P0AAI3 (FTSH_ECOLI) Reviewed, UniProtKB/Swiss-Prot

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
Synonyms:	hflB, mrsC, std, tolZ
Ordered Locus Names:	b3178, JW3145

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	644 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. Degrades a few membrane proteins that have not been assembled into complexes such as SecY, F0 ATPase subunit a and YccA, and also cytoplasmic proteins sigma-32, LpxC, KdtA and phage lambda cII protein among others. Degrades membrane proteins in a processive manner starting at either the N- or C-terminus; recognition requires a cytoplasmic tail of about 20 residues with no apparent sequence requirements. It presumably dislocates membrane-spanning and periplasmic segments of the protein into the cytoplasm to degrade them, this probably requires ATP. Degrades C-terminal-tagged cytoplasmic proteins which are tagged with an 11-amino-acid nonpolar destabilizing tail via a mechanism involving the 10SA (SsrA) stable RNA. Ref.9 Ref.10 Ref.17 Ref.25 As FtsH regulates the levels of both LpxC and KdtA it is required for synthesis of both the protein and lipid components of lipopolysaccharide (LPS). Ref.9 Ref.10 Ref.17 Ref.25
Cofactor	Binds 1 zinc ion per subunit. Requires ATP for protease catalytic activity, probably due to tight coupling of the 2 activities; ADP or non-hydrolyzable analogs cannot substitute, except when unfolded, non-physiological substrates are tested.
Enzyme regulation	Activity against phage lambda cII protein is inhibited by EDTA but not by PMSF. In vitro pre-incubation of FtsH with HflKC abolishes its activity against phage lambda cII protein; Cytoplasmic side. Ref.12
Subunit structure	The E.coli AAA domain has been modeled as a homohexamer, in Thermus thermophilus the same domain crystallizes as a homohexamer. Forms a complex with HflKC (formerly called HflA); complex formation is stimulated by ATP. Interacts with YccA, and probably weakly with QmcA. Can be cross-linked to YidC (OxaA) and to a nascent polypeptide chain for an integral membrane protein. Ref.11 Ref.12 Ref.14 Ref.23 Ref.24
Subcellular location	Cell inner membrane; Multi-pass membrane protein Ref.5 Ref.11 Ref.22.
Disruption phenotype	Lethality, due to increased levels of LpxC, which increases the level of LPS in the cell and results in formation of abnormal membrane structures in the periplasm. Lethality is suppressed under conditions in which LPS synthesis is reduced. Ref.17
Miscellaneous	The ftsH gene was discovered independently through 3 different phenotypes and received 3 different names: ftsH, for filamentous temperature-sensitive; tolZ, for colicin tolerance, and hlfB, because mutants show a high frequency of lysogenization when infected with phage lambda (Ref.29). HAMAP MF_01458
Sequence similarities	In the central section; belongs to the AAA ATPase family. In the C-terminal section; belongs to the peptidase M41 family.
Caution	Glu-476 was identified as the third Zn ligand (Ref.19), however in other crystal structures (Aquifex aeolicus and Thermotoga maritima) the conserved equivalent residue does not bind Zn. Instead it makes a hydrogen bond with the side chain of the first catalytic Zn-binding residue and indirectly stabilizes the Zn.
Sequence caution	The sequence AAA97508.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	protein catabolic process Inferred from electronic annotation. Source: InterPro proteolysis Inferred from direct assay Ref.9. Source: EcoliWiki
Cellular component	integral to membrane Inferred from direct assay Ref.5. Source: EcoliWiki plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity Inferred from direct assay Ref.9. Source: EcoliWiki CTPase activity Inferred from direct assay Ref.9. Source: EcoliWiki manganese ion binding Inferred from direct assay Ref.9. Source: EcoliWiki metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from direct assay Ref.9. Source: EcoliWiki
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 644

644

ATP-dependent zinc metalloprotease FtsH HAMAP MF_01458

PRO_0000084631

Regions

Topological domain

1 – 4

4

Cytoplasmic Probable

Transmembrane

5 – 25

21

Helical; Probable

Topological domain

26 – 98

73

Periplasmic Probable

Transmembrane

99 – 119

21

Helical; Probable

Topological domain

120 – 644

525

Cytoplasmic Probable

Nucleotide binding

192 – 199

8

ATP Potential

Sites

Active site

415

1

Probable

Metal binding

414

1

Zinc; catalytic Probable

Metal binding

418

1

Zinc; catalytic Probable

Metal binding

492

1

Zinc; catalytic By similarity

Site

225

1

Substrate binding Probable

Experimental info

Mutagenesis

201

1

L → N: No in vivo protease activity, no in vitro ATPase activity. Ref.16

Mutagenesis

225

1

F → A, D, E, G, N, Q, R, S or T: Does not complement ftsH1 at 42 degrees Celsius, no protease activity in vivo. Ref.21

