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ATP-dependent zinc metalloprotease FtsH (EC 3.4.24.-) (Cell division protease FtsH)

 FTSH_ECOLI              Reviewed;         644 AA.
P0AAI3; P28691; Q2M934;
11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
11-OCT-2005, sequence version 1.
25-OCT-2017, entry version 109.
RecName: Full=ATP-dependent zinc metalloprotease FtsH {ECO:0000255|HAMAP-Rule:MF_01458};
EC=3.4.24.- {ECO:0000255|HAMAP-Rule:MF_01458};
AltName: Full=Cell division protease FtsH;
Name=ftsH {ECO:0000255|HAMAP-Rule:MF_01458};
Synonyms=hflB, mrsC, std, tolZ; OrderedLocusNames=b3178, JW3145;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF GLU-463 AND
HIS-536.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=8444796; DOI=10.1128/jb.175.5.1344-1351.1993;
Tomoyasu T., Yuki T., Morimura S., Mori H., Yamanaka K., Niki H.,
Hiraga S., Ogura T.;
"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.";
J. Bacteriol. 175:1344-1351(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
Wang R., Kushner S.R.;
"Identification and physical analysis of new genes in the argG region
(69 min) of Escherichia coli chromosome.";
Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
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.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
SUBCELLULAR LOCATION, AND TOPOLOGY.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=8444797; DOI=10.1128/jb.175.5.1352-1357.1993;
Tomoyasu T., Yamanaka K., Murata K., Suzaki T., Bouloc P., Kato A.,
Niki H., Hiraga S., Ogura T.;
"Topology and subcellular localization of FtsH protein in Escherichia
coli.";
J. Bacteriol. 175:1352-1357(1993).
[6]
DISCUSSION OF SEQUENCE.
PubMed=1925026; DOI=10.1016/0923-2508(91)90041-8;
Ogura T., Tomoyasu T., Yuki T., Morimura S., Begg K.J., Donachie W.D.,
Mori H., Niki H., Hiraga S.;
"Structure and function of the ftsH gene in Escherichia coli.";
Res. Microbiol. 142:279-282(1991).
[7]
IDENTIFICATION OF HFLB AS FTSH.
PubMed=8248182; DOI=10.1073/pnas.90.22.10861;
Herman C., Ogura T., Tomoyasu T., Hiraga S., Akiyama Y., Ito K.,
Thomas R., D'Ari R., Bouloc P.;
"Cell growth and lambda phage development controlled by the same
essential Escherichia coli gene, ftsH/hflB.";
Proc. Natl. Acad. Sci. U.S.A. 90:10861-10865(1993).
[8]
CHARACTERIZATION.
PubMed=8106505;
Akiyama Y., Shirai Y., Ito K.;
"Involvement of FtsH in protein assembly into and through the
membrane. II. Dominant mutations affecting FtsH functions.";
J. Biol. Chem. 269:5225-5229(1994).
[9]
FUNCTION, AND SIGMA-32 AS SUBSTRATE.
PubMed=7781608;
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.;
"Escherichia coli FtsH is a membrane-bound, ATP-dependent protease
which degrades the heat-shock transcription factor sigma 32.";
EMBO J. 14:2551-2560(1995).
[10]
FUNCTION, AND SECY AS SUBSTRATE.
PubMed=7753838; DOI=10.1073/pnas.92.10.4532;
Kihara A., Akiyama Y., Ito K.;
"FtsH is required for proteolytic elimination of uncomplexed forms of
SecY, an essential protein translocase subunit.";
Proc. Natl. Acad. Sci. U.S.A. 92:4532-4536(1995).
[11]
INTERACTION WITH HFLC AND HFLK, AND SUBCELLULAR LOCATION.
STRAIN=K12 / CSH26 / AD16;
PubMed=8947034;
Kihara A., Akiyama Y., Ito K.;
"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. 15:6122-6131(1996).
[12]
ENZYME REGULATION (MICROBIAL INFECTION), AND INTERACTION WITH HFLKC.
