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Protein

ATP-dependent zinc metalloprotease FtsH

Gene

ftsH

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation
In vitro partially degrades Spo0E, the phosphatase that acts on Spo0A-P. Recognition requires the last 14 residues of Spo0E.

Cofactori

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi423 – 4231Zinc; catalyticUniRule annotation
Active sitei424 – 4241UniRule annotation
Metal bindingi427 – 4271Zinc; catalyticUniRule annotation
Metal bindingi499 – 4991Zinc; catalyticUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi201 – 2088ATPUniRule annotation

GO - Molecular functioni

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • cell division Source: UniProtKB-KW
  • protein catabolic process Source: UniProtKB
  • sporulation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Cell cycle, Cell division, Stress response

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciBSUB:BSU00690-MONOMER.

Protein family/group databases

MEROPSiM41.009.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent zinc metalloprotease FtsHUniRule annotation (EC:3.4.24.-UniRule annotation)
Alternative name(s):
Cell division protease FtsH
Gene namesi
Name:ftsHUniRule annotation
Ordered Locus Names:BSU00690
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

  • Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication; Cytoplasmic side 1 Publication

  • 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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 77CytoplasmicUniRule annotation
Transmembranei8 – 2821HelicalUniRule annotationAdd
BLAST
Topological domaini29 – 10981ExtracellularUniRule annotationAdd
BLAST
Transmembranei110 – 13021HelicalUniRule annotationAdd
BLAST
Topological domaini131 – 637507CytoplasmicUniRule annotationAdd
BLAST

GO - Cellular componenti

  • cell septum Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi207 – 2071K → N: Does not complement an ftsH deletion, loss of ATPase activity. 1 Publication
Mutagenesisi424 – 4241E → Q: Does not complement an ftsH deletion, loss of protease activity against casein. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 637637ATP-dependent zinc metalloprotease FtsHPRO_0000084627Add
BLAST

Proteomic databases

PaxDbiP37476.

Expressioni

Developmental stagei

Necessary only for stage 0 of sporulation.1 Publication

Inductioni

Induced by osmotic shock (0.8 M NaCl) and by heat shock (52 degrees Celsius).1 Publication

Interactioni

Subunit structurei

Homohexamer.UniRule annotation

Protein-protein interaction databases

IntActiP37476. 8 interactions.
MINTiMINT-8365816.
STRINGi224308.Bsubs1_010100000350.

Structurei

3D structure databases

ProteinModelPortaliP37476.
SMRiP37476. Positions 147-602.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni514 – 637124Not necessary for FtsH functionAdd
BLAST

Sequence similaritiesi

In the central section; belongs to the AAA ATPase family.UniRule annotation
In the C-terminal section; belongs to the peptidase M41 family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105C3H. Bacteria.
COG0465. LUCA.
HOGENOMiHOG000217276.
InParanoidiP37476.
KOiK03798.
OMAiHTEAWTI.
OrthoDBiEOG6PKFBJ.
PhylomeDBiP37476.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_01458. FtsH.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR005936. FtsH.
IPR027417. P-loop_NTPase.
IPR011546. Pept_M41_FtsH_extracell.
IPR000642. Peptidase_M41.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
PF06480. FtsH_ext. 1 hit.
PF01434. Peptidase_M41. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01241. FtsH_fam. 1 hit.
PROSITEiPS00674. AAA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P37476-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNRVFRNTIF YLLILLVVIG VVSYFQTSNP KTENMSYSTF IKNLDDGKVD
60 70 80 90 100
SVSVQPVRGV YEVKGQLKNY DKDQYFLTHV PEGKGADQIF NALKKTDVKV
110 120 130 140 150
EPAQETSGWV TFLTTIIPFV IIFILFFFLL NQAQGGGSRV MNFGKSKAKL
160 170 180 190 200
YTEEKKRVKF KDVAGADEEK QELVEVVEFL KDPRKFAELG ARIPKGVLLV
210 220 230 240 250
GPPGTGKTLL AKACAGEAGV PFFSISGSDF VEMFVGVGAS RVRDLFENAK
260 270 280 290 300
KNAPCLIFID EIDAVGRQRG AGLGGGHDER EQTLNQLLVE MDGFSANEGI
310 320 330 340 350
IIIAATNRAD ILDPALLRPG RFDRQITVDR PDVIGREAVL KVHARNKPLD
360 370 380 390 400
ETVNLKSIAM RTPGFSGADL ENLLNEAALV AARQNKKKID ARDIDEATDR
410 420 430 440 450
VIAGPAKKSR VISKKERNIV AYHEGGHTVI GLVLDEADMV HKVTIVPRGQ
460 470 480 490 500
AGGYAVMLPR EDRYFQTKPE LLDKIVGLLG GRVAEEIIFG EVSTGAHNDF
510 520 530 540 550
QRATNIARRM VTEFGMSEKL GPLQFGQSQG GQVFLGRDFN NEQNYSDQIA
560 570 580 590 600
YEIDQEIQRI IKECYERAKQ ILTENRDKLE LIAQTLLKVE TLDAEQIKHL
610 620 630
IDHGTLPERN FSDDEKNDDV KVNILTKTEE KKDDTKE
Length:637
Mass (Da):70,937
Last modified:October 1, 1994 - v1
Checksum:iC62B6C518B91C9D3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26185 Genomic DNA. Translation: BAA05304.1.
AL009126 Genomic DNA. Translation: CAB11845.1.
PIRiE69627.
RefSeqiNP_387950.1. NC_000964.3.
WP_003243881.1. NZ_JNCM01000028.1.

Genome annotation databases

EnsemblBacteriaiCAB11845; CAB11845; BSU00690.
GeneIDi938094.
KEGGibsu:BSU00690.
PATRICi18971613. VBIBacSub10457_0070.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26185 Genomic DNA. Translation: BAA05304.1.
AL009126 Genomic DNA. Translation: CAB11845.1.
PIRiE69627.
RefSeqiNP_387950.1. NC_000964.3.
WP_003243881.1. NZ_JNCM01000028.1.

3D structure databases

ProteinModelPortaliP37476.
SMRiP37476. Positions 147-602.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP37476. 8 interactions.
MINTiMINT-8365816.
STRINGi224308.Bsubs1_010100000350.

Protein family/group databases

MEROPSiM41.009.

Proteomic databases

PaxDbiP37476.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB11845; CAB11845; BSU00690.
GeneIDi938094.
KEGGibsu:BSU00690.
PATRICi18971613. VBIBacSub10457_0070.

Phylogenomic databases

eggNOGiENOG4105C3H. Bacteria.
COG0465. LUCA.
HOGENOMiHOG000217276.
InParanoidiP37476.
KOiK03798.
OMAiHTEAWTI.
OrthoDBiEOG6PKFBJ.
PhylomeDBiP37476.

Enzyme and pathway databases

BioCyciBSUB:BSU00690-MONOMER.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_01458. FtsH.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR005936. FtsH.
IPR027417. P-loop_NTPase.
IPR011546. Pept_M41_FtsH_extracell.
IPR000642. Peptidase_M41.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
PF06480. FtsH_ext. 1 hit.
PF01434. Peptidase_M41. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01241. FtsH_fam. 1 hit.
PROSITEiPS00674. AAA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: SPO0E AS SUBSTRATE, DEVELOPMENTAL STAGE.
    Strain: 1012.

Entry informationi

Entry nameiFTSH_BACSU
AccessioniPrimary (citable) accession number: P37476
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: February 17, 2016
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.