Mutagenesis

225

1

F → C or H: Partially complements ftsH1 at 42 degrees Celsius, some protease activity in vivo. Ref.21

Mutagenesis

225

1

F → I, L, M, V, W or Y: Complements ftsH1 at 42 degrees Celsius, restores protease activity in vivo. Ref.21

Mutagenesis

227

1

G → A: Does not complement ftsH1 at 42 degrees Celsius, no protease activity in vivo. Ref.21

Mutagenesis

297

1

T → A: Low protease activity in vivo, low ATPase activity in vitro, complements ftsH1 at 42 degrees Celsius. Ref.16

Mutagenesis

298

1

N → A: No in vivo protease activity. Ref.16

Mutagenesis

304

1

D → A or N: No in vivo protease activity, no in vitro ATPase activity; probably still binds ATP. Ref.16

Mutagenesis

304

1

D → E: Low protease activity in vivo, low ATPase activity in vitro, complements ftsH1 at 42 degrees Celsius. Ref.16

Mutagenesis

307

1

L → A: Low protease activity in vivo. Ref.16

Mutagenesis

309

1

R → A, L or K: No in vivo protease activity, no ATPase activity in vitro; probably still binds ATP. Ref.16

Mutagenesis

312

1

R → A, L or K: No in vivo protease activity, no ATPase activity in vitro; probably still binds ATP. Ref.16

Mutagenesis

414 – 418

5

HEAGH → KEAGK: Loss of protease function. Ref.16 Ref.19

Mutagenesis

414

1

H → Y: Loss of protease function. Ref.19

Mutagenesis

415

1

E → Q: Loss of protease activity in vivo. Ref.16

Mutagenesis

418

1

H → Y in tolZ21; loss of protease function in vivo, retains about 25% ATPase activity, temperature sensitive. Ref.16 Ref.19

Mutagenesis

463

1

E → K in ftsH1; a temperature-sensitive mutant which increases the frequency of lysogenization of phage lambda; when associated with A-587. Ref.1

Mutagenesis

476

1

E → D, K or V: Severe loss of protease function that is restored by excess Zn. Ref.19

Mutagenesis

476

1

E → Q: Little effect on protease function. Ref.19

Mutagenesis

536

1

H → R in hflB29; increases the frequency of lysogenization of phage lambda. Ref.1

Mutagenesis

582

1

E → D, K or Q: No effect on protease function. Ref.19

Mutagenesis

582

1

E → V: Decreased protease function. Ref.19

Secondary structure

1

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644

Helix Strand Turn

Details...