STRAIN=K12 / CSH26 / AD16;
PubMed=9159109; DOI=10.1073/pnas.94.11.5544;
Kihara A., Akiyama Y., Ito K.;
"Host regulation of lysogenic decision in bacteriophage lambda:
transmembrane modulation of FtsH (HflB), the cII degrading protease,
by HflKC (HflA).";
Proc. Natl. Acad. Sci. U.S.A. 94:5544-5549(1997).
[13]
CHARACTERIZATION.
PubMed=9573051; DOI=10.1101/gad.12.9.1348;
Herman C., Thevenet D., Bouloc P., Walker G.C., D'Ari R.;
"Degradation of carboxy-terminal-tagged cytoplasmic proteins by the
Escherichia coli protease HflB (FtsH).";
Genes Dev. 12:1348-1355(1998).
[14]
MEMBRANE SUBSTRATES, AND INTERACTION WITH YCCA.
STRAIN=K12 / CSH26 / AD16;
PubMed=9636708; DOI=10.1006/jmbi.1998.1781;
Kihara A., Akiyama Y., Ito K.;
"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.";
J. Mol. Biol. 279:175-188(1998).
[15]
MECHANISM OF MEMBRANE SUBSTRATE RECOGNITION.
STRAIN=K12 / CSH26 / AD16;
PubMed=10357810; DOI=10.1093/emboj/18.11.2970;
Kihara A., Akiyama Y., Ito K.;
"Dislocation of membrane proteins in FtsH-mediated proteolysis.";
EMBO J. 18:2970-2981(1999).
[16]
MUTAGENESIS OF LEU-201; THR-297; ASN-298; ASP-304; LEU-307; ARG-309;
ARG-312; GLU-415 AND HIS-418.
PubMed=10473576; DOI=10.1074/jbc.274.37.26225;
Karata K., Inagawa T., Wilkinson A.J., Tatsuta T., Ogura T.;
"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.";
J. Biol. Chem. 274:26225-26232(1999).
[17]
LPXC AS SUBSTRATE, FUNCTION IN REGULATING LIPOPOLYSACCHARIDE
SYNTHESIS, AND DISRUPTION PHENOTYPE.
STRAIN=K12 / W3110, and W2252;
PubMed=10048027; DOI=10.1046/j.1365-2958.1999.01221.x;
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.;
"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.";
Mol. Microbiol. 31:833-844(1999).
[18]
RECOGNITION OF MEMBRANE SUBSTRATE FROM N-TERMINUS.
PubMed=11256624; DOI=10.1093/embo-reports/kvd005;
Chiba S., Akiyama Y., Mori H., Matsuo E., Ito K.;
"Length recognition at the N-terminal tail for the initiation of FtsH-
mediated proteolysis.";
EMBO Rep. 1:47-52(2000).
[19]
ZINC-BINDING, AND MUTAGENESIS OF HIS-414; HIS-418; GLU-476 AND
GLU-582.
STRAIN=K12;
PubMed=11827531; DOI=10.1021/bi015748o;
Saikawa N., Ito K., Akiyama Y.;
"Identification of glutamic acid 479 as the gluzincin coordinator of
zinc in FtsH (HflB).";
Biochemistry 41:1861-1868(2002).
[20]
RECOGNITION OF MEMBRANE SUBSTRATE FROM C-TERMINUS.
STRAIN=K12 / JM103;
PubMed=12169602; DOI=10.1128/JB.184.17.4775-4782.2002;
Chiba S., Akiyama Y., Ito K.;
"Membrane protein degradation by FtsH can be initiated from either
end.";
J. Bacteriol. 184:4775-4782(2002).
[21]
REQUIREMENT FOR ATP, AND MUTAGENESIS OF PHE-225 AND GLY-227.
PubMed=14514680; DOI=10.1074/jbc.M308327200;
Yamada-Inagawa T., Okuno T., Karata K., Yamanaka K., Ogura T.;
"Conserved pore residues in the AAA protease FtsH are important for
proteolysis and its coupling to ATP hydrolysis.";
J. Biol. Chem. 278:50182-50187(2003).
[22]
SUBCELLULAR LOCATION.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=15919996; DOI=10.1126/science.1109730;
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
"Global topology analysis of the Escherichia coli inner membrane
proteome.";
Science 308:1321-1323(2005).
