ATP-dependent zinc metalloprotease FtsH

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P37476 (FTSH_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 99. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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

Alternative name(s):
Cell division protease FtsH

Gene names

Name:	ftsH
Ordered Locus Names:	BSU00690

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	637 AA.
Sequence status	Complete.
Protein existence	Evidence 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 In vitro partially degrades Spo0E, the phosphatase that acts on Spo0A-P. Recognition requires the last 14 residues of Spo0E. HAMAP MF_01458
Cofactor	Binds 1 zinc ion per subunit By similarity. HAMAP MF_01458
Subunit structure	Homohexamer Potential.
Subcellular location	Cell membrane; Multi-pass membrane protein; Cytoplasmic side Probable. Note: Accumulates in the midcell septum during vegetative cell division. At the onset of sporulation appears at positions near the cell poles that may coincide with future division sites. Then, FtsH becomes concentrated at the sporulation septum and disappears from the distal pole. Ref.6
Developmental stage	Necessary only for stage 0 of sporulation. Ref.8
Induction	Induced by osmotic shock (0.8 M NaCl) and by heat shock (52 degrees Celsius). Ref.3
Disruption phenotype	Required for expression of the stage 0 sporulation gene Spo0A, as well as for a normal heat or osmotic stress response, cells lacking this gene grow as long filaments and tend to lyse upon entry into stationary phase. Secretion of some extracellular proteins is also reduced. Ref.4
Sequence similarities	In the central section; belongs to the AAA ATPase family. In the C-terminal section; belongs to the peptidase M41 family.

Ontologies

Keywords
Biological process	Cell cycle Cell division Stress response
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW protein catabolic process Inferred from direct assay Ref.7. Source: UniProtKB proteolysis Inferred from electronic annotation. Source: UniProtKB-KW response to stress Inferred from electronic annotation. Source: UniProtKB-KW sporulation Inferred from mutant phenotype Ref.4. Source: UniProtKB
Cellular component	cell septum Inferred from direct assay Ref.6. Source: UniProtKB 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: UniProtKB-KW metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro nucleoside-triphosphatase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 637

637

ATP-dependent zinc metalloprotease FtsH HAMAP MF_01458

PRO_0000084627

Regions

Topological domain

1 – 7

Cytoplasmic Potential

Transmembrane

8 – 28

Helical; Potential

Topological domain

29 – 109

Extracellular Potential

Transmembrane

110 – 130

Helical; Potential

Topological domain

131 – 637

507

Cytoplasmic Potential

Nucleotide binding

201 – 208

ATP Potential

Region

514 – 637

124

Not necessary for FtsH function HAMAP MF_01458

Sites

Active site

424

By similarity

Metal binding

423

Zinc; catalytic By similarity

Metal binding

427

Zinc; catalytic By similarity

Metal binding

499

Zinc; catalytic By similarity

Experimental info

Mutagenesis

207

K → N: Does not complement an ftsH deletion, loss of ATPase activity. Ref.7

Mutagenesis

424

E → Q: Does not complement an ftsH deletion, loss of protease activity against casein. Ref.7

Sequences

Sequence

Length

Mass (Da)

Tools

P37476 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: C62B6C518B91C9D3
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FASTA

637

70,937

        10         20         30         40         50         60 
MNRVFRNTIF YLLILLVVIG VVSYFQTSNP KTENMSYSTF IKNLDDGKVD SVSVQPVRGV 

        70         80         90        100        110        120 
YEVKGQLKNY DKDQYFLTHV PEGKGADQIF NALKKTDVKV EPAQETSGWV TFLTTIIPFV 

       130        140        150        160        170        180 
IIFILFFFLL NQAQGGGSRV MNFGKSKAKL YTEEKKRVKF KDVAGADEEK QELVEVVEFL 

       190        200        210        220        230        240 
KDPRKFAELG ARIPKGVLLV GPPGTGKTLL AKACAGEAGV PFFSISGSDF VEMFVGVGAS 

       250        260        270        280        290        300 
RVRDLFENAK KNAPCLIFID EIDAVGRQRG AGLGGGHDER EQTLNQLLVE MDGFSANEGI 

       310        320        330        340        350        360 
IIIAATNRAD ILDPALLRPG RFDRQITVDR PDVIGREAVL KVHARNKPLD ETVNLKSIAM 