Beta strand

142 – 147

6

Helix

151 – 153

3

Helix

158 – 163

6

Helix

165 – 172

8

Helix

174 – 176

3

Beta strand

187 – 191

5

Helix

198 – 209

12

Beta strand

213 – 216

4

Helix

230 – 241

12

Beta strand

245 – 250

6

Helix

253 – 256

4

Helix

270 – 283

14

Beta strand

287 – 289

3

Beta strand

291 – 298

8

Turn

300 – 302

3

Helix

305 – 308

4

Beta strand

315 – 318

4

Helix

324 – 335

12

Helix

346 – 351

6

Helix

358 – 374

17

Beta strand

378 – 380

3

Helix

382 – 392

11

Sequences

	Sequence		Length	Mass (Da)
	P0AAI3 [UniParc]. Last modified October 11, 2005. Version 1. Checksum: E24A753D8F486CA1	FASTA	644	70,708
	10 20 30 40 50 60 MAKNLILWLV IAVVLMSVFQ SFGPSESNGR KVDYSTFLQE VNNDQVREAR INGREINVTK 70 80 90 100 110 120 KDSNRYTTYI PVQDPKLLDN LLTKNVKVVG EPPEEPSLLA SIFISWFPML LLIGVWIFFM 130 140 150 160 170 180 RQMQGGGGKG AMSFGKSKAR MLTEDQIKTT FADVAGCDEA KEEVAELVEY LREPSRFQKL 190 200 210 220 230 240 GGKIPKGVLM VGPPGTGKTL LAKAIAGEAK VPFFTISGSD FVEMFVGVGA SRVRDMFEQA 250 260 270 280 290 300 KKAAPCIIFI DEIDAVGRQR GAGLGGGHDE REQTLNQMLV EMDGFEGNEG IIVIAATNRP 310 320 330 340 350 360 DVLDPALLRP GRFDRQVVVG LPDVRGREQI LKVHMRRVPL APDIDAAIIA RGTPGFSGAD 370 380 390 400 410 420 LANLVNEAAL FAARGNKRVV SMVEFEKAKD KIMMGAERRS MVMTEAQKES TAYHEAGHAI 430 440 450 460 470 480 IGRLVPEHDP VHKVTIIPRG RALGVTFFLP EGDAISASRQ KLESQISTLY GGRLAEEIIY 490 500 510 520 530 540 GPEHVSTGAS NDIKVATNLA RNMVTQWGFS EKLGPLLYAE EEGEVFLGRS VAKAKHMSDE 550 560 570 580 590 600 TARIIDQEVK ALIERNYNRA RQLLTDNMDI LHAMKDALMK YETIDAPQID DLMARRDVRP 610 620 630 640 PAGWEEPGAS NNSGDNGSPK APRPVDEPRT PNPGNTMSEQ LGDK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Escherichia coli FtsH protein is a prokaryotic member of a protein family of putative ATPases involved in membrane functions, cell cycle control, and gene expression." Tomoyasu T., Yuki T., Morimura S., Mori H., Yamanaka K., Niki H., Hiraga S., Ogura T. J. Bacteriol. 175:1344-1351(1993) [PubMed: 8444796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF GLU-463 AND HIS-536. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"Identification and physical analysis of new genes in the argG region (69 min) of Escherichia coli chromosome." Wang R., Kushner S.R. Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Topology and subcellular localization of FtsH protein in Escherichia coli." Tomoyasu T., Yamanaka K., Murata K., Suzaki T., Bouloc P., Kato A., Niki H., Hiraga S., Ogura T. J. Bacteriol. 175:1352-1357(1993) [PubMed: 8444797] [Abstract] Cited for: SUBCELLULAR LOCATION, TOPOLOGY. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Structure and function of the ftsH gene in Escherichia coli." Ogura T., Tomoyasu T., Yuki T., Morimura S., Begg K.J., Donachie W.D., Mori H., Niki H., Hiraga S. Res. Microbiol. 142:279-282(1991) [PubMed: 1925026] [Abstract] Cited for: DISCUSSION OF SEQUENCE.
[7]	"Cell growth and lambda phage development controlled by the same essential Escherichia coli gene, ftsH/hflB." Herman C., Ogura T., Tomoyasu T., Hiraga S., Akiyama Y., Ito K., Thomas R., D'Ari R., Bouloc P. Proc. Natl. Acad. Sci. U.S.A. 90:10861-10865(1993) [PubMed: 8248182] [Abstract] Cited for: IDENTIFICATION OF HFLB AS FTSH.
[8]	"Involvement of FtsH in protein assembly into and through the membrane. II. Dominant mutations affecting FtsH functions." Akiyama Y., Shirai Y., Ito K. J. Biol. Chem. 269:5225-5229(1994) [PubMed: 8106505] [Abstract] Cited for: CHARACTERIZATION.
[9]	"Escherichia coli FtsH is a membrane-bound, ATP-dependent protease which degrades the heat-shock transcription factor sigma 32." Tomoyasu T., Gamer J., Bukau B., Kanemori M., Mori H., Rutman A.J., Oppenheim A.B., Yura T., Yamanaka K., Niki H., Hiraga S., Ogura T. EMBO J. 14:2551-2560(1995) [PubMed: 7781608] [Abstract] Cited for: FUNCTION, SIGMA-32 AS SUBSTRATE.
[10]	"FtsH is required for proteolytic elimination of uncomplexed forms of SecY, an essential protein translocase subunit." Kihara A., Akiyama Y., Ito K. Proc. Natl. Acad. Sci. U.S.A. 92:4532-4536(1995) [PubMed: 7753838] [Abstract] Cited for: FUNCTION, SECY AS SUBSTRATE.
[11]	"A protease complex in the Escherichia coli plasma membrane: HflKC (HflA) forms a complex with FtsH (HflB), regulating its proteolytic activity against SecY." Kihara A., Akiyama Y., Ito K. EMBO J. 15:6122-6131(1996) [PubMed: 8947034] [Abstract] Cited for: INTERACTION WITH HFLC AND HFLK, SUBCELLULAR LOCATION. Strain: K12 / CSH26 / AD16.
[12]	"Host regulation of lysogenic decision in bacteriophage lambda: transmembrane modulation of FtsH (HflB), the cII degrading protease, by HflKC (HflA)." Kihara A., Akiyama Y., Ito K. Proc. Natl. Acad. Sci. U.S.A. 94:5544-5549(1997) [PubMed: 9159109] [Abstract] Cited for: ENZYME REGULATION, INTERACTION WITH HFLKC. Strain: K12 / CSH26 / AD16.
[13]	"Degradation of carboxy-terminal-tagged cytoplasmic proteins by the Escherichia coli protease HflB (FtsH)." Herman C., Thevenet D., Bouloc P., Walker G.C., D'Ari R. Genes Dev. 12:1348-1355(1998) [PubMed: 9573051] [Abstract] Cited for: CHARACTERIZATION.
