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ECOLI:FTSH

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) ftsH (ECO:0000255 with HAMAP-Rule:MF_01458) (synonyms: hflB, mrsC, std, tolZ)
Protein Name(s) ATP-dependent zinc metalloprotease FtsH (ECO:0000255 with HAMAP-Rule:MF_01458)

Cell division protease FtsH

External Links
UniProt P0AAI3
EMBL M83138
U01376
U18997
U00096
AP009048
PIR S35109
RefSeq NP_417645.1
YP_491363.1
PDB 1LV7
PDBsum 1LV7
ProteinModelPortal P0AAI3
SMR P0AAI3
DIP DIP-35828N
IntAct P0AAI3
MINT MINT-1226643
STRING 511145.b3178
MEROPS M41.001
PaxDb P0AAI3
PRIDE P0AAI3
EnsemblBacteria AAC76210
BAE77222
GeneID 12933986
947690
KEGG ecj:Y75_p3098
eco:b3178
PATRIC 32121774
EchoBASE EB1469
EcoGene EG11506
eggNOG COG0465
HOGENOM HOG000217276
InParanoid P0AAI3
KO K03798
OMA DAKQIDD
OrthoDB EOG6PKFBJ
PhylomeDB P0AAI3
BioCyc EcoCyc:EG11506-MONOMER
ECOL316407:JW3145-MONOMER
MetaCyc:EG11506-MONOMER
SABIO-RK P0AAI3
EvolutionaryTrace P0AAI3
PRO PR:P0AAI3
Proteomes UP000000318
UP000000625
Genevestigator P0AAI3
GO GO:0016021
GO:0005886
GO:0005524
GO:0016887
GO:0043273
GO:0030145
GO:0004222
GO:0008270
GO:0006200
GO:0030163
GO:0006508
Gene3D 3.40.50.300
HAMAP MF_01458
InterPro IPR003593
IPR003959
IPR003960
IPR005936
IPR027417
IPR011546
IPR000642
Pfam PF00004
PF06480
PF01434
SMART SM00382
SUPFAM SSF52540
TIGRFAMs TIGR01241
PROSITE PS00674

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0006508

proteolysis

PMID:7753838[1]

ECO:0000315

P

Figure 2 shows overproduction of FtsH in the mutant increases degradation of SecY.

complete

involved_in

GO:0030163

protein catabolic process

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000554354
UniProtKB:P37476
UniProtKB:P9WQN3

P

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11506
PANTHER:PTN000554253
UniProtKB:P9WQN3
UniProtKB:Q8I526

P

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000554354
UniProtKB:P9WQN3

C

Seeded From UniProt

complete

enables

GO:0004176

ATP-dependent peptidase activity

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11506
MGI:MGI:1351651
PANTHER:PTN000554253
SGD:S000006228
UniProtKB:Q8I526
UniProtKB:Q96TA2

F

Seeded From UniProt

complete

enables

GO:0043273

CTPase activity

PMID:7781608[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0030145

manganese ion binding

PMID:7781608[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0016887

ATPase activity

PMID:7781608[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0016021

integral component of membrane

PMID:8444797[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0008270

zinc ion binding

PMID:7781608[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

PMID:7781608[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0098796

membrane protein complex

PMID:8947034[5]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0ABC3
UniProtKB:P0ABC7

C

Seeded From UniProt

complete

enables

GO:0008270

zinc ion binding

PMID:7781608[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008270

zinc ion binding

PMID:7781608[3]

ECO:0000255

match to sequence model evidence used in manual assertion

F

Seeded From UniProt

Missing: with/from

involved_in

GO:0006508

proteolysis

PMID:7724592[6]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

PMID:8980112[7]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

PMID:7781608[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005887

integral component of plasma membrane

PMID:1925026[8]

ECO:0000255

match to sequence model evidence used in manual assertion

C

Seeded From UniProt

Missing: with/from

enables

GO:0005524

ATP binding

PMID:1925026[8]

ECO:0000255

match to sequence model evidence used in manual assertion

F

Seeded From UniProt

Missing: with/from

enables

GO:0004222

metalloendopeptidase activity

PMID:10809689[9]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004176

ATP-dependent peptidase activity

PMID:8980112[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004176

ATP-dependent peptidase activity

PMID:7781608[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004222

metalloendopeptidase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000642
InterPro:IPR005936
InterPro:IPR011546
InterPro:IPR037219

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000642
InterPro:IPR003959
InterPro:IPR003960
InterPro:IPR011546
InterPro:IPR037219

F

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000642
InterPro:IPR037219

P

Seeded From UniProt

complete

enables

GO:0008270

zinc ion binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011546

F

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005936

C

Seeded From UniProt

complete

part_of

GO:0016021

integral component of membrane

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011546

C

Seeded From UniProt

complete

enables

GO:0016887

ATPase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000078252

F

Seeded From UniProt

complete

involved_in

GO:0030163

protein catabolic process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000078252

P

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000078252

F

Seeded From UniProt

complete

enables

GO:0008270

zinc ion binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000078252

F

Seeded From UniProt

complete

enables

GO:0008233

peptidase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000078252

F

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000078252

C

Seeded From UniProt

complete

enables

GO:0008233

peptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0645

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0645

P

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

enables

GO:0008237

metallopeptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0482

F

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

part_of

GO:0016021

integral component of membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0812

C

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

GO_REF:0000037
GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0997
UniProtKB-KW:KW-1003
UniProtKB-SubCell:SL-0037

C

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

edit table

Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ Kihara, A et al. (1995) FtsH is required for proteolytic elimination of uncomplexed forms of SecY, an essential protein translocase subunit. Proc. Natl. Acad. Sci. U.S.A. 92 4532-6 PubMed GONUTS page
  2. ↑ 2.0 2.1 2.2 2.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  3. ↑ 3.0 3.1 3.2 3.3 3.4 3.5 3.6 3.7 3.8 Tomoyasu, T et al. (1995) Escherichia coli FtsH is a membrane-bound, ATP-dependent protease which degrades the heat-shock transcription factor sigma 32. EMBO J. 14 2551-60 PubMed GONUTS page
  4. ↑ Tomoyasu, T et al. (1993) Topology and subcellular localization of FtsH protein in Escherichia coli. J. Bacteriol. 175 1352-7 PubMed GONUTS page
  5. ↑ Kihara, A et al. (1996) A protease complex in the Escherichia coli plasma membrane: HflKC (HflA) forms a complex with FtsH (HflB), regulating its proteolytic activity against SecY. EMBO J. 15 6122-31 PubMed GONUTS page
  6. ↑ Herman, C et al. (1995) Degradation of sigma 32, the heat shock regulator in Escherichia coli, is governed by HflB. Proc. Natl. Acad. Sci. U.S.A. 92 3516-20 PubMed GONUTS page
  7. ↑ 7.0 7.1 Akiyama, Y et al. (1996) Subunit a of proton ATPase F0 sector is a substrate of the FtsH protease in Escherichia coli. FEBS Lett. 399 26-8 PubMed GONUTS page
  8. ↑ 8.0 8.1 Ogura, T et al. () Structure and function of the ftsH gene in Escherichia coli. Res. Microbiol. 142 279-82 PubMed GONUTS page
  9. ↑ Shotland, Y et al. (2000) Proteolysis of bacteriophage lambda CII by Escherichia coli FtsH (HflB). J. Bacteriol. 182 3111-6 PubMed GONUTS page
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