAA+_ATPase. IPR003959. ATPase_AAA_core. IPR003960. ATPase_AAA_CS. IPR005936. FtsH. IPR027417. P-loop_NTPase. IPR000642. Peptidase_M41. [Graphical view]
Pfam	PF00004. AAA. 1 hit. PF01434. Peptidase_M41. 1 hit. [Graphical view]
SMART	SM00382. AAA. 1 hit. [Graphical view]
SUPFAM	SSF52540. SSF52540. 1 hit.
TIGRFAMs	TIGR01241. FtsH_fam. 1 hit.
PROSITE	PS00674. AAA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

F0RJX2_DEIPM

Accession

Primary (citable) accession number: F0RJX2

Entry history

Integrated into UniProtKB/TrEMBL:	May 3, 2011
Last sequence update:	May 3, 2011
Last modified:	May 29, 2013
This is version 17 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)

Molecule processing

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