[14]	"Different pathways for protein degradation by the FtsH/HflKC membrane-embedded protease complex: an implication from the interference by a mutant form of a new substrate protein, YccA." Kihara A., Akiyama Y., Ito K. J. Mol. Biol. 279:175-188(1998) [PubMed: 9636708] [Abstract] Cited for: MEMBRANE SUBSTRATES, INTERACTION WITH YCCA. Strain: K12 / CSH26 / AD16.
[15]	"Dislocation of membrane proteins in FtsH-mediated proteolysis." Kihara A., Akiyama Y., Ito K. EMBO J. 18:2970-2981(1999) [PubMed: 10357810] [Abstract] Cited for: MECHANISM OF MEMBRANE SUBSTRATE RECOGNITION. Strain: K12 / CSH26 / AD16.
[16]	"Dissecting the role of a conserved motif (the second region of homology) in the AAA family of ATPases. Site-directed mutagenesis of the ATP-dependent protease FtsH." Karata K., Inagawa T., Wilkinson A.J., Tatsuta T., Ogura T. J. Biol. Chem. 274:26225-26232(1999) [PubMed: 10473576] [Abstract] Cited for: MUTAGENESIS OF LYS-201; THR-297; ASN-298; ASP-304; LEU-307; ARG-309; ARG-312; GLN-415 AND HIS-418.
[17]	"Balanced biosynthesis of major membrane components through regulated degradation of the committed enzyme of lipid A biosynthesis by the AAA protease FtsH (HflB) in Escherichia coli." Ogura T., Inoue K., Tatsuta T., Suzaki T., Karata K., Young K., Su L.H., Fierke C.A., Jackman J.E., Raetz C.R., Coleman J., Tomoyasu T., Matsuzawa H. Mol. Microbiol. 31:833-844(1999) [PubMed: 10048027] [Abstract] Cited for: LPXC AS SUBSTRATE, FUNCTION IN REGULATING LIPOPOLYSACCHARIDE SYNTHESIS, DISRUPTION PHENOTYPE. Strain: K12 / W3110 and W2252.
[18]	"Length recognition at the N-terminal tail for the initiation of FtsH-mediated proteolysis." Chiba S., Akiyama Y., Mori H., Matsuo E., Ito K. EMBO Rep. 1:47-52(2000) [PubMed: 11256624] [Abstract] Cited for: RECOGNITION OF MEMBRANE SUBSTRATE FROM N-TERMINUS.
[19]	"Identification of glutamic acid 479 as the gluzincin coordinator of zinc in FtsH (HflB)." Saikawa N., Ito K., Akiyama Y. Biochemistry 41:1861-1868(2002) [PubMed: 11827531] [Abstract] Cited for: ZINC-BINDING, MUTAGENESIS OF HIS-414; HIS-418; GLU-476 AND GLU-582. Strain: K12.
[20]	"Membrane protein degradation by FtsH can be initiated from either end." Chiba S., Akiyama Y., Ito K. J. Bacteriol. 184:4775-4782(2002) [PubMed: 12169602] [Abstract] Cited for: RECOGNITION OF MEMBRANE SUBSTRATE FROM C-TERMINUS. Strain: K12 / JM103.
[21]	"Conserved pore residues in the AAA protease FtsH are important for proteolysis and its coupling to ATP hydrolysis." Yamada-Inagawa T., Okuno T., Karata K., Yamanaka K., Ogura T. J. Biol. Chem. 278:50182-50187(2003) [PubMed: 14514680] [Abstract] Cited for: REQUIREMENT FOR ATP, MUTAGENESIS OF PHE-225 AND GLY-227.
[22]	"Global topology analysis of the Escherichia coli inner membrane proteome." Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G. Science 308:1321-1323(2005) [PubMed: 15919996] [Abstract] Cited for: SUBCELLULAR LOCATION. Strain: K12 / MG1655 / ATCC 47076.
[23]	"The Escherichia coli plasma membrane contains two PHB (prohibitin homology) domain protein complexes of opposite orientations." Chiba S., Ito K., Akiyama Y. Mol. Microbiol. 60:448-457(2006) [PubMed: 16573693] [Abstract] Cited for: POSSIBLE INTERACTION WITH QMCA. Strain: K12.
[24]	"Detection of cross-links between FtsH, YidC, HflK/C suggests a linked role for these proteins in quality control upon insertion of bacterial inner membrane proteins." van Bloois E., Dekker H.L., Froderberg L., Houben E.N., Urbanus M.L., de Koster C.G., de Gier J.W., Luirink J. FEBS Lett. 582:1419-1424(2008) [PubMed: 18387365] [Abstract] Cited for: INTERACTION WITH YIDC (OXAA).
[25]	"Dual role of FtsH in regulating lipopolysaccharide biosynthesis in Escherichia coli." Katz C., Ron E.Z. J. Bacteriol. 190:7117-7122(2008) [PubMed: 18776015] [Abstract] Cited for: KDO TRANSFERASE (KDTA) AS SUBSTRATE, FUNCTION IN REGULATING LIPOPOLYSACCHARIDE BIOSYNTHESIS. Strain: K12 / MG1655 / ATCC 47076.
[26]	"Crystallization of the AAA domain of the ATP-dependent protease FtsH of Escherichia coli." Krzywda S., Brzozowski A.M., Karata K., Ogura T., Wilkinson A.J. Acta Crystallogr. D 582:1066-1067(2002) [PubMed: 12037319] [Abstract] Cited for: PRELIMINARY CRYSTALLIZATION.
[27]	"The crystal structure of the AAA domain of the ATP-dependent protease FtsH of Escherichia coli at 1.5 A resolution." Krzywda S., Brzozowski A.M., Verma C., Karata K., Ogura T., Wilkinson A.J. Structure 10:1073-1083(2002) [PubMed: 12176385] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 141-395.
[28]	"Quality control of cytoplasmic membrane proteins in Escherichia coli." Akiyama Y. J. Biochem. 146:449-454(2009) [PubMed: 19454621] [Abstract] Cited for: REVIEW.
[29]	"Degradation of cytoplasmic substrates by FtsH, a membrane-anchored protease with many talents." Narberhaus F., Obrist M., Fuhrer F., Langklotz S. Res. Microbiol. 160:652-659(2009) [PubMed: 19744556] [Abstract] Cited for: REVIEW.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M83138 Genomic DNA. Translation: AAA23813.1.
U01376 Genomic DNA. Translation: AAA97508.1. Different initiation.
U18997 Genomic DNA. Translation: AAA57979.1.
U00096 Genomic DNA. Translation: AAC76210.1.
AP009048 Genomic DNA. Translation: BAE77222.1.