[23]
POSSIBLE INTERACTION WITH QMCA.
STRAIN=K12;
PubMed=16573693; DOI=10.1111/j.1365-2958.2006.05104.x;
Chiba S., Ito K., Akiyama Y.;
"The Escherichia coli plasma membrane contains two PHB (prohibitin
homology) domain protein complexes of opposite orientations.";
Mol. Microbiol. 60:448-457(2006).
[24]
INTERACTION WITH YIDC (OXAA).
PubMed=18387365; DOI=10.1016/j.febslet.2008.02.082;
van Bloois E., Dekker H.L., Froderberg L., Houben E.N., Urbanus M.L.,
de Koster C.G., de Gier J.W., Luirink J.;
"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.";
FEBS Lett. 582:1419-1424(2008).
[25]
KDO TRANSFERASE (KDTA) AS SUBSTRATE, AND FUNCTION IN REGULATING
LIPOPOLYSACCHARIDE BIOSYNTHESIS.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=18776015; DOI=10.1128/JB.00871-08;
Katz C., Ron E.Z.;
"Dual role of FtsH in regulating lipopolysaccharide biosynthesis in
Escherichia coli.";
J. Bacteriol. 190:7117-7122(2008).
[26]
PRELIMINARY CRYSTALLIZATION.
PubMed=12037319; DOI=10.1107/S0907444902006972;
Krzywda S., Brzozowski A.M., Karata K., Ogura T., Wilkinson A.J.;
"Crystallization of the AAA domain of the ATP-dependent protease FtsH
of Escherichia coli.";
Acta Crystallogr. D 582:1066-1067(2002).
[27]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 141-395.
PubMed=12176385; DOI=10.1016/S0969-2126(02)00806-7;
Krzywda S., Brzozowski A.M., Verma C., Karata K., Ogura T.,
Wilkinson A.J.;
"The crystal structure of the AAA domain of the ATP-dependent protease
FtsH of Escherichia coli at 1.5 A resolution.";
Structure 10:1073-1083(2002).
[28]
REVIEW.
PubMed=19454621; DOI=10.1093/jb/mvp071;
Akiyama Y.;
"Quality control of cytoplasmic membrane proteins in Escherichia
coli.";
J. Biochem. 146:449-454(2009).
[29]
REVIEW.
PubMed=19744556; DOI=10.1016/j.resmic.2009.08.011;
Narberhaus F., Obrist M., Fuhrer F., Langklotz S.;
"Degradation of cytoplasmic substrates by FtsH, a membrane-anchored
protease with many talents.";
Res. Microbiol. 160:652-659(2009).
-!- 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, F(0) 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.
-!- FUNCTION: 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).
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Note=Binds 1 zinc ion per subunit.;
-!- ENZYME REGULATION: (Microbial infection) 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 at the cytoplasmic side of the membrane.
{ECO:0000269|PubMed:9159109}.
-!- SUBUNIT: 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.
{ECO:0000269|PubMed:18387365, ECO:0000269|PubMed:8947034,
ECO:0000269|PubMed:9159109, ECO:0000269|PubMed:9636708}.
-!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
Rule:MF_01458, ECO:0000269|PubMed:15919996,
ECO:0000269|PubMed:8444797, ECO:0000269|PubMed:8947034}; Multi-
pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01458,
ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:8444797,
ECO:0000269|PubMed:8947034}.
-!- 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. {ECO:0000269|PubMed:10048027}.
-!- 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. {ECO:0000305|PubMed:19744556}.
-!- MISCELLANEOUS: 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.
-!- SIMILARITY: In the central section; belongs to the AAA ATPase
family. {ECO:0000255|HAMAP-Rule:MF_01458}.
-!- SIMILARITY: In the C-terminal section; belongs to the peptidase
M41 family. {ECO:0000255|HAMAP-Rule:MF_01458}.
-!- CAUTION: Glu-476 was identified as the third Zn ligand
(PubMed:11827531), 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. {ECO:0000305|PubMed:11827531}.
-!- SEQUENCE CAUTION:
Sequence=AAA97508.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; M83138; AAA23813.1; -; Genomic_DNA.