       370        380        390        400        410        420 
RTPGFSGADL ENLLNEAALV AARQNKKKID ARDIDEATDR VIAGPAKKSR VISKKERNIV 

       430        440        450        460        470        480 
AYHEGGHTVI GLVLDEADMV HKVTIVPRGQ AGGYAVMLPR EDRYFQTKPE LLDKIVGLLG 

       490        500        510        520        530        540 
GRVAEEIIFG EVSTGAHNDF QRATNIARRM VTEFGMSEKL GPLQFGQSQG GQVFLGRDFN 

       550        560        570        580        590        600 
NEQNYSDQIA YEIDQEIQRI IKECYERAKQ ILTENRDKLE LIAQTLLKVE TLDAEQIKHL 

       610        620        630 
IDHGTLPERN FSDDEKNDDV KVNILTKTEE KKDDTKE

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin." Ogasawara N., Nakai S., Yoshikawa H. DNA Res. 1:1-14(1994) [PubMed: 7584024] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[3]	"The ftsH gene of Bacillus subtilis is transiently induced after osmotic and temperature upshift." Deuerling E., Paeslack B., Schumann W. J. Bacteriol. 177:4105-4112(1995) [PubMed: 7608085] [Abstract] Cited for: INDUCTION. Strain: 1012.
[4]	"The ftsH gene of Bacillus subtilis is involved in major cellular processes such as sporulation, stress adaptation and secretion." Deuerling E., Mogk A., Richter C., Purucker M., Schumann W. Mol. Microbiol. 23:921-933(1997) [PubMed: 9076729] [Abstract] Cited for: DISRUPTION PHENOTYPE. Strain: 1012.
[5]	"Role of the sporulation protein BofA in regulating activation of the Bacillus subtilis developmental transcription factor sigmaK." Resnekov O. J. Bacteriol. 181:5384-5388(1999) [PubMed: 10464210] [Abstract] Cited for: SPOIVFA AS A POSSIBLE SUBSTRATE.
[6]	"The FtsH protein accumulates at the septum of Bacillus subtilis during cell division and sporulation." Wehrl W., Niederweis M., Schumann W. J. Bacteriol. 182:3870-3873(2000) [PubMed: 10851010] [Abstract] Cited for: SUBCELLULAR LOCATION.
[7]	"Construction and analyses of mutant ftsH alleles of Bacillus subtilis involving the ATPase- and Zn-binding domains." Kotschwar M., Harfst E., Ohanjan T., Schumann W. Curr. Microbiol. 49:180-185(2004) [PubMed: 15386101] [Abstract] Cited for: ATPASE AND PROTEASE ACTIVITIES, MUTAGENESIS OF LYS-207 AND GLU-424. Strain: 1012.
[8]	"The Spo0E phosphatase of Bacillus subtilis is a substrate of the FtsH metalloprotease." Le A.T., Schumann W. Microbiology 155:1122-1132(2009) [PubMed: 19332814] [Abstract] Cited for: SPO0E AS SUBSTRATE, DEVELOPMENTAL STAGE. Strain: 1012.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D26185 Genomic DNA. Translation: BAA05304.1. AL009126 Genomic DNA. Translation: CAB11845.1.
PIR	E69627.
RefSeq	NP_387950.1. NC_000964.3.
3D structure databases
ProteinModelPortal	P37476.
SMR	P37476. Positions 147-602.
ModBase	Search...
Protein-protein interaction databases
IntAct	P37476. 7 interactions.
Protein family/group databases
MEROPS	M41.009.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000001428; EBBACP00000001428; EBBACG00000001426.
GeneID	938094.
GenomeReviews	Gene locus BSU00690 in contig AL009126_GR.
KEGG	bsu:BSU00690.
NMPDR	fig\|224308.1.peg.69.
PATRIC	18971613. VBIBacSub10457_0070.
Organism-specific databases
GenoList	BSU00690. [Micado]
Phylogenomic databases
GeneTree	EBGT00050000001925.
HOGENOM	HBG724153.
OMA	KETISHE.
PhylomeDB	P37476.
ProtClustDB	CLSK886567.
Enzyme and pathway databases
BioCyc	BSUB:BSU00690-MONOMER.
Family and domain databases
HAMAP	MF_01458. FtsH. [Tree]
InterPro	IPR003593. 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]
KO	K03798.
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

FTSH_BACSU

Accession

Primary (citable) accession number: P37476

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	January 25, 2012
This is version 99 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction 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

Relevant documents