PIR

S35109.

RefSeq

NP_417645.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LV7	X-ray	1.50	A	141-395	[»]

ProteinModelPortal

P0AAI3.

SMR

P0AAI3. Positions 139-602.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35828N.

IntAct

P0AAI3. 26 interactions.

MINT

MINT-1226643.

Protein family/group databases

MEROPS

M41.001.

Proteomic databases

PRIDE

P0AAI3.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000000369; EBESCP00000000369; EBESCG00000195129.
EBESCT00000000370; EBESCP00000000370; EBESCG00000195129.
EBESCT00000017485; EBESCP00000016776; EBESCG00000016541.

GeneID

947690.

GenomeReviews

Gene locus JW3145 in contig AP009048_GR.
Gene locus b3178 in contig U00096_GR.

KEGG

ecj:JW3145.
eco:b3178.

PATRIC

32121774. VBIEscCol129921_3271.

Organism-specific databases

EchoBASE

EB1469.

EcoGene

EG11506. ftsH.

Phylogenomic databases

eggNOG

COG0465.

GeneTree

EBGT00050000009542.

HOGENOM

HBG724153.

OMA

TYIPVND.

PhylomeDB

P0AAI3.

ProtClustDB

PRK10733.

Enzyme and pathway databases

BioCyc

EcoCyc:EG11506-MONOMER.
MetaCyc:EG11506-MONOMER.

Gene expression databases

Genevestigator

P0AAI3.

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_ECOLI

Accession

Primary (citable) accession number: P0AAI3
Secondary accession number(s): P28691, Q2M934

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2005
Last sequence update:	October 11, 2005
Last modified:	January 25, 2012
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program