EMBL; U01376; AAA97508.1; ALT_INIT; Genomic_DNA.
EMBL; U18997; AAA57979.1; -; Genomic_DNA.
EMBL; U00096; AAC76210.1; -; Genomic_DNA.
EMBL; AP009048; BAE77222.1; -; Genomic_DNA.
PIR; S35109; S35109.
RefSeq; NP_417645.1; NC_000913.3.
RefSeq; WP_001107467.1; NZ_LN832404.1.
PDB; 1LV7; X-ray; 1.50 A; A=141-395.
PDB; 4V0B; X-ray; 2.55 A; A/B/C=25-96.
PDBsum; 1LV7; -.
PDBsum; 4V0B; -.
ProteinModelPortal; P0AAI3; -.
SMR; P0AAI3; -.
BioGrid; 4262980; 336.
DIP; DIP-35828N; -.
IntAct; P0AAI3; 28.
MINT; MINT-1226643; -.
STRING; 316385.ECDH10B_3352; -.
MEROPS; M41.001; -.
PaxDb; P0AAI3; -.
PRIDE; P0AAI3; -.
EnsemblBacteria; AAC76210; AAC76210; b3178.
EnsemblBacteria; BAE77222; BAE77222; BAE77222.
GeneID; 947690; -.
KEGG; ecj:JW3145; -.
KEGG; eco:b3178; -.
PATRIC; fig|511145.12.peg.3271; -.
EchoBASE; EB1469; -.
EcoGene; EG11506; ftsH.
eggNOG; ENOG4105C3H; Bacteria.
eggNOG; COG0465; LUCA.
HOGENOM; HOG000217276; -.
InParanoid; P0AAI3; -.
KO; K03798; -.
PhylomeDB; P0AAI3; -.
BioCyc; EcoCyc:EG11506-MONOMER; -.
BioCyc; MetaCyc:EG11506-MONOMER; -.
BRENDA; 3.4.24.B17; 2026.
BRENDA; 3.4.24.B20; 2026.
SABIO-RK; P0AAI3; -.
EvolutionaryTrace; P0AAI3; -.
PRO; PR:P0AAI3; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0016021; C:integral component of membrane; IDA:EcoliWiki.
GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
GO; GO:0098796; C:membrane protein complex; IPI:EcoCyc.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; ISM:EcoCyc.
GO; GO:0004176; F:ATP-dependent peptidase activity; IDA:EcoCyc.
GO; GO:0016887; F:ATPase activity; IDA:EcoliWiki.
GO; GO:0043273; F:CTPase activity; IDA:EcoliWiki.
GO; GO:0030145; F:manganese ion binding; IDA:EcoliWiki.
GO; GO:0004222; F:metalloendopeptidase activity; IDA:EcoCyc.
GO; GO:0008237; F:metallopeptidase activity; IBA:GO_Central.
GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
GO; GO:0030163; P:protein catabolic process; IBA:GO_Central.
GO; GO:0006508; P:proteolysis; IDA:EcoCyc.
HAMAP; MF_01458; FtsH; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR003959; ATPase_AAA_core.
InterPro; IPR003960; ATPase_AAA_CS.
InterPro; IPR005936; FtsH.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR011546; Pept_M41_FtsH_extracell.
InterPro; IPR000642; Peptidase_M41.
InterPro; IPR037219; Peptidase_M41-like.
Pfam; PF00004; AAA; 1.
Pfam; PF06480; FtsH_ext; 1.
Pfam; PF01434; Peptidase_M41; 1.
SMART; SM00382; AAA; 1.
SUPFAM; SSF140990; SSF140990; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR01241; FtsH_fam; 1.
PROSITE; PS00674; AAA; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Cell inner membrane; Cell membrane;
Complete proteome; Hydrolase; Membrane; Metal-binding;
Metalloprotease; Nucleotide-binding; Protease; Reference proteome;
Transmembrane; Transmembrane helix; Zinc.
CHAIN 1 644 ATP-dependent zinc metalloprotease FtsH.
/FTId=PRO_0000084631.
TOPO_DOM 1 4 Cytoplasmic.
{ECO:0000305|PubMed:8444797}.
TRANSMEM 5 25 Helical. {ECO:0000305}.
TOPO_DOM 26 98 Periplasmic.
{ECO:0000305|PubMed:8444797}.
TRANSMEM 99 119 Helical. {ECO:0000305}.
TOPO_DOM 120 644 Cytoplasmic.
{ECO:0000305|PubMed:8444797}.
NP_BIND 192 199 ATP. {ECO:0000255|HAMAP-Rule:MF_01458}.
ACT_SITE 415 415 {ECO:0000305}.
METAL 414 414 Zinc; catalytic. {ECO:0000305}.
METAL 418 418 Zinc; catalytic. {ECO:0000305}.
METAL 492 492 Zinc; catalytic. {ECO:0000255|HAMAP-
Rule:MF_01458}.
SITE 225 225 Substrate binding. {ECO:0000305}.
MUTAGEN 201 201 L->N: No in vivo protease activity, no in
vitro ATPase activity.
{ECO:0000269|PubMed:10473576}.
MUTAGEN 225 225 F->A,D,E,G,N,Q,R,S,T: Does not complement
ftsH1 at 42 degrees Celsius, no protease
activity in vivo.
{ECO:0000269|PubMed:14514680}.
MUTAGEN 225 225 F->C,H: Partially complements ftsH1 at 42
degrees Celsius, some protease activity
in vivo. {ECO:0000269|PubMed:14514680}.
MUTAGEN 225 225 F->I,L,M,V,W,Y: Complements ftsH1 at 42
degrees Celsius, restores protease
activity in vivo.
{ECO:0000269|PubMed:14514680}.
MUTAGEN 227 227 G->A: Does not complement ftsH1 at 42
degrees Celsius, no protease activity in
vivo. {ECO:0000269|PubMed:14514680}.
MUTAGEN 297 297 T->A: Low protease activity in vivo, low
ATPase activity in vitro, complements
ftsH1 at 42 degrees Celsius.
{ECO:0000269|PubMed:10473576}.
MUTAGEN 298 298 N->A: No in vivo protease activity.
{ECO:0000269|PubMed:10473576}.
MUTAGEN 304 304 D->A,N: No in vivo protease activity, no
in vitro ATPase activity; probably still
binds ATP. {ECO:0000269|PubMed:10473576}.
MUTAGEN 304 304 D->E: Low protease activity in vivo, low
ATPase activity in vitro, complements
ftsH1 at 42 degrees Celsius.
{ECO:0000269|PubMed:10473576}.
MUTAGEN 307 307 L->A: Low protease activity in vivo.
{ECO:0000269|PubMed:10473576}.
MUTAGEN 309 309 R->A,L,K: No in vivo protease activity,
no ATPase activity in vitro; probably
still binds ATP.
{ECO:0000269|PubMed:10473576}.
MUTAGEN 312 312 R->A,L,K: No in vivo protease activity,
no ATPase activity in vitro; probably
still binds ATP.
{ECO:0000269|PubMed:10473576}.
MUTAGEN 414 418 HEAGH->KEAGK: Loss of protease function.
MUTAGEN 414 414 H->Y: Loss of protease function.
{ECO:0000269|PubMed:11827531}.
MUTAGEN 415 415 E->Q: Loss of protease activity in vivo.
{ECO:0000269|PubMed:10473576}.
MUTAGEN 418 418 H->Y: In tolZ21; loss of protease
function in vivo, retains about 25%
ATPase activity, temperature sensitive.
{ECO:0000269|PubMed:10473576,
ECO:0000269|PubMed:11827531}.
MUTAGEN 463 463 E->K: In ftsH1; a temperature-sensitive
mutant which increases the frequency of
lysogenization of phage lambda; when
associated with A-587.
{ECO:0000269|PubMed:8444796}.
MUTAGEN 476 476 E->D,K,V: Severe loss of protease
function that is restored by excess Zn.
{ECO:0000269|PubMed:11827531}.
MUTAGEN 476 476 E->Q: Little effect on protease function.
{ECO:0000269|PubMed:11827531}.
MUTAGEN 536 536 H->R: In hflB29; increases the frequency
of lysogenization of phage lambda.
{ECO:0000269|PubMed:8444796}.
MUTAGEN 582 582 E->D,K,Q: No effect on protease function.
{ECO:0000269|PubMed:11827531}.
MUTAGEN 582 582 E->V: Decreased protease function.
{ECO:0000269|PubMed:11827531}.
HELIX 34 42 {ECO:0000244|PDB:4V0B}.
STRAND 46 52 {ECO:0000244|PDB:4V0B}.
STRAND 55 60 {ECO:0000244|PDB:4V0B}.
STRAND 65 69 {ECO:0000244|PDB:4V0B}.
HELIX 77 83 {ECO:0000244|PDB:4V0B}.
STRAND 87 90 {ECO:0000244|PDB:4V0B}.
STRAND 142 144 {ECO:0000244|PDB:1LV7}.
HELIX 151 153 {ECO:0000244|PDB:1LV7}.
HELIX 158 163 {ECO:0000244|PDB:1LV7}.
HELIX 165 172 {ECO:0000244|PDB:1LV7}.
HELIX 174 176 {ECO:0000244|PDB:1LV7}.
STRAND 187 191 {ECO:0000244|PDB:1LV7}.
HELIX 198 209 {ECO:0000244|PDB:1LV7}.
STRAND 213 216 {ECO:0000244|PDB:1LV7}.
HELIX 230 241 {ECO:0000244|PDB:1LV7}.
STRAND 245 250 {ECO:0000244|PDB:1LV7}.
HELIX 253 256 {ECO:0000244|PDB:1LV7}.
HELIX 270 283 {ECO:0000244|PDB:1LV7}.
STRAND 287 289 {ECO:0000244|PDB:1LV7}.
STRAND 291 298 {ECO:0000244|PDB:1LV7}.
TURN 300 302 {ECO:0000244|PDB:1LV7}.
HELIX 305 308 {ECO:0000244|PDB:1LV7}.
STRAND 315 318 {ECO:0000244|PDB:1LV7}.
HELIX 324 335 {ECO:0000244|PDB:1LV7}.
HELIX 346 351 {ECO:0000244|PDB:1LV7}.
HELIX 358 374 {ECO:0000244|PDB:1LV7}.
STRAND 378 380 {ECO:0000244|PDB:1LV7}.
HELIX 382 392 {ECO:0000244|PDB:1LV7}.
SEQUENCE 644 AA; 70708 MW; E24A753D8F486CA1 CRC64;
MAKNLILWLV IAVVLMSVFQ SFGPSESNGR KVDYSTFLQE VNNDQVREAR INGREINVTK
KDSNRYTTYI PVQDPKLLDN LLTKNVKVVG EPPEEPSLLA SIFISWFPML LLIGVWIFFM
RQMQGGGGKG AMSFGKSKAR MLTEDQIKTT FADVAGCDEA KEEVAELVEY LREPSRFQKL
GGKIPKGVLM VGPPGTGKTL LAKAIAGEAK VPFFTISGSD FVEMFVGVGA SRVRDMFEQA
KKAAPCIIFI DEIDAVGRQR GAGLGGGHDE REQTLNQMLV EMDGFEGNEG IIVIAATNRP
DVLDPALLRP GRFDRQVVVG LPDVRGREQI LKVHMRRVPL APDIDAAIIA RGTPGFSGAD
LANLVNEAAL FAARGNKRVV SMVEFEKAKD KIMMGAERRS MVMTEAQKES TAYHEAGHAI
IGRLVPEHDP VHKVTIIPRG RALGVTFFLP EGDAISASRQ KLESQISTLY GGRLAEEIIY
GPEHVSTGAS NDIKVATNLA RNMVTQWGFS EKLGPLLYAE EEGEVFLGRS VAKAKHMSDE
TARIIDQEVK ALIERNYNRA RQLLTDNMDI LHAMKDALMK YETIDAPQID DLMARRDVRP
PAGWEEPGAS NNSGDNGSPK APRPVDEPRT PNPGNTMSEQ LGDK


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